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https://en.wikipedia.org/wiki/Glutamate%E2%80%94putrescine%20ligase | In enzymology, a glutamate-putrescine ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + putrescine ADP + phosphate + gamma-L-glutamylputrescine
The 3 substrates of this enzyme are ATP, L-glutamate, and putrescine, whereas its 3 products are ADP, phosphate, and gamma-L-glutamylputrescine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is L-glutamate:putrescine ligase (ADP-forming). Other names in common use include gamma-glutamylputrescine synthetase, and YcjK. This enzyme participates in urea cycle and metabolism of amino groups.
References
EC 6.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%E2%80%94tRNA%28Gln%29%20ligase | In enzymology, a glutamate—tRNAGln ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + tRNAGlx AMP + diphosphate + glutamyl-tRNAGlx
The 3 substrates of this enzyme are ATP, L-glutamate, and tRNAGlx, whereas its 3 products are AMP, diphosphate, and glutamyl-tRNAGlx.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamate:tRNAGlx ligase (AMP-forming). This enzyme is also called glutamyl-tRNA synthetase. This enzyme participates in glutamate metabolism.
References
EC 6.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%E2%80%94tRNA%20ligase | In enzymology, a glutamate—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + tRNAGlu AMP + diphosphate + L-glutamyl-tRNAGlu
The 3 substrates of this enzyme are ATP, L-glutamate, and tRNA(Glu), whereas its 3 products are AMP, diphosphate, and L-glutamyl-tRNA(Glu).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamate:tRNAGlu ligase (AMP-forming). Other names in common use include glutamyl-tRNA synthetase, glutamyl-transfer ribonucleate synthetase, glutamyl-transfer RNA synthetase, glutamyl-transfer ribonucleic acid synthetase, glutamate-tRNA synthetase, and glutamic acid translase. This enzyme participates in 3 metabolic pathways: glutamate metabolism, porphyrin and chlorophyll metabolism, and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamine%E2%80%94tRNA%20ligase | In enzymology, a glutamine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamine + tRNAGln AMP + diphosphate + L-glutaminyl-tRNAGln
The 3 substrates of this enzyme are ATP, L-glutamine, and tRNA(Gln), whereas its 3 products are AMP, diphosphate, and L-glutaminyl-tRNA(Gln).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamine:tRNAGln ligase (AMP-forming). Other names in common use include glutaminyl-tRNA synthetase, glutaminyl-transfer RNA synthetase, glutaminyl-transfer ribonucleate synthetase, glutamine-tRNA synthetase, glutamine translase, glutamate-tRNA ligase, glutaminyl ribonucleic acid, and GlnRS. This enzyme participates in glutamate metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutaminyl-tRNA%20synthase%20%28glutamine-hydrolysing%29 | In enzymology, a glutaminyl-tRNA synthase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction
ATP + glutamyl-tRNAGln + L-glutamine ADP + phosphate + glutaminyl-tRNAGln + L-glutamate
The 3 substrates of this enzyme are ATP, glutamyl-tRNA(Gln), and L-glutamine, whereas its 4 products are ADP, phosphate, glutaminyl-tRNA(Gln), and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming). This enzyme participates in glutamate metabolism and alanine and aspartate metabolism.
References
EC 6.3.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutarate%E2%80%94CoA%20ligase | In enzymology, a glutarate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + glutarate + CoA ADP + phosphate + glutaryl-CoA
The 3 substrates of this enzyme are ATP, glutarate, and CoA, whereas its 3 products are ADP, phosphate, and glutaryl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA synthetase, and glutaryl coenzyme A synthetase. This enzyme participates in fatty acid metabolism and lysine degradation.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutathionylspermidine%20synthase | In enzymology, a glutathionylspermidine synthase () is an enzyme that catalyzes the chemical reaction
glutathione + spermidine + ATP glutathionylspermidine + ADP + phosphate
The 3 substrates of this enzyme are glutathione, spermidine, and ATP, whereas its 3 products are glutathionylspermidine, ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule]. This enzyme is also called glutathione:spermidine ligase (ADP-forming). This enzyme participates in glutathione metabolism. It employs one cofactor, magnesium.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 6.3.1
Magnesium enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycine%E2%80%94tRNA%20ligase | Glycine—tRNA ligase also known as glycyl–tRNA synthetase is an enzyme that in humans is encoded by the GARS1 gene.
Function
This gene encodes glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. The encoded enzyme is an (alpha)2 dimer which belongs to the class II family of tRNA synthetases.
Reaction
In enzymology, a glycine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + glycine + tRNAGly AMP + diphosphate + glycyl-tRNAGly
The 3 substrates of this enzyme are ATP, glycine, and tRNA(Gly), whereas its 3 products are AMP, diphosphate, and glycyl-tRNA(Gly).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is glycine:tRNAGly ligase (AMP-forming). Other names in common use include glycyl-tRNA synthetase, glycyl-transfer ribonucleate synthetase, glycyl-transfer RNA synthetase, glycyl-transfer ribonucleic acid synthetase, and glycyl translase. This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.
Interactions
Glycyl-tRNA synthetase has been shown to interact with EEF1D. Mutant forms of the protein associated with peripheral nerve disease have been shown to aberrantly bind to the transmembrane receptor proteins neuropilin 1 and Trk receptors A-C.
Clinical relevance
Glycyl-tRNA synthetase has been shown to be a tar |
https://en.wikipedia.org/wiki/Histidine%E2%80%94tRNA%20ligase | In enzymology, a histidine-tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-histidine + tRNAHis AMP + diphosphate + L-histidyl-tRNAHis
The 3 substrates of this enzyme are ATP, L-histidine, and tRNA(His), whereas its 3 products are AMP, diphosphate, and L-histidyl-tRNA(His).
This enzyme participates in histidine metabolism and aminoacyl-trna biosynthesis.
Nomenclature
Histidine—tRNA ligase belongs to the family of ligase enzymes, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-histidine:tRNAHis ligase (AMP-forming). Other names in common use include histidyl-tRNA synthetase, histidyl-transfer ribonucleate synthetase, and histidine translase.
See also
Anti-Jo1
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Homoglutathione%20synthase | In enzymology, a homoglutathione synthase () is an enzyme that catalyzes the chemical reaction
ATP + γ-L-glutamyl-L-cysteine + β-alanine ADP + phosphate + γ-Lglutamyl-L-cysteinyl-β-alanine
The 3 substrates of this enzyme are ATP, gamma-L-glutamyl-L-cysteine, and beta-alanine, whereas its 3 products are ADP, phosphate, and gamma-L-glutamyl-L-cysteinyl-beta-alanine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteine:beta-alanine ligase (ADP-forming). Other names in common use include homoglutathione synthetase, and beta-alanine specific hGSH synthetase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydrogenobyrinic%20acid%20a%2Cc-diamide%20synthase%20%28glutamine-hydrolysing%29 | In enzymology, a hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction
2 ATP + hydrogenobyrinic acid + 2 L-glutamine + 2 H2O 2 ADP + 2 phosphate + hydrogenobyrinic acid a,c-diamide + 2 L-glutamate
The four substrates of this enzyme are ATP, hydrogenobyrinic acid, L-glutamine, and H2O; its four products are ADP, phosphate, hydrogenobyrinic acid a,c-diamide, and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is hydrogenobyrinic-acid:L-glutamine amido-ligase (AMP-forming). This enzyme is also called CobB and is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
References
EC 6.3.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Imidazoleacetate%E2%80%94phosphoribosyldiphosphate%20ligase | In enzymology, an imidazoleacetate—phosphoribosyldiphosphate ligase () is an enzyme that catalyzes a chemical reaction
ATP + imidazole-4-acetate + 5-phosphoribosyl diphosphate ADP + phosphate + 1-(5-phosphoribosyl)imidazole-4-acetate + diphosphate
The 3 substrates of this enzyme are ATP, imidazole-4-acetate, and 5-phosphoribosyl diphosphate, whereas its 4 products are ADP, phosphate, 1-(5-phosphoribosyl)imidazole-4-acetate, and diphosphate.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is imidazoleacetate:5-phosphoribosyl-diphosphate ligase (ADP- and diphosphate-forming). This enzyme is also called 5-phosphoribosylimidazoleacetate synthetase. This enzyme participates in histidine metabolism.
References
EC 6.3.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indoleacetate%E2%80%94lysine%20synthetase | In enzymology, an indoleacetate—lysine synthetase () is an enzyme that catalyzes the chemical reaction
ATP + (indol-3-yl)acetate + L-lysine ADP + phosphate + N6-[(indol-3-yl)acetyl]-L-lysine
The 3 substrates of this enzyme are ATP, (indol-3-yl)acetate, and L-lysine, whereas its 3 products are ADP, phosphate, and [[N6-[(indol-3-yl)acetyl]-L-lysine]].
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is (indol-3-yl)acetate:L-lysine ligase (ADP-forming). This enzyme is also called indoleacetate:L-lysine ligase (ADP-forming).
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoleucine%E2%80%94tRNA%20ligase | In enzymology, an isoleucine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-isoleucine + tRNAIle AMP + diphosphate + L-isoleucyl-tRNAIle
The 3 substrates of this enzyme are ATP, L-isoleucine, and tRNA(Ile), whereas its 3 products are AMP, diphosphate, and L-isoleucyl-tRNA(Ile).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-isoleucine:tRNAIle ligase (AMP-forming). Other names in common use include isoleucyl-tRNA synthetase, isoleucyl-transfer ribonucleate synthetase, isoleucyl-transfer RNA synthetase, isoleucine-transfer RNA ligase, isoleucine-tRNA synthetase, and isoleucine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-amino-acid%20alpha-ligase | In enzymology, an L-amino-acid alpha-ligase () is an enzyme that catalyzes the chemical reaction
ATP + an L-amino acid + an L-amino acid ADP + phosphate + L-aminoacyl-L-amino acid
Thus, the two substrates of this enzyme are ATP and L-amino acid, whereas its 3 products are ADP, phosphate, and L-aminoacyl-L-amino acid.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-amino acid:L-amino acid ligase (ADP-forming). Other names in common use include L-amino acid alpha-ligase, bacilysin synthetase, YwfE, and L-amino acid ligase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leucine%E2%80%94tRNA%20ligase | In enzymology, a leucine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-leucine + tRNALeu AMP + diphosphate + L-leucyl-tRNALeu
The 3 substrates of this enzyme are ATP, L-leucine, and tRNA(Leu), whereas its 3 products are AMP, diphosphate, and L-leucyl-tRNA(Leu).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-leucine:tRNALeu ligase (AMP-forming). Other names in common use include leucyl-tRNA synthetase, leucyl-transfer ribonucleate synthetase, leucyl-transfer RNA synthetase, leucyl-transfer ribonucleic acid synthetase, leucine-tRNA synthetase, and leucine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
See also
Leucyl-tRNA synthetase
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Long-chain-fatty-acid%E2%80%94%28acyl-carrier-protein%29%20ligase | In enzymology, a long-chain-fatty-acid—[acyl-carrier-protein] ligase () is an enzyme that catalyzes the chemical reaction
ATP + an acid + [acyl-carrier-protein] AMP + diphosphate + acyl-[acyl-carrier-protein]
The 3 substrates of this enzyme are ATP, acid, and acyl-carrier-protein, whereas its 3 products are AMP, diphosphate, and [[acyl-[acyl-carrier-protein]]].
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). Other names in common use include acyl-[acyl-carrier-protein] synthetase, acyl-[acyl carrier protein] synthetase, acyl-ACP synthetase, acyl-[acyl-carrier-protein]synthetase, stearoyl-ACP synthetase, and acyl-acyl carrier protein synthetase. This enzyme participates in fatty acid metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Long-chain-fatty-acid%E2%80%94luciferin-component%20ligase | In enzymology, a long-chain-fatty-acid—luciferin-component ligase () is an enzyme that catalyzes the chemical reaction
ATP + an acid + protein AMP + diphosphate + an acyl-protein thioester
The 3 substrates of this enzyme are ATP, acid, and protein, whereas its 3 products are AMP, diphosphate, and acyl-protein thioester.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is long-chain-fatty-acid:protein ligase (AMP-forming). This enzyme is also called acyl-protein synthetase.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GYKI%2052895 | GYKI 52895 is a drug which is a 2,3-benzodiazepine derivative that also shares the 3,4-methylenedioxyamphetamine pharmacophore. Unlike other similar drugs, GYKI 52895 is a selective dopamine reuptake inhibitor (DARI), which appears to have an atypical mode of action compared to other DARIs. Its DRI activity is shared by numerous addictive drugs including amphetamine and its derivatives (e.g. dextromethamphetamine), cocaine, and methylphenidate and its derivatives (e.g. ethylphenidate). However, dopaminergic drugs are also prone to producing emetic effects such as in the case of apomorphine.
Egis Pharmaceuticals began clinical development of the drug in 1997 for major depressive disorder and Parkinson's disease, but it was discontinued in 2001.
See also
GYKI 52466, another 2,3-benzodiazepine with other than GABAergic function
Tifluadom
Lufuradom
Benzodiazepine
Substituted methylenedioxyphenethylamine
References
Dopamine reuptake inhibitors
Anilines
Benzodiazepines
Benzodioxoles
Abandoned drugs |
https://en.wikipedia.org/wiki/Lysine%E2%80%94tRNA%20ligase | In enzymology, a lysine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-lysine + tRNALys AMP + diphosphate + L-lysyl-tRNALys
The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys).
This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).
Nomenclature
This enzyme belongs to the family of ligases, to be specific, those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-lysine:tRNALys ligase (AMP-forming). Other names in common use include lysyl-tRNA synthetase, lysyl-transfer ribonucleate synthetase, lysyl-transfer RNA synthetase, L-lysine-transfer RNA ligase, lysine-tRNA synthetase, and lysine translase.
References
Further reading
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Lysine%E2%80%94tRNA%28Pyl%29%20ligase | In enzymology, a lysine-tRNAPyl ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-lysine + tRNAPyl AMP + diphosphate + L-lysyl-tRNAPyl
The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Pyl), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Pyl).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-lysine:tRNAPyl ligase (AMP-forming).
References
EC 6.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Magnesium%20chelatase | Magnesium-chelatase is a three-component enzyme () that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of chlorophyll and bacteriochlorophyll. As a result, it is thought that Mg-chelatase has an important role in channeling intermediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth:
protoporphyrin IX + + ATP + ADP + phosphate + Mg-protoporphyrin IX + 2
The four substrates of this enzyme are ATP, protoporphyrin IX, Mg2+, and H2O; its four products are ADP, phosphate, Mg-protoporphyrin IX, and H+.
This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is Mg-protoporphyrin IX magnesium-lyase. Other names in common use include protoporphyrin IX magnesium-chelatase, protoporphyrin IX Mg-chelatase, magnesium-protoporphyrin IX chelatase, magnesium-protoporphyrin chelatase, magnesium-chelatase, Mg-chelatase, and Mg-protoporphyrin IX magnesio-lyase. This enzyme is part of the biosynthetic pathway to chlorophylls.
See also
Biosynthesis of chlorophylls
References
EC 6.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malate%E2%80%94CoA%20ligase | In enzymology, a malate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + malate + CoA ADP + phosphate + malyl-CoA
The 3 substrates of this enzyme are ATP, malate, and CoA, whereas its 3 products are ADP, phosphate, and malyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is malate:CoA ligase (ADP-forming). Other names in common use include malyl-CoA synthetase, malyl coenzyme A synthetase, and malate thiokinase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methionine%E2%80%94tRNA%20ligase | In enzymology, a methionine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-methionine + tRNAMet AMP + diphosphate + L-methionyl-tRNAMet
The 3 substrates of this enzyme are ATP, L-methionine, and tRNA(Met), whereas its 3 products are AMP, diphosphate, and L-methionyl-tRNA(Met).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-methionine:tRNAMet ligase (AMP-forming). Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ribonucleate synthetase, methionyl-transfer RNA synthetase, methionine translase, and MetRS. This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna biosynthesis.
Role in oxidative stress
During oxidative stress, methionine—tRNA ligase might be phosphorylated, which results in promiscuity of this enzyme, where it aminoacylates methionine to various non-Met tRNAs. This in turn leads to substitution of amino acids in proteins with methionine, which helps relieve oxidative stress in the cell.
Structural studies
As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , and .
References
Further reading
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/ACV%20synthetase | ACV synthetase (ACVS, L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase, N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase, ) is an enzyme that catalyzes the chemical reaction
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O 3 AMP + 3 PPi + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
The five substrates of this enzyme are ATP, L-2-aminohexanedioate, L-cysteine, L-valine, and H2O, whereas its three products are AMP, diphosphate, and N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine.
ACVS is an example of a nonribosomal peptide synthetase (NRPS). It participates in penicillin and cephalosporin biosyntheses.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/NAD%2B%20synthase | In enzymology, a NAD+ synthase () is an enzyme that catalyzes the chemical reaction
ATP + deamido-NAD+ + NH3 AMP + diphosphate + NAD+
The 3 substrates of this enzyme are ATP, deamido-NAD+, and NH3, whereas its 3 products are AMP, diphosphate, and NAD+.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is deamido-NAD+:ammonia ligase (AMP-forming). Other names in common use include NAD+ synthetase, NAD+ synthase, nicotinamide adenine dinucleotide synthetase, and diphosphopyridine nucleotide synthetase. This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 6.3.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/NAD%2B%20synthase%20%28glutamine-hydrolysing%29 | In enzymology, a NAD+ synthase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction
ATP + deamido-NAD+ + L-glutamine + H2O AMP + diphosphate + NAD+ + L-glutamate. In eukaryotes, this enzyme contains a glutaminase domain related to nitrilase.
The substrates of this enzyme are ATP, deamido-NAD+, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, NAD+, and glutamate
This enzyme participates in glutamate metabolism and nicotinate and nicotinamide metabolism.
Nomenclature
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is deamido-NAD+:L-glutamine amido-ligase (AMP-forming).
References
EC 6.3.5
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/O-succinylbenzoate%E2%80%94CoA%20ligase | o-Succinylbenzoate—CoA ligase (), encoded from the menE gene in Escherichia coli, catalyzes the fifth reaction in the synthesis of menaquinone (vitamin K2). This pathway is called 1, 4-dihydroxy-2-naphthoate biosynthesis I. Vitamin K is a quinone that serves as an electron transporter during anaerobic respiration. This process of anaerobic respiration allows the bacteria to generate the energy required to survive.
Background
The systematic name for the MenE enzyme is 2-succinylbenzoate: CoA ligase (AMP-forming). Other names for this enzyme include: o-succinylbenzoate-CoA synthase; o-succinylbenzoyl-coenzyme A synthetase; OSB-CoA synthetase; OSB: CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. The EC number is 6.2.1.26. MenE belongs to the ligase enzyme family, or class 6.
In the presence of 0.5mM of Ca(2+), K(+), Na(+), and Zn(2+) the enzyme activity was increased twofold. In the presence of .5 mM of Co(2+) and Mn(2+) the enzyme activity was increased fourfold. Mg(2+) is the ion that increases the enzyme activity the most. With .5 mM of Mg(2+) enzyme activity was increased sixfold. Inhibitors of this enzyme include diethylprocarbonate, Fe(2+), Hg(2+), and Mg(2+) (above 1mM).
The maximum specific enzymatic activity is 3.2 micromol/min/mg. The optimum pH is 7.5. The maximum pH is 8. The optimum temperature is 30 degrees Celsius and the maximum temperature is 40 degrees Celsius. The molecular weight of o-succinylbenzoate CoA ligase is 185000 Da or 185 kDa. This en |
https://en.wikipedia.org/wiki/Oxalate%E2%80%94CoA%20ligase | In enzymology, an oxalate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + oxalate + CoA AMP + diphosphate + oxalyl-CoA
The 3 substrates of this enzyme are ATP, oxalate, and coenzyme A (CoA), whereas its 3 products are AMP, diphosphate, and oxalyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is oxalate:CoA ligase (AMP-forming). Other names in common use include oxalyl-CoA synthetase, and oxalyl coenzyme A synthetase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Organisms with Oxalate-CoA Ligases include:
Arabidopsis thaliana
Saccharomyces cerevisiae
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pantoate%E2%80%94beta-alanine%20ligase | In enzymology, a pantoate—β-alanine ligase () is an enzyme that catalyzes the chemical reaction
ATP + (R)-pantoate + β-alanine AMP + diphosphate + (R)-pantothenate
The 3 substrates of this enzyme are ATP, (R)-pantoate, and beta-alanine, whereas its 3 products are AMP, diphosphate, and (R)-pantothenate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is (R)-pantoate:beta-alanine ligase (AMP-forming). Other names in common use include pantothenate synthetase, pantoate activating enzyme, pantoic-activating enzyme, and D-pantoate:beta-alanine ligase (AMP-forming). This enzyme participates in beta-alanine metabolism and pantothenate and CoA biosynthesis.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .
References
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phenylacetate%E2%80%94CoA%20ligase | In enzymology, a phenylacetate—CoA ligase is an enzyme () that catalyzes the chemical reaction
ATP + phenylacetate + CoA AMP + diphosphate + phenylacetyl-CoA
The 3 substrates of this enzyme are ATP, phenylacetate, and CoA. Its 3 products are AMP, diphosphate, and phenylacetyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is phenylacetate:CoA ligase (AMP-forming). Other names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (AMP-forming). This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylalanine%E2%80%94tRNA%20ligase | In enzymology, a phenylalanine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-phenylalanine + tRNAPhe AMP + diphosphate + L-phenylalanyl-tRNAPhe
The 3 substrates of this enzyme are ATP, L-phenylalanine, and tRNAPhe, whereas its 3 products are AMP, diphosphate, and L-phenylalanyl-tRNAPhe.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-phenylalanine:tRNAPhe ligase (AMP-forming). Other names in common use include phenylalanyl-tRNA synthetase, phenylalanyl-transfer ribonucleate synthetase, phenylalanine-tRNA synthetase, phenylalanyl-transfer RNA synthetase, phenylalanyl-tRNA ligase, phenylalanyl-transfer RNA ligase, L-phenylalanyl-tRNA synthetase, and phenylalanine translase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis.
Phenylalanine-tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it.
Structural studies
As of late 2007, 10 structures have been solved for thi |
https://en.wikipedia.org/wiki/Phosphopantothenate%E2%80%94cysteine%20ligase | In enzymology, a phosphopantothenate—cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme () that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The reaction is:
NTP + (R)-4'-phosphopantothenate + L-cysteine NMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
The nucleoside triphosphate (NTP) involved in the reaction varies from species to species. Phosphopantothenate—cysteine ligase from the bacterium Escherichia coli uses cytidine triphosphate (CTP) as an energy donor, whilst the human isoform uses adenosine triphosphate (ATP).
Nomenclature
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide syntheses). The systematic name of this enzyme class is (R)-4'-phosphopantothenate:L-cysteine ligase. This enzyme is also called phosphopantothenoylcysteine synthetase.
Gene
Phosphopantothenoylcysteine synthetase in humans is encoded by the PPCS gene.
Protein structure
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Phosphopantothenate—cysteine ligase
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoribosylamine%E2%80%94glycine%20ligase | Phosphoribosylamine—glycine ligase, also known as glycinamide ribonucleotide synthetase (GARS), () is an enzyme that catalyzes the chemical reaction
ATP + 5-phospho-D-ribosylamine + glycine ADP + phosphate +
which is the second step in purine biosynthesis.
The 3 substrates of this enzyme are ATP, 5-phospho-D-ribosylamine, and glycine, whereas its 3 products are ADP, phosphate, and .
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds.
In bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). The purD genes often contain PurD RNA motif in their 5' UTR. In yeast, GARS is part of a bifunctional enzyme (encoded by the ADE5/7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS). In higher eukaryotes, including humans, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART.
Nomenclature
The systematic name of this enzyme class is 5-phospho-D-ribosylamine:glycine ligase (ADP-forming). Other names in common use include:
phosphoribosylglycinamide synthetase
glycinamide ribonucleotide synthetase
phosphoribosylglycineamide synthetase
glycineamide ribonucleotide synthetase
2-amino-N-ribosylacetamide 5'-phosphate kinosynthase
5'-phosphoribosylglycinamide synthetase
GAR synthetase
Mechanism
GARS operates via an ordered, sequential mechanism. 5-phospho-D-ribosylamine (PRA) binds first, th |
https://en.wikipedia.org/wiki/Phosphoribosylaminoimidazolesuccinocarboxamide%20synthase | In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase (). It is an enzyme that catalyzes the chemical reaction
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
The 3 substrates of this enzyme are ATP, 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, and L-aspartate, whereas its 3 products are ADP, phosphate, and (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate.
This enzyme belongs to the family of ligases, to be specific those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate ligase (ADP-forming). This enzyme participates in purine metabolism.
This particular protein family is of huge importance as it is found in all three domains of life. It is the seventh step in the pathway of purine biosynthesis. Purines are vital to all cells as they are involved in energy metabolism and DNA synthesis. Furthermore, they are of specific interest to scientific researchers as the study of the purine biosynthesis pathway could lead to the development of chemotherapeutic drugs. This is because most cancers lack a salvage pathway for adenine nuc |
https://en.wikipedia.org/wiki/Phosphoribosylformylglycinamidine%20synthase | In enzymology, a phosphoribosylformylglycinamidine synthase () is an enzyme that catalyzes the chemical reaction
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
The 4 substrates of this enzyme are ATP, N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide, L-glutamine, and H2O, whereas its 4 products are ADP, phosphate, 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine, and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming). Other names in common use include phosphoribosylformylglycinamidine synthetase, formylglycinamide ribonucloetide amidotransferase, phosphoribosylformylglycineamidine synthetase, FGAM synthetase, FGAR amidotransferase, 5'-phosphoribosylformylglycinamide:L-glutamine amido-ligase, (ADP-forming), 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine, and amido-ligase (ADP-forming).
It is known as ADE6 in Saccharomyces cerevisiae (budding yeast) genetics.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
Regulation
This enzyme participates in purine metabolism. Oncogenic and physiological signals lead to the ERK-dependent PF |
https://en.wikipedia.org/wiki/Phytanate%E2%80%94CoA%20ligase | In enzymology, a phytanate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + phytanate + CoA AMP + diphosphate + phytanoyl-CoA
The 3 substrates of this enzyme are ATP, phytanate, and CoA, whereas its 3 products are AMP, diphosphate, and phytanoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is phytanate:CoA ligase (AMP-forming). This enzyme is also called phytanoyl-CoA ligase.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Proline%E2%80%94tRNA%20ligase | In enzymology, a proline—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-proline + tRNAPro AMP + diphosphate + L-prolyl-tRNAPro
The 3 substrates of this enzyme are ATP, L-proline, and tRNA(Pro), whereas its 3 products are AMP, diphosphate, and L-prolyl-tRNA(Pro).
This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.
Nomenclature
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-proline:tRNAPro ligase (AMP-forming). Other names in common use include prolyl-tRNA synthetase, prolyl-transferRNA synthetase, prolyl-transfer ribonucleate synthetase, proline translase, prolyl-transfer ribonucleic acid synthetase, prolyl-s-RNA synthetase, and prolinyl-tRNA ligase.
References
Further reading
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nerisopam | Nerisopam (GYKI-52322, EGIS-6775) is a drug which is a 2,3-benzodiazepine derivative, related to tofisopam. It has potent anxiolytic and neuroleptic effects in animal studies.
See also
Benzodiazepine
References
Benzodiazepines
Phenol ethers |
https://en.wikipedia.org/wiki/Propionate%E2%80%94CoA%20ligase | In enzymology, a propionate—CoA ligase () is an enzyme that catalyzes the chemical reaction
ATP + propanoate + CoA AMP + diphosphate + propanoyl-CoA
The 3 substrates of this enzyme are ATP, propanoate, and CoA, whereas its 3 products are AMP, diphosphate, and propanoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-CoA synthetase. This enzyme participates in propanoate metabolism.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribose-5-phosphate%E2%80%94ammonia%20ligase | In enzymology, a ribose-5-phosphate—ammonia ligase () is an enzyme that catalyzes the chemical reaction
ATP + ribose 5-phosphate + NH3 ADP + phosphate + 5-phosphoribosylamine
The 3 substrates of this enzyme are ATP, ribose 5-phosphate, and NH3, whereas its 3 products are ADP, phosphate, and 5-phosphoribosylamine.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). This enzyme participates in purine metabolism.
References
EC 6.3.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/RNA-3%27-phosphate%20cyclase | In enzymology, a RNA-3′-phosphate cyclase () is an enzyme that catalyzes the chemical reaction
ATP + RNA 3'-terminal-phosphate AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
Thus, the two substrates of this enzyme are ATP and RNA 3'-terminal-phosphate, whereas its 3 products are AMP, diphosphate, and RNA terminal-2',3'-cyclic-phosphate.
This enzyme belongs to the family of ligases, specifically those forming phosphoric-ester bonds. The systematic name of this enzyme class is RNA-3'-phosphate:RNA ligase (cyclizing, AMP-forming). This enzyme is also called RNA cyclase.
Structural studies
As of 2010, three structures have been solved for this class of enzymes, with PDB accession codes and , (un-adenylated) and (adenylated).
References
Further reading
EC 6.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/RNA%20ligase%20%28ATP%29 | In enzymology, an RNA ligase (ATP) () is an enzyme that catalyzes the chemical reaction
ATP + (ribonucleotide)n + (ribonucleotide)m AMP + diphosphate + (ribonucleotide)n+m
The 3 substrates of this enzyme are ATP, (ribonucleotide)n, and (ribonucleotide)m, whereas its 3 products are AMP, diphosphate, and (ribonucleotide)n+m.
This enzyme belongs to the family of ligases, specifically those forming phosphoric-ester bonds. The systematic name of this enzyme class is poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming). Other names in common use include polyribonucleotide synthase (ATP), RNA ligase, polyribonucleotide ligase, and ribonucleic ligase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 6.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Serine%E2%80%94tRNA%20ligase | In enzymology, a serine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-serine + tRNASer AMP + diphosphate + L-seryl-tRNASer
The 3 substrates of this enzyme are ATP, L-serine, and tRNA(Ser), whereas its 3 products are AMP, diphosphate, and L-seryl-tRNA(Ser).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-serine:tRNASer ligase (AMP-forming). Other names in common use include seryl-tRNA synthetase, SerRS, seryl-transfer ribonucleate synthetase, seryl-transfer RNA synthetase, seryl-transfer ribonucleic acid synthetase, and serine translase. This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Succinate%E2%80%94CoA%20ligase%20%28ADP-forming%29 | In enzymology, a succinate-CoA ligase (ADP-forming) () is an enzyme that catalyzes the chemical reaction
ATP + succinate + CoA ADP + phosphate + succinyl-CoA
The 3 substrates of this enzyme are ATP, succinate, and CoA, whereas its 3 products are ADP, phosphate, and succinyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is succinate:CoA ligase (ADP-forming). Other names in common use include succinyl-CoA synthetase (ADP-forming), succinic thiokinase, succinate thiokinase, succinyl-CoA synthetase, succinyl coenzyme A synthetase (adenosine diphosphate-forming), succinyl coenzyme A synthetase, A-STK (adenin nucleotide-linked succinate thiokinase), STK, and A-SCS. This enzyme participates in 4 metabolic pathways: Citric acid cycle, propanoate metabolism, c5-branched dibasic acid metabolism, and reductive carboxylate cycle (CO2 fixation).
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p. 387-399.
EC 6.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Succinate%E2%80%94CoA%20ligase%20%28GDP-forming%29 | In enzymology, a succinate—CoA ligase (GDP-forming) () is an enzyme that catalyzes the chemical reaction
GTP + succinate + CoA GDP + phosphate + succinyl-CoA
The 3 substrates of this enzyme are GTP, succinate, and CoA, whereas its 3 products are GDP, phosphate, and succinyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is succinate:CoA ligase (GDP-forming). Other names in common use include succinyl-CoA synthetase (GDP-forming), succinyl coenzyme A synthetase (guanosine diphosphate-forming), succinate thiokinase, succinic thiokinase, succinyl coenzyme A synthetase, succinate-phosphorylating enzyme, P-enzyme, SCS, G-STK, succinyl coenzyme A synthetase (GDP-forming), succinyl CoA synthetase, and succinyl coenzyme A synthetase. This enzyme participates in the citric acid cycle and propanoate metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p. 387-399.
EC 6.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tetrahydrofolate%20synthase | In enzymology, a tetrahydrofolate synthase () is an enzyme that catalyzes the chemical reaction
ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1
The 3 substrates of this enzyme are ATP, [[tetrahydropteroyl-[gamma-Glu]n]], and L-glutamate, whereas its 3 products are ADP, phosphate, and [[tetrahydropteroyl-[gamma-Glu]n+1]].
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is tetrahydropteroyl-gamma-polyglutamate:L-glutamate gamma-ligase (ADP-forming). This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Threonine%E2%80%94tRNA%20ligase | In enzymology, a threonine-tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-threonine + tRNA(Thr) AMP + diphosphate + L-threonyl-tRNA(Thr)
The three substrates of this enzyme are ATP, L-threonine, and threonine-specific transfer RNA [tRNA(Thr)], whereas its three products are AMP, diphosphate, and L-threonyl-tRNA(Thr).
The systematic name of this enzyme class is L-threonine:tRNAThr ligase (AMP-forming). Other names in common use include threonyl-tRNA synthetase, threonyl-transfer ribonucleate synthetase, threonyl-transfer RNA synthetase, threonyl-transfer ribonucleic acid synthetase, threonyl ribonucleic synthetase, threonine-transfer ribonucleate synthetase, threonine translase, threonyl-tRNA synthetase, and TARS.
Threonine—tRNA ligase (TARS) belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in tRNA and related compounds. More precisely, it belongs to the family of the aminoacyl-tRNA synthetases. These latter enzymes link amino acids to their cognate transfer RNAs (tRNA) in aminoacylation reactions that establish the connection between a specific amino acid and a nucleotide triplet anticodon embedded in the tRNA. During their long evolution, some of these enzymes have acquired additional functions, including roles in RNA splicing, RNA trafficking, transcriptional regulation, translational regulation, and cell signaling.
Structural studies
As of late 2007, 17 structures have been solved for this class of enzymes, |
https://en.wikipedia.org/wiki/Trans-feruloyl-CoA%20synthase | In enzymology, a trans-feruloyl—CoA synthase () is an enzyme that catalyzes the chemical reaction
ferulic acid + CoASH + ATP trans-feruloyl-CoA + products of ATP breakdown
The 3 substrates of this enzyme are ferulic acid, CoASH, and ATP, whereas its two products are trans-feruloyl-CoA and products of ATP breakdown.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is trans-ferulate:CoASH ligase (ATP-hydrolysing). This enzyme is also called trans-feruloyl-CoA synthetase.
References
EC 6.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/PDGFB | Platelet-derived growth factor subunit B is a protein that in humans is encoded by the PDGFB gene.
Function
The protein encoded by this gene is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha (PDGFA) polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds.
Clinical significance
Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 17, at sites where the PDGFB and COL1A1 genes are respectively located or, alternatively, an abnormal small supernumerary ring chromosome merge these two genes to form a COL1A-PDGFB fusion gene. This fusion gene greatly overproduces PDGFB and is considered responsible for causing the development and/or progression of three closely related fibroblastic and myofibroblastic tumors of the skin: giant cell fibroblastoma, dermatofibrosarcoma protuberans, and dermatofibrosarcoma protuberans, sarcomatous.
Two splice variants have been identified for the PDGFB gene.
See also
Platelet-derived growth factor
References
Further reading
Growth factors |
https://en.wikipedia.org/wiki/Trypanothione%20synthase | In enzymology, a trypanothione synthase () is an enzyme that catalyzes the chemical reaction
glutathione + glutathionylspermidine + ATP N1,N8-bis(glutathionyl)spermidine + ADP + phosphate
The 3 substrates of this enzyme are glutathione, glutathionylspermidine, and ATP, whereas its 3 products are N1,N8-bis(glutathionyl)spermidine, ADP, and phosphate.
This reaction is especially important for protozoa in the order kinetoplastida as the molecule of N1,N8-bis(glutathionyl)spermidine, also known as trypanothione, is homologous to the function of glutathione in most other prokaryotic and eukaryotic cells. This means that it is a key intermediate in maintaining thiol redox within the cell and defending against harmful oxidative effects in such protozoa.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is glutathionylspermidine:glutathione ligase (ADP-forming).
Structure
The active bifunctional enzyme of trypanothione synthase is found as a 74.4 KDa monomer consisting of 652 residues with two catalytic domains. Its C-terminal domain is a synthetase and has an ATP-grasp family fold that is usually found in carbon-nitrogen ligases. The N-terminal domain is a cysteine, histidine-dependent aminohydrolase amidase. Structurally the synthetase and amidase domains are bound together by three residues of Glu-650-Asp-651-Glu-652 through hydroge |
https://en.wikipedia.org/wiki/Tryptophan%E2%80%94tRNA%20ligase | In enzymology, a tryptophan-tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-tryptophan + tRNATrp AMP + diphosphate + L-tryptophyl-tRNATrp
The 3 substrates of this enzyme are ATP, L-tryptophan, and tRNA(Trp), whereas its 3 products are AMP, diphosphate, and L-tryptophyl-tRNATrp.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-tryptophan:tRNATrp ligase (AMP-forming). Other names in common use include tryptophanyl-tRNA synthetase, L-tryptophan-tRNATrp ligase (AMP-forming), tryptophanyl-transfer ribonucleate synthetase, tryptophanyl-transfer ribonucleic acid synthetase, tryptophanyl-transfer RNA synthetase, tryptophanyl ribonucleic synthetase, tryptophanyl-transfer ribonucleic synthetase, tryptophanyl-tRNA synthase, tryptophan translase, and TrpRS. This enzyme participates in tryptophan metabolism and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , and .
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tubulin%E2%80%94tyrosine%20ligase | In enzymology, a tubulin—tyrosine ligase () is an enzyme that catalyzes the chemical reaction
ATP + detyrosinated α-tubulin + L-tyrosine α-tubulin + ADP + phosphate
The 3 substrates of this enzyme are ATP, detyrosinated alpha-tubulin, and L-tyrosine, whereas its 3 products are alpha-tubulin, ADP, and phosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is alpha-tubulin:L-tyrosine ligase (ADP-forming).
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tyrosine%E2%80%94arginine%20ligase | In enzymology, a tyrosine—arginine ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-tyrosine + L-arginine AMP + diphosphate + L-tyrosyl-L-arginine
The 3 substrates of this enzyme are ATP, L-tyrosine, and L-arginine, whereas its 3 products are AMP, diphosphate, and L-tyrosyl-L-arginine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-tyrosine:L-arginine ligase (AMP-forming). Other names in common use include tyrosyl-arginine synthase, kyotorphin synthase, kyotorphin-synthesizing enzyme, and kyotorphin synthetase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tyrosine%E2%80%94tRNA%20ligase | Tyrosine—tRNA ligase (), also known as tyrosyl-tRNA synthetase is an enzyme that is encoded by the gene YARS. Tyrosine—tRNA ligase catalyzes the chemical reaction
ATP + L-tyrosine + tRNA(Tyr) AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
The three substrates of this enzyme are ATP, L-tyrosine, and a tyrosine-specific transfer RNA [tRNA(Tyr) or tRNATyr], whereas its three products are AMP, diphosphate, and L-tyrosyl-tRNA(Tyr).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in tRNA and related compounds. More specifically, it belongs to the family of the aminoacyl-tRNA synthetases. These latter enzymes link amino acids to their cognate transfer RNAs (tRNA) in aminoacylation reactions that establish the connection between a specific amino acid and a nucleotide triplet anticodon embedded in the tRNA. Therefore, they are the enzymes that translate the genetic code in vivo. The 20 enzymes, corresponding to the 20 natural amino acids, are divided into two classes of 10 enzymes each. This division is defined by the unique architectures associated with the catalytic domains and by signature sequences specific to each class.
Structural studies
As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes
The tyrosyl-tRNA synthetases (YARS) are either homodimers or monomers with a pseudo-dimeric structure. Each subunit or pseudo-subunit comprises an N-terminal domain which has: (i) about 230 amino aci |
https://en.wikipedia.org/wiki/Ubiquitin%E2%80%94calmodulin%20ligase | In enzymology, an ubiquitin-calmodulin ligase () is an enzyme that catalyzes the chemical reaction
n ATP + calmodulin + n ubiquitin n AMP + n diphosphate + (ubiquitin)n-calmodulin
The 3 substrates of this enzyme are ATP, calmodulin, and ubiquitin, whereas its 3 products are AMP, diphosphate, and (ubiquitin)n-calmodulin.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is calmodulin:ubiquitin ligase (AMP-forming). Other names in common use include ubiquityl-calmodulin synthase, ubiquitin-calmodulin synthetase, ubiquityl-calmodulin synthetase, and uCaM-synthetase.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramate%E2%80%94L-alanine%20ligase | In enzymology, a UDP-N-acetylmuramate—L-alanine ligase () is an enzyme that catalyzes the chemical reaction
ATP + UDP-N-acetylmuramate + L-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramate, and L-alanine, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is UDP-N-acetylmuramate:L-alanine ligase (ADP-forming). Other names in common use include MurC synthetase, UDP-N-acetylmuramoyl-L-alanine synthetase, uridine diphospho-N-acetylmuramoylalanine synthetase, UDP-N-acetylmuramoylalanine synthetase, L-alanine-adding enzyme, UDP-acetylmuramyl-L-alanine synthetase, UDPMurNAc-L-alanine synthetase, L-Ala ligase, uridine diphosphate N-acetylmuramate:L-alanine ligase, uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase, uridine-diphosphate-N-acetylmuramate:L-alanine ligase, UDP-MurNAc:L-alanine ligase, alanine-adding enzyme, and UDP-N-acetylmuramyl:L-alanine ligase. This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
See also
Muramyl ligase
References
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanine%E2%80%94D-glutamate%20ligase | In enzymology, a UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase () is an enzyme that catalyzes the chemical reaction
ATP + UDP-N-acetylmuramoyl-L-alanine + D-glutamate ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanine, and D-glutamate, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanyl-D-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (ADP-forming). Other names in common use include MurD synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase, D-glutamate-adding enzyme, D-glutamate ligase, UDP-Mur-NAC-L-Ala:D-Glu ligase, UDP-N-acetylmuramoyl-L-alanine:glutamate ligase (ADP-forming), and UDP-N-acetylmuramoylalanine-D-glutamate ligase. This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
See also
Muramyl ligase
References
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanyl-D-glutamate%E2%80%94L-lysine%20ligase | In enzymology, a UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase () is an enzyme that catalyzes the chemical reaction
ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate, and L-lysine, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine gamma-ligase (ADP-forming). Other names in common use include MurE synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine, synthetase, and UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase. This enzyme participates in peptidoglycan biosynthesis.
References
EC 6.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-tripeptide%E2%80%94D-alanyl-D-alanine%20ligase | In enzymology, a UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase () is an enzyme that catalyzes the chemical reaction
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- alanine
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine, and D-alanyl-D-alanine, whereas its 4 products are ADP, phosphate, UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-, and alanine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).
Nomenclature
The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine:D-alanyl-D-alanine ligase (ADP-forming). Other names in common use include MurF synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, synthetase, UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine, ligase, uridine diphosphoacetylmuramoylpentapeptide synthetase, UDPacetylmuramoylpentapeptide synthetase, and UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase. This enzyme participates in lysine biosynthesis and peptidoglycan biosynthesis.
References
EC 6.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Urea%20carboxylase | In enzymology, a urea carboxylase () is an enzyme that catalyzes the chemical reaction
ATP + urea + HCO3- ADP + phosphate + urea-1-carboxylate
The 3 substrates of this enzyme are ATP, urea, and HCO3-, whereas its 3 products are ADP, phosphate, and urea-1-carboxylate (allophanate).
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is urea:carbon-dioxide ligase (ADP-forming). This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, biotin.
See also
Allophanate hydrolase
References
EC 6.3.4
Biotin enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Valine%E2%80%94tRNA%20ligase | In enzymology, a valine—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-valine + tRNAVal AMP + diphosphate + L-valyl-tRNAVal
The 3 substrates of this enzyme are ATP, L-valine, and tRNA(Val), whereas its 3 products are AMP, diphosphate, and L-valyl-tRNA(Val).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP-forming). Other names in common use include valyl-tRNA synthetase, valyl-transfer ribonucleate synthetase, valyl-transfer RNA synthetase, valyl-transfer ribonucleic acid synthetase, valine transfer ribonucleate ligase, and valine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
See also
VARS
References
EC 6.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Lehr%20%28glassmaking%29 | In the manufacture of float glass, a lehr oven is a long kiln with an end-to-end temperature gradient, which is used for annealing newly made glass objects that are transported through the temperature gradient either on rollers or on a conveyor belt. The annealing renders glass into a stronger material with fewer internal stresses, and with a lower probability of breaking.
The rapid cooling of molten glass results in an uneven temperature distribution throughout the material. This temperature differential results in mechanical stresses throughout the molten glass, which may be sufficient to cause the material to crack as it cools to ambient temperature or to make it susceptible to cracking during later use, either spontaneously or due to mechanical or thermal shock. To prevent such material weaknesses, objects made from molten glass are annealed by gradual cooling in a lehr oven, from the annealing point, a temperature just below the solidification temperature of the glass. In the process of annealing glass, the temperature is first equalised by holding or "soaking" the glass at the annealing point for a period of time that depends on the maximum thickness of the glass. The glass is then slowly cooled at a rate that depends upon the maximum thickness of the glass, ranging from tens of degrees Celsius per hour (for thin slabs of glass) to fractions of a degree Celsius per hour (for thick slabs of glass).
See also
Annealing (glass)
References
Glass engineering and science
G |
https://en.wikipedia.org/wiki/List%20of%20Grand%20Slam%20boys%27%20doubles%20champions | List of Boys' Doubles Junior Grand Slam tournaments tennis champions:
Champions by year
Statistics
Most Grand Slam doubles titles
Note: when a tie, the person to reach the mark first is listed first.
Career Grand Slam
Players who won all four Grand Slam titles over the course of their careers.
The event at which the Career Grand Slam was completed indicated in bold
Three titles in a single season
Surface Slam
Players who won Grand Slam titles on clay, grass and hard courts in a calendar year.
Channel Slam
Players who won the French Open-Wimbledon double.
Sources
ITF Australian Open
ITF Roland Garros
ITF Wimbledon
ITF US Open
See also
List of Grand Slam boys' singles champions
List of Grand Slam girls' singles champions
List of Grand Slam girls' doubles champions
Tennis statistics
Boys
Grand Slam Men's Singles champions
Grand Slam
Boys |
https://en.wikipedia.org/wiki/Peripheral%20myelin%20protein%2022 | Growth arrest-specific protein 3 (GAS-3), also called peripheral myelin protein 22 (PMP22), is a protein which in humans is encoded by the PMP22 gene.
PMP22 is a 22 kDa transmembrane glycoprotein made up of 160 amino acids, and is mainly expressed in the Schwann cells of the peripheral nervous system. Schwann cells show high expression of PMP22, where it can constitute 2-5% of total protein content in compact myelin. Compact myelin is the bulk of the peripheral neuron's myelin sheath, a protective fatty layer that provides electrical insulation for the neuronal axon. The level of PMP22 expression is relatively low in the central nervous system of adults.
Like other membrane proteins, newly translated PMP22 protein is temporarily sequestered to the endoplasmic reticulum (ER) and Golgi apparatus for post-translational modifications. PMP22 protein is glycosylated with an N terminus-linked sugar and co-localized with the chaperone protein calnexin in the ER. After the protein is transported to the Golgi apparatus it can then become incorporated in the plasma membrane of the cell.
Structure and function
In humans, the PMP22 gene is located on chromosome 17p12 and spans approximately 40kb. The gene contains six exons conserved in both humans and rodents, two of which are 5’ untranslated exons (1a and 1b) and result in two different RNA transcripts with identical coding sequences. The two transcripts differ in their 5' untranslated regions and have their own promoter regulatin |
https://en.wikipedia.org/wiki/MPZ | MPZ or mpz may refer to:
Myelin protein zero, a single membrane glycoprotein which in humans is encoded by the MPZ gene
MPZ, the DS100 code for Penzberg station, Bavaria, Germany
MPZ, the IATA and FAA LID code for Mount Pleasant Municipal Airport (Iowa), Iowa, United States
mpz, the ISO 639-3 code for Mpi language, Thailand |
https://en.wikipedia.org/wiki/PRKCG | Protein kinase C gamma type is an enzyme that in humans is encoded by the PRKCG gene.
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play distinct roles in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase is expressed solely in the brain and spinal cord and its localization is restricted to neurons. It has been demonstrated that several neuronal functions, including long term potentiation (LTP) and long term depression (LTD), specifically require this kinase. Knockout studies in mice also suggest that this kinase may be involved in neuropathic pain development. Defects in this protein have been associated with neurodegenerative disorder spinocerebellar ataxia-14 (SCA14).
Interactions
PRKCG has been shown to interact with GRIA4.
See also
Protein kinase C
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Spinocerebellar Ataxia Type 14
EC 2.7.11 |
https://en.wikipedia.org/wiki/Membrane-bound%20transcription%20factor%20site-1%20protease | Membrane-bound transcription factor site-1 protease, or site-1 protease (S1P) for short, also known as subtilisin/kexin-isozyme 1 (SKI-1), is an enzyme (EC 3.4.21.112) that in humans is encoded by the MBTPS1 gene. S1P cleaves the endoplasmic reticulum loop of sterol regulatory element-binding protein (SREBP) transcription factors.
Function
This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. The encoded protein undergoes an initial autocatalytic processing event in the endoplasmic reticulum (ER) to generate a heterodimer which exits the ER and sorts to the cis/medial-Golgi where a second autocatalytic event takes place and the catalytic activity is acquired. It encodes a type 1 membrane bound protease which is ubiquitously expressed and regulates cholesterol or lipid homeostasis via cleavage of substrates at non-basic residues.
Clinical significance
Mutations in this gene may be associated with lysosomal dysfunction.
See also
Membrane-bound transcription factor site-2 protease
References
External links
EC 3.4.21 |
https://en.wikipedia.org/wiki/Membrane-bound%20transcription%20factor%20site-2%20protease | Membrane-bound transcription factor site-2 protease, also known as S2P endopeptidase or site-2 protease (S2P), is an enzyme () encoded by the gene which liberates the N-terminal fragment of sterol regulatory element-binding protein (SREBP) transcription factors from membranes. S2P cleaves the transmembrane domain of SREPB, making it a member of the class of intramembrane proteases.
S2P catalyses the following chemical reaction
Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP)-1, SREBP-2 and forms of the transcriptional activator ATF6.
This enzyme belongs to the peptidase family M50.
Function
This gene encodes an intramembrane zinc metalloprotease, which is essential in development. This protease functions in the signal protein activation involved in sterol control of transcription and the ER stress response. Mutations in this gene have been associated with ichthyosis follicularis with atrichia and photophobia (IFAP syndrome); IFAP syndrome has been quantitatively linked to a reduction in cholesterol homeostasis and ER stress response.[provided by RefSeq, Aug 2009].
See also
Membrane-bound transcription factor site-1 protease
References
External links
EC 3.4.24 |
https://en.wikipedia.org/wiki/S2P | S2P may refer to:
Biochemistry
Membrane-bound transcription factor peptidase, site 2, an enzyme
Computing
S2P File Format, a Touchstone File format for 2-port S-parameters
, a complexity class expressing "symmetric alternation"
Microsoft Surface Pro 2, a Surface-series Windows 8 tablet
UK Pensions
State Second Pension |
https://en.wikipedia.org/wiki/Dipodinae | Dipodinae is a subfamily of Dipodidae.
Classification
Subfamily Dipodinae
Tribe Dipodini
Genus Dipus
Northern three-toed jerboa, Dipus sagitta
Genus Eremodipus
Lichtenstein's jerboa, Eremodipus lichtensteini
Genus Jaculus
Blanford's jerboa, Jaculus blanfordi
Lesser Egyptian jerboa, Jaculus jaculus
Greater Egyptian jerboa, Jaculus orientalis
Thaler's jerboa, Jaculus thaleri
Genus Stylodipus, three-toed Jerboas
Andrews's three-toed jerboa, Stylodipus andrewsi
Mongolian three-toed jerboa, Stylodipus sungorus
Thick-tailed three-toed jerboa, Stylodipus telum
Tribe Paradipodini
Genus Paradipus
Comb-toed jerboa, Paradipus ctenodactylus
Notes
Dipodidae
Taxa named by Gotthelf Fischer von Waldheim
Mammal subfamilies |
https://en.wikipedia.org/wiki/Rubidium%20silver%20iodide | Rubidium silver iodide is a ternary inorganic compound with the formula RbAg4I5. Its conductivity involves the movement of silver ions within the crystal lattice. It was discovered while searching for chemicals which had the ionic conductivity properties of alpha-phase silver iodide at temperatures below 146 °C for AgI.
RbAg4I5 can be formed by melting together or grinding together stoichiometric quantities of rubidium iodide and silver(I) iodide. The reported conductivity is 25 siemens per metre (that is a 1×1×10 mm bar would have a resistance of 400 ohms along the long axis).
The crystal structure is composed of sets of iodine tetrahedra; they share faces through which the silver ions diffuse.
RbAg4I5 was proposed around 1970 as a solid electrolyte for batteries, and has been used in conjunction with electrodes of silver and of RbI3. Its conductivity does not exhibit substantial variation with changes in relative humidity.
Rubidium silver iodide family is a group of compounds and solid solutions that are isostructural with the RbAg4I5 alpha modification. Examples of such advanced superionic conductors with mobile Ag+ and Cu+ cations include KAg4I5, NH4Ag4I5, K1−xCsxAg4I5, Rb1−xCsxAg4I5, CsAg4Br1−xI2+x, CsAg4ClBr2I2, CsAg4Cl3I2, RbCu4Cl3I2 and KCu4I5.
References
Metal halides
Iodides
Rubidium compounds
Silver compounds
Alkali metal iodides |
https://en.wikipedia.org/wiki/Alpha-2C%20adrenergic%20receptor | The alpha-2C adrenergic receptor (α2C adrenoceptor), also known as ADRA2C, is an alpha-2 adrenergic receptor, and also denotes the human gene encoding it.
Receptor
Alpha-2-adrenergic receptors include 3 highly homologous subtypes: alpha2A, alpha2B, and alpha2C. These receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system. Studies in mice revealed that both the alpha2A and alpha2C subtypes were required for normal presynaptic control of transmitter release from sympathetic nerves in the heart and from central noradrenergic neurons; the alpha2A subtype inhibited transmitter release at high stimulation frequencies, whereas the alpha2C subtype modulated neurotransmission at lower levels of nerve activity.
Gene
This gene encodes the alpha2C subtype, which contains no introns in either its coding or untranslated sequences.
Ligands
Agonists
(R)-3-Nitrobiphenyline (also weak antagonist at α2A and α2B)
Antagonists
BMY 7378 (also α1D antagonist)
JP-1302: selective over α2A, α2B, α2C
N-{2-[4-(2,3-dihydro-benzo[1,4]dioxin-2-ylmethyl)-[1,4]diazepan-1-yl]-ethyl}-2-phenoxy-nicotinamide
Quetiapine
Risperidone
Spiroxatrine
Yohimbine derivatives 9 and 10: >43 fold selectivity over α2A, α2B and α1 subtypes
Brexpiprazole
See also
Adrenergic receptor
References
External links
Further reading
Adrenergic receptors |
https://en.wikipedia.org/wiki/Alpha-2B%20adrenergic%20receptor | The alpha-2B adrenergic receptor (α2B adrenoceptor), is a G-protein coupled receptor. It is a subtype of the adrenergic receptor family. The human gene encoding this receptor has the symbol ADRA2B.
ADRA2B orthologs have been identified in several mammals.
Receptor
α2-adrenergic receptors include 3 highly homologous subtypes: α2A, α2B, and α2C. These receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system.
Clinical significance
This gene encodes the α2B subtype, which was observed to associate with eIF-2B, a guanine nucleotide exchange protein that functions in regulation of translation. A polymorphic variant of the α2B subtype, which lacks 3 glutamic acids from a glutamic acid repeat element, was identified to have decreased G protein-coupled receptor kinase-mediated phosphorylation and desensitization; this polymorphic form is also associated with reduced basal metabolic rate in obese subjects and may therefore contribute to the pathogenesis of obesity. This gene contains no introns in either its coding or untranslated sequences.
A deletion variant of the α2B adrenergic receptor has been shown to be related to emotional memory in Europeans and Africans. This variant also predisposed people who had it to focus more on negative aspects of a situation. This predisposition remained present in people with the variant gene who took a single dose of the noradrenergic antidepressan |
https://en.wikipedia.org/wiki/YWHAB | 14-3-3 protein beta/alpha is a protein that in humans is encoded by the YWHAB gene.
Function
This gene encodes a protein belonging to the 14-3-3 family of proteins, members of which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals. The encoded protein has been shown to interact with RAF1 and CDC25 phosphatases, suggesting that it may play a role in linking mitogenic signaling and the cell cycle machinery. Two transcript variants, which encode the same protein, have been identified for this gene.
Interactions
YWHAB has been shown to interact with:
BRAF,
C-Raf,
CD29,
CDC25A,
CDC25B,
Cbl gene,
EPB41L3,
HDAC4
KCNK3,
MAPK7,
PTPN3,
PRKCZ,
RPS6KA1,
TESK1,
TNFAIP3, and
WEE1.
See also
14-3-3 proteins
References
Further reading
14-3-3 proteins |
https://en.wikipedia.org/wiki/Alpha-2A%20adrenergic%20receptor | The alpha-2A adrenergic receptor (α2A adrenoceptor), also known as ADRA2A, is an α2 adrenergic receptor, and also denotes the human gene encoding it.
Receptor
α2 adrenergic receptors include 3 highly homologous subtypes: α2A, α2B, and α2C. These receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system. Studies in mice revealed that both the α2A and α2C subtypes were required for normal presynaptic control of transmitter release from sympathetic nerves in the heart and from central noradrenergic neurons; the α2A subtype inhibited transmitter release at high stimulation frequencies, whereas the α2C subtype modulated neurotransmission at lower levels of nerve activity
Gene
This gene encodes α2A subtype and it contains no introns in either its coding or untranslated sequences.
Ligands
Agonists
4-NEMD
Brimonidine
Clonidine
Dexmedetomidine
Guanfacine
Lofexidine
Myrcene
Medetomidine
PS75
Tizanidine
Xylazine
Antagonists
Idazoxan
1-PP (active metabolite of buspirone and gepirone)
Asenapine
BRL-44408
Clozapine
Lurasidone
Mianserin
Mirtazapine
Paliperidone
Risperidone
Yohimbine
See also
Adrenergic receptor
References
External links
Further reading
Adrenergic receptors
Biology of attention deficit hyperactivity disorder |
https://en.wikipedia.org/wiki/Alpha-1B%20adrenergic%20receptor | The alpha-1B adrenergic receptor (α1B-adrenoreceptor), also known as ADRA1B, is an alpha-1 adrenergic receptor, and also denotes the human gene encoding it. The crystal structure of the α1B-adrenergic receptor has been determined in complex with the inverse agonist (+)-cyclazosin.
Receptor
There are 3 alpha-1 adrenergic receptor subtypes: alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and different subtypes show different patterns of activation. They activate mitogenic responses and regulate growth and proliferation of many cells.
Gene
This gene encodes alpha-1B-adrenergic receptor, which induces neoplastic transformation when transfected into NIH 3T3 fibroblasts and other cell lines. Thus, this normal cellular gene is identified as a protooncogene. This gene comprises 2 exons and a single large intron of at least 20 kb that interrupts the coding region.
Ligands
Antagonists
L-765,314
Risperidone
Brexpiprazole
Interactions
Alpha-1B adrenergic receptor has been shown to interact with AP2M1. A role in regulation of dopaminergic neurotransmission has also been suggested.
See also
Adrenergic receptor
References
External links
Further reading
Adrenergic receptors |
https://en.wikipedia.org/wiki/Alpha-1D%20adrenergic%20receptor | The alpha-1D adrenergic receptor (α1D adrenoreceptor), also known as ADRA1D, is an alpha-1 adrenergic receptor, and also denotes the human gene encoding it.
Receptor
There are 3 alpha-1 adrenergic receptor subtypes: alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and different subtypes show different patterns of activation. They activate mitogenic responses and regulate growth and proliferation of many cells.
Gene
This gene encodes alpha-1D-adrenergic receptor. Similar to alpha-1B-adrenergic receptor gene, this gene comprises 2 exons and a single intron that interrupts the coding region.
Ligands
Antagonists
A-315456
BMY 7378 (also α2C antagonist)
See also
Adrenergic receptor
References
External links
Further reading
Adrenergic receptors |
https://en.wikipedia.org/wiki/Ubiquitin%20B | Ubiquitin is a protein that in humans is encoded by the UBB gene.
Function
Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for ATP-dependent, non-lysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to histone H2A in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein (UBB+1) has been noticed in patients with Alzheimer's disease, Down syndrome, other tauopathies (e.g. Pick's disease) and polyglutamine disease (e.g. Huntington's disease).
References
Further reading |
https://en.wikipedia.org/wiki/Myotonin-protein%20kinase | Myotonin-protein kinase (MT-PK) also known as myotonic dystrophy protein kinase (MDPK) or dystrophia myotonica protein kinase (DMPK) is an enzyme that in humans is encoded by the DMPK gene.
The dmpk gene product is a Ser/Thr protein kinase homologous to the MRCK p21-activated kinases and Rho kinase family. Data obtained by using antibodies that detect specific isoforms of DMPK indicate that the most abundant isoform of DMPK is an 80-kDa protein expressed almost exclusively in smooth, skeletal, and cardiac muscles. This kinase exists both as a membrane-associated and as a soluble form in human left ventricular samples. The different C termini of DMPK that arise from alternative splicing determine its localization to the endoplasmic reticulum, mitochondria, or cytosol in transfected COS-1 cells. Among the substrates for DMPK proposed by in vitro studies are phospholemman, the dihydropyridine receptor, and the myosin phosphatase targeting subunit. However, an in vivo demonstration of the phosphorylation of these substrates by DMPK remains to be established, and a link between these substrates and the clinical manifestations of myotonic dystrophy (DM) is unclear.
Function
Myotonin-protein kinase is a serine-threonine kinase that is closely related to other kinases that interact with members of the Rho family of small GTPases. Substrates for this enzyme include myogenin, the beta-subunit of the L-type calcium channels, and phospholemman. Although the specific function of this |
https://en.wikipedia.org/wiki/Ommaya%20reservoir | An Ommaya reservoir is an intraventricular catheter system that can be used for the aspiration of cerebrospinal fluid or for the delivery of drugs (e.g. chemotherapy) into the cerebrospinal fluid. It consists of a catheter in one lateral ventricle attached to a reservoir implanted under the scalp. It is used to treat brain tumors, leukemia/lymphoma or leptomeningeal disease by intrathecal drug administration. In the palliative care of terminal cancer, an Ommaya reservoir can be inserted for intracerebroventricular injection (ICV) of morphine.
It was originally invented in 1963 by Ayub K. Ommaya, a Pakistani-American neurosurgeon.
In January 2017, researchers at University of Texas Southwestern Medical Centre used an Ommaya reservoir to measure the intracranial pressure that is regularly observed in astronauts in zero-gravity conditions.
References
Science and technology in Pakistan
Medical equipment
Drug delivery devices
Pakistani inventions
History of science and technology in Pakistan
Neurosurgical procedures |
https://en.wikipedia.org/wiki/Major%20histocompatibility%20complex%2C%20class%20II%2C%20DQ%20alpha%201 | Major histocompatibility complex, class II, DQ alpha 1, also known as HLA-DQA1, is a human gene present on short arm of chromosome 6 (6p21.3) and also denotes the genetic locus which contains this gene. The protein encoded by this gene is one of two proteins that are required to form the DQ heterodimer, a cell surface receptor essential to the function of the immune system.
Function
HLA-DQA1 belongs to the HLA class II alpha chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen-presenting cells (APC: B lymphocytes, dendritic cells, macrophages).
Gene structure and polymorphisms
The alpha chain contains 5 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular protein domains, exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation.
Alleles
DQ1
There are four commonly encountered DQA1 alleles: DQA1*0101, *0102, *0103, *0104. These alleles are always found in haplotypes with HLA-DQB1*05 (DQ5) and HLA-DQB1*06 (DQ6). DQ1 is a serotype, rare among |
https://en.wikipedia.org/wiki/Catecholborane | Catecholborane (abbreviated HBcat) is an organoboron compound that is useful in organic synthesis. This colourless liquid is a derivative of catechol and a borane, having the formula C6H4O2BH.
Synthesis and structure
Traditionally catecholborane is produced by treating catechol with borane (BH3) in a cooled solution of THF. However, this method results in a loss of 2 mole equivalents of the hydride. Nöth and Männig described the reaction of alkali-metal boron hydride (LiBH4, NaBH4, of KBH4) with tris(catecholato)bisborane in an ethereal solvent such as diethyl ether. In 2001, Herbert Brown and coworkers prepared catecholborane by treatment of tri-o-phenylene bis-borate with diborane.
Unlike borane itself or alkylboranes, catechol borane exists as a monomer. This behavior is a consequence of the electronic influence of the aryloxy groups that diminish the Lewis acidity of the boron centre. Pinacolborane adopts a similar structure.
Reactions
Catecholborane is less reactive in hydroborations than borane-THF or borane-dimethylsulfide.
When catecholborane is treated with a terminal alkyne, a trans vinylborane is formed:
C6H4O2BH + HC2R → C6H4O2B-CHCHR
The product is a precursor to the Suzuki reaction and is the only borane which stops at the alkene instead of reacting further to the alkane.
Catecholborane may be used as a stereoselective reducing agent when converting β-hydroxy ketones to syn 1,3-diols.
Catecholborane oxidatively adds to low valent metal complexes, affordi |
https://en.wikipedia.org/wiki/NCK1 | Cytoplasmic protein NCK1 is a protein that in humans is encoded by the NCK1 gene.
Gene
The Nck (non-catalytic region of tyrosine kinase adaptor protein 1) belongs to the adaptor family of proteins. The nck gene was initially isolated from a human melanoma cDNA library using a monoclonal antibody produced against the human melanoma-associated antigen. The Nck family has two known members in human cells (Nck-1/Nckalpha and NcK2/NcKbeta), two in mouse cells (mNckalpha and mNckbeta/Grb4) and one in drosophila (Dock means dreadlocks-ortholog).
The two murine gene products exhibit 68% amino acid identity to one another, with most of the sequence variation being located to the linker regions between the SH3 and SH2 domains, and are 96% identical to their human counterparts. While human nck-1 gene has been localised to the 3q21 locus of chromosome 3, the nck-2 gene can be found on chromosome 2 at the 2q12 locus.
Function
The protein encoded by this gene is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. It is located in the cytoplasm and is an adaptor protein involved in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.
Nck1 has been linked to glucose tolerance and insulin signaling within certain tissues, namely the liver, in obese mice. A deletion of the protein also causes a decrease of ER stress signaling within these obese cells, which is normally increased by the excessi |
https://en.wikipedia.org/wiki/Jim%20Creek%20Naval%20Radio%20Station | Jim Creek Naval Radio Station is a United States Navy very low frequency (VLF) radio transmitter facility at Jim Creek near Oso, Washington. The primary mission of this site is to communicate orders one-way to submarines of the Pacific fleet. Radio waves in the very low frequency band can penetrate seawater and be received by submerged submarines which cannot be reached by radio communications at other frequencies. Established in 1953, the transmitter radiates on 24.8 kHz with a power of 1.2 megawatts and a callsign of NLK, and is one of the most powerful radio transmitters in the world. Located near Arlington, Washington, in the foothills of the Cascades, north of Seattle, the site has .
Antenna
Much of the site is devoted to the enormous overhead wire antenna array that is necessary to efficiently radiate the VLF waves. The antenna, shown above, consists of ten catenary cables, 5,640–8,700 ft (1,719–2,652 m, 1.1–1.6 miles) long, suspended in a zigzag pattern over the valley between Wheeler mountain and Blue mountain on twelve 200 ft. towers on the mountains' crests. Each cable receives energy from a vertical cable attached at the center, which drops down to the valley floor where it is fed by one of two "bus" transmission lines which extend along the valley from the transmitter building in the center.
This type of antenna, called a "valley-span" antenna, functions as a capacitively top-loaded electrically short monopole antenna. The vertical cables are the main radiati |
https://en.wikipedia.org/wiki/Retinoid%20X%20receptor%20gamma | Retinoid X receptor gamma (RXR-gamma), also known as NR2B3 (nuclear receptor subfamily 2, group B, member 3) is a nuclear receptor that in humans is encoded by the RXRG gene.
Function
This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the antiproliferative effects of retinoic acid (RA). This receptor forms heterodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. This gene is expressed at significantly lower levels in non-small cell lung cancer cells. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
See also
Retinoid X receptor
Interactions
Retinoid X receptor gamma has been shown to interact with ITGB3BP.
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/Serum%20response%20factor | Serum response factor, also known as SRF, is a transcription factor protein.
Function
Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).
SRF is important during the development of the embryo, as it has been linked to the formation of mesoderm. In the fully developed mammal, SRF is crucial for the growth of skeletal muscle. Interaction of SRF with other proteins, such as steroid hormone receptors, may contribute to regulation of muscle growth by steroids. Interaction of SRF with other proteins such as myocardin or Elk-1 may enhance or suppress expression of genes important for growth of vascular smooth muscle.
Clinical significance
Lack of skin SRF is associated with psoriasis and other skin diseases.
Interactions
Serum response factor has been shown to interact with:
ASCC3,
ATF6,
CEBPB,
CREB-binding protein,
ELK4,
GATA4,
GTF2F1,
GTF2I,
Myogenin,
NFYA,
Nuclear receptor co-repressor 2,
Promyelocytic leukemia protein and
Src, |
https://en.wikipedia.org/wiki/Dithiete | Dithiete is an unsaturated heterocyclic compound that contains two adjacent sulfur atoms and two sp2-hybridized carbon centers. Derivatives are known collectively as dithietes or 1,2-dithietes. With 6 π electrons, 1,2-dithietes are examples of aromatic organosulfur compounds. A few 1,2-dithietes have been isolated. 3,4-Bis(trifluoromethyl)-1,2-dithiete is a particularly stable example.
Unsubstituted 1,2-dithiete has been generated in thermolytic reactions and was characterized by microwave spectroscopy, ultraviolet photoelectron spectroscopy and infrared spectroscopy in a low temperature matrix. The open ring isomer, dithioglyoxal, HC(S)C(S)H, is less stable than the 1,2-dithiete.
The dithione can be prepared (as trans-dithioglyoxal) by low temperature photolysis of 1,3-dithiol-2-one. Quantum chemical calculations reproduce the observed greater stability of 1,2-dithiete only if large basis-sets with polarization functions are used.
See also
Dithietane - the corresponding saturated ring
Thiete - an analogue with only one sulfur atom
Additional reading
References
Organosulfur compounds
Organic disulfides
Sulfur heterocycles
Four-membered rings |
https://en.wikipedia.org/wiki/Unified%20Power%20Format | Unified Power Format (UPF) is the popular name of the Institute of Electrical and Electronics Engineers (IEEE) standard for specifying power intent in power optimization of electronic design automation. The IEEE 1801-2009 release of the standard was based on a donation from the Accellera organization. The current release is IEEE 1801-2018.
History
A Unified Power Format technical committee was formed by the Accellera organization, chaired by Stephen Bailey of Mentor Graphics.
As a reaction to the Power Forward Initiative the group was proposed in July 2006 and met on September 13, 2006.
It submitted its first draft in January 2007, and a version 1.0 was approved to be published on February 26, 2007.
Joe Daniels was technical editor.
Files written to this standard annotate an electric design with the power and power control intent of that design. Elements of that annotation include:
Power Supplies: supply nets, supply sets, power states
Power Control: power switches
Additional Protection: level shifters and isolation
Memory retention during times of limited power: retention strategies and supply set power states
Refinable descriptions of the potential power applied to the electronic system: power states, transitions, a set of simstate, power/ground pin type (pg_type) and function attributes of nets, and the -update argument to support the progressive refinement of the power intent.
The standard describes extensions to the Tool Command Language (Tcl): commands and argu |
https://en.wikipedia.org/wiki/Retinoid%20X%20receptor%20beta | Retinoid X receptor beta (RXR-beta), also known as NR2B2 (nuclear receptor subfamily 2, group B, member 2) is a nuclear receptor that in humans is encoded by the RXRB gene.
This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the effects of retinoic acid (RA). This receptor forms heterodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. The gene lies within the major histocompatibility complex (MHC) class II region on chromosome 6. An alternatively spliced transcript variant has been described, but its full length sequence has not been determined.
Interactive pathway map
See also
Retinoid X receptor
References
Further reading
Intracellular receptors
Transcription factors |
https://en.wikipedia.org/wiki/EPAS1 | Endothelial PAS domain-containing protein 1 (EPAS1, also known as hypoxia-inducible factor-2alpha (HIF-2α)) is a protein that is encoded by the EPAS1 gene in mammals. It is a type of hypoxia-inducible factor, a group of transcription factors involved in the physiological response to oxygen concentration. The gene is active under hypoxic conditions. It is also important in the development of the heart, and for maintaining the catecholamine balance required for protection of the heart. Mutation often leads to neuroendocrine tumors.
However, several characterized alleles of EPAS1 contribute to high-altitude adaptation in humans. One such allele, which has been inherited from Denisovan archaic hominins, is known to confer increased athletic performance in some people, and has therefore been referred to as the "super athlete gene".
Function
The EPAS1 gene encodes one subunit of a transcription factor involved in the induction of genes regulated by oxygen, and which is induced as oxygen concentration falls (hypoxia). The protein contains a basic helix-loop-helix protein dimerization domain as well as a domain found in signal transduction proteins which respond to oxygen levels. EPAS1 is involved in the development of the embryonic heart and is expressed in endothelial cells that line the walls of blood vessels in the umbilical cord.
EPAS1 is also essential for the maintenance of catecholamine homeostasis and protection against heart failure during early embryonic development. |
https://en.wikipedia.org/wiki/USH1G | Usher syndrome type-1G protein is a protein that in humans is encoded by the USH1G gene.
This gene encodes a protein that contains three ankyrin domains, a class I PDZ-binding motif and a sterile alpha motif. The encoded protein interacts with harmonin, which is associated with Usher syndrome type 1C.
This protein plays a role in the development and maintenance of the auditory and visual systems and functions in the cohesion of hair bundles formed by inner ear sensory cells. Mutations in this gene are associated with Usher syndrome type 1G (USH1G).
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Usher Syndrome Type I |
https://en.wikipedia.org/wiki/HIF3A | Hypoxia-inducible factor 3 alpha is a protein that in humans is encoded by the HIF3A gene.
Function
The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit heterodimeric transcription factors that regulate many adaptive responses to low oxygen tension (hypoxia). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. At least three transcript variants encoding three different isoforms have been found for this gene.
In rats, it plays a negative role in the adaptation to hypoxia, because the inhibition of HIF-3α expression leads to an increase in physical endurance.
Clinical significance
DNA methylation in the introns of HIF3A is associated with BMI an adiposity.
See also
Hypoxia inducible factors
References
Further reading
Transcription factors
PAS-domain-containing proteins |
https://en.wikipedia.org/wiki/Peroxisome%20proliferator-activated%20receptor%20delta | Peroxisome proliferator-activated receptor delta (PPAR-delta), or (PPAR-beta), also known as Nuclear hormone receptor 1 (NUC1) is a nuclear receptor that in humans is encoded by the PPARD gene.
This gene encodes a member of the peroxisome proliferator-activated receptor (PPAR) family. It was first identified in Xenopus in 1993.
Function
PPAR-delta is a nuclear hormone receptor that governs a variety of biological processes and may be involved in the development of several chronic diseases, including diabetes, obesity, atherosclerosis, and cancer.
In muscle PPARD expression is increased by exercise, resulting in increased oxidative (fat-burning) capacity and an increase in type I fibers. Both PPAR-delta and AMPK agonists are regarded as exercise mimetics. In adipose tissue PPAR-β/δ increases both oxidation as well as uncoupling of oxidative phosphorylation.
PPAR-delta may function as an integrator of transcription repression and nuclear receptor signaling. It activates transcription of a variety of target genes by binding to specific DNA elements. Well described target genes of PPARδ include PDK4, ANGPTL4, PLIN2, and CD36. The expression of this gene is found to be elevated in colorectal cancer cells. The elevated expression can be repressed by adenomatosis polyposis coli (APC), a tumor suppressor protein involved in the APC/beta-catenin signaling pathway. Knockout studies in mice suggested the role of this protein in myelination of the corpus callosum, epidermal cell prol |
https://en.wikipedia.org/wiki/Netherlands%20Institute%20for%20the%20Classification%20of%20Audiovisual%20Media | Netherlands Institute for the Classification of Audiovisual Media (Nederlands Instituut voor de Classificatie van Audiovisuele Media) is the institute responsible for the content given for review for the Dutch motion picture rating system, Kijkwijzer, and the software given for review for the European video game content rating system PEGI.
History
The first call for regulation within the audiovisual world came from the government at the end of the 1980s, to protect younger audience from possible bad influences. With an explosive growth of audiovisual media, the European Commission called for action, which resulted in the "not for all ages"-governmentnote in 1997. This note pleaded for an independent institute, which would have to serve as a guiding institute for selfregulating within the audiovisual branch.
In 1999 the Nederlands Instituut voor de Classificatie van Audiovisuele Media was founded, in close cooperation with the ministries of Education, Culture & Science (OCW), Public health, Wellbeing and Sport (VWS) and Justice. NICAM began with an initiating and coordinating role in the founding of Kijkwijzer, which was officially accepted by the government in 2000, and became a law on February 22, 2001.
In April 2003, the NICAM was given the task of evaluating computer- and videogame software for the newly founded Pan European Game Information. The British Video Standards Council acts as an agent in the United Kingdom for NICAM due to "high concentration of videogame publ |
https://en.wikipedia.org/wiki/Political%20methodology | Political methodology is a subfield of political science that studies the quantitative and qualitative methods used to study politics. Quantitative methods combine statistics, mathematics, and formal theory. Political methodology is often used for positive research, in contrast to normative research. Psephology, a skill or technique within political methodology, is the "quantitative analysis of elections and balloting".
Journals
Political methodology is often published in the "top 3" journals (American Political Science Review, American Journal of Political Science, and Journal of Politics), in sub-field journals, and in methods-focused journals.
Political Analysis
Political Science Research and Methods
Notable researchers
Gary King
Rob Franzese
Jeff Gill
Phil Schrodt
Jan Box-Steffensmeier
Simon Jackman
Jonathan Nagler
Jim Stimson
Larry Bartels
Donald Green
References
External links
The Society for Political Methodology's homepage
US News Rankings for Political Methodology
Political science |
https://en.wikipedia.org/wiki/Tin%20cry | Tin cry is the characteristic sound heard when a bar made of tin is bent. Variously described as a "screaming" or "crackling" sound, the effect is caused by the crystal twinning in the metal. The sound is not particularly loud, despite terms like "crying" and "screaming". It is very noticeable when a hot-dip tin coated sheet metal is bent at high speed over rollers during processing.
Tin cry is often demonstrated using a simple science experiment. A bar of tin will "cry" repeatedly when bent until it breaks. The experiment can then be recycled by melting and recrystallizing the metal. The low melting point of tin - makes re-casting easy. Tin anneals at reasonably-low temperature as well, normalizing tin's microstructure of crystallites/grains.
Although the cry is most typical of tin, a similar effect occurs in other metals, such as niobium, indium, zinc, cadmium, gallium, and solid mercury.
References
External links
Tin cry on YouTube
Mercury cry on YouTube
Tin
Materials degradation
Fracture mechanics |
https://en.wikipedia.org/wiki/Kininogen%201 | Kininogen-1 (KNG1), also known as alpha-2-thiol proteinase inhibitor, Williams-Fitzgerald-Flaujeac factor or the HMWK-kallikrein factor is a protein that in humans is encoded by the KNG1 gene. Kininogen-1 is the precursor protein to high-molecular-weight kininogen (HMWK), low-molecular-weight kininogen (LMWK), and bradykinin.
Expression
The KNG1 gene uses alternative splicing to generate two different proteins: high-molecular-weight kininogen (HMWK) and low-molecular-weight kininogen (LMWK). HMWK in turn is cleaved by the enzyme kallikrein to produce bradykinin.
KNG1 gene → low-molecular-weight kininogen (LMWK) protein (contains 427 amino acids) or high-molecular-weight kininogen (HMWK) protein (644 amino acids)
HMWK protein → bradykinin peptide (9 amino acids)
Function
HMWK is essential for blood coagulation and assembly of the kallikrein-kinin system. Also, bradykinin, a peptide causing numerous physiological effects, is released from HMWK. In contrast to HMWK, LMWK is not involved in blood coagulation.
Kininogen-1 is a constituent of the blood coagulation system as well as the kinin-kallikrein system.
See also
high-molecular-weight kininogen
low-molecular-weight kininogen
bradykinin
References
Further reading
External links
LMWK laboratory information
Coagulation system
Kinin–kallikrein system
Cofactors |
https://en.wikipedia.org/wiki/George%20E.%20Kimball | George Elbert Kimball (July 12, 1906 – December 6, 1967) was an American professor of quantum chemistry, and a pioneer of operations research algorithms during World War II.
Early life
George E. Kimball was born to Arthur G. Kimball in Chicago in 1906 and he grew up in New Britain, Connecticut. He was the oldest of three children in a middle-class family; his younger brother, Penn Kimball, also became a professor at Columbia, in journalism. His interest in chemistry was due to his high school chemistry teacher. He attended New Britain High School and graduated in 1923. He spent a year at Phillips Exeter Academy and in 1924 he enrolled at Princeton University. Apparently his father was of the opinion that there were already too many graduates of Yale University in Connecticut. Kimball later claimed that he chose the chemistry program at Princeton because it allowed him to study not only chemistry, but also an equal amount of physics and mathematics, which were also of interest to him. Kimball received his bachelor's degree in 1928, and at that time his main interest was quantum chemistry, which at that time was a field that was still in its infancy, following significant theoretical breakthroughs in quantum mechanics in 1925.
He returned to Princeton's chemistry department to be a graduate student on a graduate fellowship and worked under Hugh Taylor. Kimball's doctoral thesis was on quantum mechanics of the recombination of hydrogen atoms, and he received his Ph.D. in 1932 |
https://en.wikipedia.org/wiki/Receptor%20for%20activated%20C%20kinase%201 | Receptor for activated C kinase 1 (RACK1), also known as guanine nucleotide-binding protein subunit beta-2-like 1 (GNB2L1), is a 35 kDa protein that in humans is encoded by the RACK1 gene.
Function
RACK1 was originally isolated and identified as an intracellular protein receptor for protein kinase C, noting the significant homology to the beta subunit of heterotrimeric G proteins. Later studies established RACK1, and its yeast homolog Asc1, as a core ribosomal protein of the eukaryotic small (40S) ribosomal subunit. Much of the function of Asc1/RACK1 appears to result from its position on the 'head' of the 40S ribosomal subunit. Asc1/RACK1 participates in several aspects of eukaryotic translation and ribosome quality control, including IRES-mediated translation, non-stop decay, non-functional 18S ribosomal RNA decay, and frameshifting.
Interactions
RACK1 is positioned at the solvent-exposed surface of the 40S ribosomal subunit, where it is held in place through contacts with both the 18S rRNA and other ribosomal proteins, including uS3, uS9, and eS17. Additionally, RACK1 has been shown to interact with:
AGTRAP
Androgen receptor,
CD18,
CD29
Cyclin A1
EIF6,
FYN,
IFNAR2,
Janus kinase 1
OTUB1,
P73,
PDE4D,
PRKCB1,
PRKCE,
PTPRM,
RAS p21 protein activator 1,
ST7,
STAT1,
Src, and
Tyrosine kinase 2.
See also
Eukaryotic small ribosomal subunit (40S)
Protein kinase C
Heterotrimeric G protein
References
Further reading
|
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