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https://en.wikipedia.org/wiki/Nicotianamine%20synthase | In enzymology, a nicotianamine synthase () is an enzyme that catalyzes the chemical reaction
3 S-adenosyl-L-methionine 3 S-methyl-5'-thioadenosine + nicotianamine
Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, S-methyl-5'-thioadenosine and nicotianamine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-Lmethioni ne 3-amino-3-carboxypropyltransferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/O-acetylhomoserine%20aminocarboxypropyltransferase | In enzymology, an O-acetylhomoserine aminocarboxypropyltransferase () is an enzyme that catalyzes the chemical reaction
O-acetyl-L-homoserine + methanethiol L-methionine + acetate
Thus, the two substrates of this enzyme are O-acetyl-L-homoserine and methanethiol, whereas its two products are L-methyionine and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is ''O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase. Other names in common use include O-acetyl-L-homoserine acetate-lyase (adding methanethiol), O-acetyl-L-homoserine sulfhydrolase, O-acetylhomoserine (thiol)-lyase, O''-acetylhomoserine sulfhydrolase, and methionine synthase. This enzyme participates in methionine metabolism and cysteine metabolism.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/O-phosphoserine%20sulfhydrylase | In enzymology, an O-phosphoserine sulfhydrylase () is an enzyme that catalyzes the chemical reaction
O-phospho-L-serine + hydrogen sulfide L-cysteine + phosphate
Thus, the two substrates of this enzyme are O-phospho-L-serine and hydrogen sulfide, whereas its two products are L-cysteine and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O-phospho-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase. This enzyme is also called O-phosphoserine(thiol)-lyase. This enzyme participates in cysteine metabolism and sulfur metabolism.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoglycerol%20geranylgeranyltransferase | In enzymology, a phosphoglycerol geranylgeranyltransferase () is an enzyme that catalyzes the chemical reaction
geranylgeranyl diphosphate + sn-glyceryl 1-phosphate diphosphate + sn-3-O-(geranylgeranyl)glyceryl 1-phosphate
Thus, the two substrates of this enzyme are geranylgeranyl diphosphate and sn-glyceryl 1-phosphate, whereas its two products are diphosphate and sn-3-O-(geranylgeranyl)glyceryl 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is geranylgeranyl diphosphate:sn-glyceryl phosphate geranylgeranyltransferase. Other names in common use include glycerol phosphate geranylgeranyltransferase, geranylgeranyl-transferase, and prenyltransferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein%20geranylgeranyltransferase%20type%20I | In enzymology, a protein geranylgeranyltransferase type I () is an enzyme that catalyzes the chemical reaction
geranylgeranyl diphosphate + protein-cysteine S-geranylgeranyl-protein + diphosphate
Thus, the two substrates of this enzyme are geranylgeranyl diphosphate and protein-cysteine, whereas its two products are S-geranylgeranyl-protein and diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is geranylgeranyl-diphosphate:protein-cysteine geranyltransferase. Other names in common use include GGTase-I, and GGTaseI.
Structural studies
As of late 2007, 17 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , and .
References
Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, p. 31-118.
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Rubber%20cis-polyprenylcistransferase | In enzymology, a rubber cis-polyprenylcistransferase () is an enzyme that catalyzes the chemical reaction
poly-cis-polyprenyl diphosphate + isopentenyl diphosphate diphosphate + a poly-cis-polyprenyl diphosphate longer by one C5 unit
Thus, the two substrates of this enzyme are poly-cis-polyprenyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and poly-cis-polyprenyl diphosphate longer by one C5 unit.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is poly-cis-polyprenyl-diphosphate:isopentenyl-diphosphate polyprenylcistransferase. Other names in common use include rubber allyltransferase, rubber transferase, isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase, cis-prenyl transferase, rubber polymerase, and rubber prenyltransferase. This enzyme participates in biosynthesis of steroids.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sym-norspermidine%20synthase | In enzymology, a sym-norspermidine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosylmethioninamine + propane-1,3-diamine 5'-methylthioadenosine + bis(3-aminopropyl)amine
Thus, the two substrates of this enzyme are S-adenosylmethioninamine and propane-1,3-diamine, whereas its two products are 5'-methylthioadenosine and bis(3-aminopropyl)amine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosylmethioninamine:propane-1,3-diamine 3-aminopropyltransferase. This enzyme participates in urea cycle and metabolism of amino groups.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiamine-phosphate%20diphosphorylase | In enzymology, a thiamine-phosphate diphosphorylase () is an enzyme that catalyzes the chemical reaction
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole diphosphate + thiamine monophosphate
The two substrates of this enzyme are 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate and 4-methyl-5-(2-phosphono-oxyethyl)thiazole; its two products are diphosphate and thiamine monophosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. This enzyme is on the biosynthetic pathway to thiamine.
Nomenclature
The systematic name of this enzyme class is 2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2 -phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase. Other names in common use include
thiamine phosphate synthase,
thiamine phosphate pyrophosphorylase,
thiamine monophosphate pyrophosphorylase, and
TMP-PPase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
References
Further reading
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Heptaprenyl%20diphosphate%20synthase | In enzymology, a heptaprenyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate 4 diphosphate + all-trans-heptaprenyl diphosphate
Thus, the two substrates of this enzyme are (2E,6E)-farnesyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and all-trans-heptaprenyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 4 isopentenyl units). Other names in common use include all-trans-heptaprenyl-diphosphate synthase, heptaprenyl pyrophosphate synthase, and heptaprenyl pyrophosphate synthetase. This enzyme participates in biosynthesis of steroids.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA-uridine%20aminocarboxypropyltransferase | In enzymology, a tRNA-uridine aminocarboxypropyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA uridine 5'-methylthioadenosine + tRNA 3-(3-amino-3-carboxypropyl)-uridine
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and tRNA uridine, whereas its two products are 5'-methylthioadenosine and tRNA 3-(3-amino-3-carboxypropyl)-uridine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA-uridine 3-(3-amino-3-carboxypropyl)transferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tryptophan%20dimethylallyltransferase | In enzymology, a tryptophan dimethylallyltransferase () is an enzyme that catalyzes the chemical reaction
dimethylallyl diphosphate + L-tryptophan diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
Thus, the two substrates of this enzyme are dimethylallyl diphosphate and L-tryptophan, whereas its two products are diphosphate and 4-(3-methylbut-2-enyl)-L-tryptophan.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is . Other names in common use include , , , DMAT synthetase, and .
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%201-carboxyvinyltransferase | In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase () is an enzyme that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
Thus, the two substrates of this enzyme are phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine, whereas its two products are phosphate and UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine. The pyruvate moiety provides the linker that bridges the glycan and peptide portion of peptidoglycan.
The enzyme is inhibited by the antibiotic fosfomycin, which covalently modifies an active site cysteine residue.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase. This enzyme participates in amino sugars metabolism and glycan biosynthesis.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
Literature
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Uracilylalanine%20synthase | In enzymology, an uracilylalanine synthase () is an enzyme that catalyzes the chemical reaction
O3-acetyl-L-serine + uracil 3-(uracil-1-yl)-L-alanine + acetate
Thus, the two substrates of this enzyme are O3-acetyl-L-serine and uracil, whereas its two products are 3-(uracil-1-yl)-L-alanine and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase. Other names in common use include O3-acetyl-L-serine acetate-lyase (adding uracil), isowillardiine synthase, willardiine synthase, and 3-O-acetyl-L-serine:uracil 1-(2-amino-2-carboxyethyl)transferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Zeatin%209-aminocarboxyethyltransferase | In enzymology, a zeatin 9-aminocarboxyethyltransferase () is an enzyme that catalyzes the chemical reaction
O-acetyl-L-serine + zeatin lupinate + acetate
Thus, the two substrates of this enzyme are O-acetyl-L-serine and zeatin, whereas its two products are lupinate and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3-acetyl-L-serine:zeatin 2-amino-2-carboxyethyltransferase. Other names in common use include beta-(9-cytokinin)-alanine synthase, beta-(9-cytokinin)alanine synthase, O-acetyl-L-serine acetate-lyase (adding N6-substituted adenine), lupinate synthetase, lupinic acid synthase, lupinic acid synthetase, and 3-O-acetyl-L-serine:zeatin 2-amino-2-carboxyethyltransferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Z-farnesyl%20diphosphate%20synthase | In enzymology, a Z-farnesyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction
geranyl diphosphate + isopentenyl diphosphate diphosphate + (2Z,6E)-farnesyl diphosphate
Thus, the two substrates of this enzyme are geranyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and (2Z,6E)-farnesyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is geranyl-diphosphate:isopentenyl-diphosphate geranylcistransferase. This enzyme is also called (Z)-farnesyl diphosphate synthase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oximinotransferase | In enzymology, an oximinotransferase () is an enzyme that catalyzes the chemical reaction
pyruvate oxime + acetone pyruvate + acetone oxime
Thus, the two substrates of this enzyme are pyruvate oxime and acetone, whereas its two products are pyruvate and acetone oxime.
This enzyme belongs to the family of transferases, specifically those transferring nitrogenous groups oximinotransferases. The systematic name of this enzyme class is pyruvate-oxime:acetone oximinotransferase. Other names in common use include transoximinase, oximase, pyruvate-acetone oximinotransferase, and transoximase.
References
EC 2.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxine%205%27-phosphate%20synthase | In enzymology, a pyridoxine 5'-phosphate synthase () is an enzyme that catalyzes the chemical reaction
1-deoxy-D-xylulose 5-phosphate + 3-hydroxy-1-aminoacetone phosphate pyridoxine-5'-phosphate + phosphate + 2 H2O
The two substrates of this enzyme are 1-deoxy-D-xylulose 5-phosphate (DXP) and 3-hydroxy-1-aminoacetone phosphate (HAP), whereas its 3 products are H2O, phosphate, and pyridoxine-5'-phosphate (a vitamer of pyridoxal phosphate).
Mechanism
In the first step of this condensation reaction, the amine group of HAP forms a Schiff base with the ketone group of DXP. The hydroxyl group on C4 of DXP is eliminated, forming an enol. The enol eliminates the phosphate derived from DXP, and water is added to the resulting double bond to reform the enol. This enol then attacks the HAP ketone group to close the ring and the resulting hydroxyl group is eliminated to form a double bond. A deprotonation causes the ring to aromatize, completing the synthesis of pyridoxine-5'-phosphate.
3-hydroxy-1-aminoacetone phosphate is unstable, so the reaction mechanism cannot be confirmed directly. Nonetheless, 14C and 18O isotopic labeling experiments, as well as structural studies, support the mechanism shown here. A glutamate residue, Glu72, is positioned ideally to perform most of the acid-base catalysis required in this mechanism, with histidine residues His45 and His193 appearing to play roles as well.
Structure
Pyridoxine-5'-phosphate synthase, or pdxJ, is a TIM barrel protein, alt |
https://en.wikipedia.org/wiki/1D-1-guanidino-3-amino-1%2C3-dideoxy-scyllo-inositol%20transaminase | In enzymology, a 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase () is an enzyme that catalyzes the chemical reaction
1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol + pyruvate 1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol + L-alanine
Thus, the two substrates of this enzyme are 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol and pyruvate, whereas its two products are 1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol:pyruvate aminotransferase. Other names in common use include guanidinoaminodideoxy-scyllo-inositol-pyruvate aminotransferase, and L-alanine-N-amidino-3-(or 5-)keto-scyllo-inosamine transaminase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C5-diaminovalerate%20transaminase | In enzymology, a 2,5-diaminovalerate transaminase () is an enzyme that catalyzes the chemical reaction
2,5-diaminopentanoate + 2-oxoglutarate 5-amino-2-oxopentanoate + L-glutamate
Thus, the two substrates of this enzyme are 2,5-diaminopentanoate and 2-oxoglutarate, whereas its two products are 5-amino-2-oxopentanoate and L-glutamate.
It employs one cofactor, pyridoxal phosphate.
Nomenclature
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 2,5-diaminopentanoate:2-oxoglutarate aminotransferase. Other names in common use include diamino-acid transaminase, and diamino acid aminotransferase.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-aminoadipate%20transaminase | In enzymology, a 2-aminoadipate transaminase () is an enzyme that catalyzes the chemical reaction
L-2-aminoadipate + 2-oxoglutarate 2-oxoadipate + L-glutamate
Thus, the two substrates of this enzyme are L-2-aminoadipate and 2-oxoglutarate, whereas its two products are 2-oxoadipate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2-aminoadipate:2-oxoglutarate aminotransferase. Other names in common use include alpha-aminoadipate aminotransferase, 2-aminoadipate aminotransferase, 2-aminoadipic aminotransferase, glutamic-ketoadipic transaminase, and glutamate-alpha-ketoadipate transaminase. This enzyme participates in lysine biosynthesis and lysine degradation. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-aminoethylphosphonate%E2%80%94pyruvate%20transaminase | In enzymology, a 2-aminoethylphosphonate—pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
(2-aminoethyl)phosphonate + pyruvate 2-phosphonoacetaldehyde + L-alanine
Thus, the two substrates of this enzyme are (2-aminoethyl)phosphonate and pyruvate, whereas its two products are 2-phosphonoacetaldehyde and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is (2-aminoethyl)phosphonate:pyruvate aminotransferase. Other names in common use include (2-aminoethyl)phosphonate transaminase, (2-aminoethyl)phosphonate aminotransferase, (2-aminoethyl)phosphonic acid aminotransferase, 2-aminoethylphosphonate-pyruvate aminotransferase, 2-aminoethylphosphonate aminotransferase, 2-aminoethylphosphonate transaminase, AEP transaminase, and AEPT. This enzyme participates in aminophosphonate metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-aminohexanoate%20transaminase | In enzymology, a 2-aminohexanoate transaminase () is an enzyme that catalyzes the chemical reaction
L-2-aminohexanoate + 2-oxoglutarate 2-oxohexanoate + L-glutamate
Thus, the two substrates of this enzyme are L-2-aminohexanoate and 2-oxoglutarate, whereas its two products are 2-oxohexanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2-aminohexanoate:2-oxoglutarate aminotransferase. Other names in common use include norleucine transaminase, norleucine (leucine) aminotransferase, and leucine L-norleucine: 2-oxoglutarate aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-aminobutyrate%20transaminase | In enzymology, 4-aminobutyrate transaminase (), also called GABA transaminase or 4-aminobutyrate aminotransferase, or GABA-T, is an enzyme that catalyzes the chemical reaction:
4-aminobutanoate + 2-oxoglutarate succinate semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are 4-aminobutanoate (GABA) and 2-oxoglutarate. The two products are succinate semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 4-aminobutanoate:2-oxoglutarate aminotransferase. This enzyme participates in 5 metabolic pathways: alanine and aspartate metabolism, glutamate metabolism, beta-alanine metabolism, propanoate metabolism, and butanoate metabolism. It employs one cofactor, pyridoxal phosphate.
This enzyme is found in prokaryotes, plants, fungi, and animals (including humans). Pigs have often been used when studying how this protein may work in humans.
Enzyme Commission number
GABA-T is Enzyme Commission number 2.6.1.19. This means that it is in the transferase class of enzymes, the nitrogenous transferase sub-class and the transaminase sub-subclass. As a nitrogenous transferase, its role is to transfer nitrogenous groups from one molecule to another. As a transaminase, GABA-T's role is to move functional groups from an amino acid and a α-keto acid, and vice versa. In the case of GABA-T, it takes a nitrogen group from GABA and uses it to cr |
https://en.wikipedia.org/wiki/Terrace%20ledge%20kink%20model | In chemistry, the Terrace Ledge Kink model (TLK), which is also referred to as the Terrace Step Kink model (TSK), describes the thermodynamics of crystal surface formation and transformation, as well as the energetics of surface defect formation. It is based upon the idea that the energy of an atom’s position on a crystal surface is determined by its bonding to neighboring atoms and that transitions simply involve the counting of broken and formed bonds. The TLK model can be applied to surface science topics such as crystal growth, surface diffusion, roughening, and vaporization.
History
The TLK model is credited as having originated from papers published in the 1920s by the German chemist W. Kossel and the Bulgarian chemist I. N. Stranski wherein the thermodynamic stability of step edges were discussed.
Definitions
Depending on the position of an atom on a surface, it can be referred to by one of several names. Figure 1 illustrates the names for the atomic positions and point defects on a surface for a simple cubic lattice.
Figure 2 shows a scanning tunneling microscopy topographic image of a step edge that shows many of the features in Figure 1.Figure 3 shows a crystal surface with steps, kinks, adatoms, and vacancies in a closely packed crystalline material, which resembles the surface featured in Figure 2.
Thermodynamics
The energy required to remove an atom from the surface depends on the number of bonds to other surface atoms which must be broken. For a simpl |
https://en.wikipedia.org/wiki/4-hydroxyglutamate%20transaminase | In enzymology, a 4-hydroxyglutamate transaminase () is an enzyme that catalyzes the chemical reaction
4-hydroxy-L-glutamate + 2-oxoglutarate 4-hydroxy-2-oxoglutarate + L-glutamate
Thus, the two substrates of this enzyme are 4-hydroxy-L-glutamate and 2-oxoglutarate, whereas its two products are 4-hydroxy-2-oxoglutarate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 4-hydroxy-L-glutamate:2-oxoglutarate aminotransferase. This enzyme is also called 4-hydroxyglutamate aminotransferase. This enzyme participates in arginine and proline metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-aminovalerate%20transaminase | In enzymology, a 5-aminovalerate transaminase () is an enzyme that catalyzes the chemical reaction
5-aminopentanoate + 2-oxoglutarate 5-oxopentanoate + L-glutamate
Thus, the two substrates of this enzyme are 5-aminopentanoate and 2-oxoglutarate, whereas its two products are 5-oxopentanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 5-aminopentanoate:2-oxoglutarate aminotransferase. Other names in common use include 5-aminovalerate aminotransferase, delta-aminovalerate aminotransferase, and delta-aminovalerate transaminase. This enzyme participates in lysine degradation. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylornithine%20transaminase | In enzymology, an acetylornithine transaminase () is an enzyme that catalyzes the chemical reaction
N2-acetyl-L-ornithine + 2-oxoglutarate N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and 2-oxoglutarate, whereas its two products are N-acetyl-L-glutamate 5-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Other names in common use include acetylornithine delta-transaminase, ACOAT, acetylornithine 5-aminotransferase, acetylornithine aminotransferase, N-acetylornithine aminotransferase, N-acetylornithine-delta-transaminase, N2-acetylornithine 5-transaminase, N2-acetyl-L-ornithine:2-oxoglutarate aminotransferase, succinylornithine aminotransferase, and 2-N-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase. This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Adenosylmethionine%E2%80%948-amino-7-oxononanoate%20transaminase | In enzymology, an adenosylmethionine-8-amino-7-oxononanoate transaminase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 8-amino-7-oxononanoate S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and 8-amino-7-oxononanoate, whereas its two products are S-adenosyl-4-methylthio-2-oxobutanoate and 7,8-diaminononanoate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase. Other names in common use include 7,8-diaminonanoate transaminase, 7,8-diaminononanoate transaminase, DAPA transaminase, 7,8-diaminopelargonic acid aminotransferase, DAPA aminotransferase, 7-keto-8-aminopelargonic acid, diaminopelargonate synthase, and 7-keto-8-aminopelargonic acid aminotransferase. This enzyme participates in biotin metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alanine%E2%80%94glyoxylate%20transaminase | In enzymology, an alanine-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction
L-alanine + glyoxylate pyruvate + glycine
Thus, the two substrates of this enzyme are L-alanine and glyoxylate, whereas its two products are pyruvate and glycine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:glyoxylate aminotransferase. Other names in common use include AGT, alanine-glyoxylate aminotransferase, alanine-glyoxylic aminotransferase, and L-alanine-glycine transaminase. This enzyme participates in alanine and aspartate metabolism and glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alanine%E2%80%94oxo-acid%20transaminase | In enzymology, an alanine-oxo-acid transaminase () is an enzyme that catalyzes the chemical reaction
L-alanine + a 2-oxo acid pyruvate + an L-amino acid
Thus, the two substrates of this enzyme are L-alanine and 2-oxo acid, whereas its two products are pyruvate and L-amino acid.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:2-oxo-acid aminotransferase. Other names in common use include L-alanine-alpha-keto acid aminotransferase, leucine-alanine transaminase, alanine-keto acid aminotransferase, and alanine-oxo acid aminotransferase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alanine%E2%80%94oxomalonate%20transaminase | In enzymology, an alanine-oxomalonate transaminase () is an enzyme that catalyzes the chemical reaction
L-alanine + oxomalonate pyruvate + aminomalonate
Thus, the two substrates of this enzyme are L-alanine and oxomalonate, whereas its two products are pyruvate and aminomalonate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:oxomalonate aminotransferase. Other names in common use include alanine-oxomalonate aminotransferase, L-alanine-ketomalonate transaminase, and alanine-ketomalonate (mesoxalate) transaminase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/IC3b | iC3b is a protein fragment that is part of the complement system, a component of the vertebrate immune system. iC3b is produced when complement factor I cleaves C3b. Complement receptors on white blood cells are able to bind iC3b, so iC3b functions as an opsonin. Unlike intact C3b, iC3b cannot associate with factor B, thus preventing amplification of the complement cascade through the alternative pathway. Complement factor I can further cleave iC3b into a protein fragment known as C3d.
References |
https://en.wikipedia.org/wiki/Subgenomic%20mRNA | Subgenomic mRNAs are essentially smaller sections of the original transcribed template strand.
3' to 5' DNA or RNA
During transcription, the original template strand is usually read from the 3' to the 5' end from beginning to end. Subgenomic mRNAs are created when transcription begins at the 3' end of the template strand (or 5' of the to-be-newly synthesized template) and begins to copy towards the 5' end of the template strand before "jumping" to the end of the template and copying the last nucleotides of the 5' end of the template, (finishing the 3' tail for the newly created strand).
As a result, the translated strand will have a similar 5' end to varying degrees with the original template (depending on which part of the template the transcription jumped over) and a similar 3' end to the template.
5' to 3' (positive sense) viral RNA
Positive-sense (5' to 3') viral RNA which may be directly translated into the desired viral proteins, undergoes a similar process as described in 3' to 5'. Portions of the viral RNA may be skipped during translation.
Result
The result is that many different proteins can be created from the same mRNA strand, with similar 5' ends (to varying degrees) and same 3' ends. Or, different proteins can be created with positive sense viral RNA.
The 5' section on the newly created strand matches that of the template strand, and this section on the template strand is referred to as the "nested set".
3' |
https://en.wikipedia.org/wiki/Nervous%20%28Gene%20Summers%20song%29 | "Nervous" is a rockabilly/doo-wop song first recorded by Gene Summers and His Rebels in 1958 and later covered by Robert Gordon and Link Wray, among others. It was composed by Mary Tarver in 1957, published by Ted Music, BMI and issued on Jan/Jane Records. The "Nervous" recording session took place at Liberty Records Studios in Hollywood, California in June 1958 and featured Rene Hall and James McClung on guitar, Plas Johnson on saxophone, Earl Palmer on drums, and George "Red" Callendar on bass. The background vocal group was the Five Masks (Al "TNT" Braggs, Cal Valentine, Robert Valentine, Billy Fred Thomas and Jesse Lee Floyd). The flipside of "Nervous" was "Gotta Lotta That".
Reviews
BILLBOARD MAGAZINE - June 1958 Reviews of New Pop Records
GENE SUMMERS
Nervous....83
JAN 102 - Strong material and strong performance by the new talent. It's a powerful beat job and the kids should flip over it. Action already reported from the southwest territories. (Ted, BMI)
The Cash Box - The Cash Box Best Bets - June 14, 1958 "NERVOUS" (2:22) [Ted, BMI - Tarver]Gene Summers & His Rebels (January 102)"...exciting opus...could spread like wildfire...strong merchandise..."
"Nervous" cover versions
Johnny Devlin - New Zealand
Lonstars - Finland
Rock-Ola & The Freewheelers - Finland
Robert Gordon - United States
Robert Gordon with Link Wray - United States
References
Gene Summers discography from Rocky Productions, France
Gene Summers discography from Wangdangdula Finland
Gene Summe |
https://en.wikipedia.org/wiki/Barium%20bromide | Barium bromide is the chemical compound with the formula BaBr2. It is ionic and hygroscopic in nature.
Structure and properties
BaBr2 crystallizes in the lead chloride (cotunnite) motif, giving white orthorhombic crystals that are deliquescent.
In aqueous solution BaBr2 behaves as a simple salt.
Solutions of barium bromide reacts with the sulfate salts to produce a solid precipitate of barium sulfate.
BaBr2 + → BaSO4 + 2 Br−
Similar reactions occur with oxalic acid, hydrofluoric acid, and phosphoric acid, giving solid precipitates of barium oxalate, fluoride, and phosphate, respectively.
Preparation
Barium bromide can be prepared by treating barium sulfide or barium carbonate with hydrobromic acid:
BaS + 2 HBr → BaBr2 + H2S
BaCO3 + 2 HBr → BaBr2 + CO2 + H2O
Barium bromide crystallizes from concentrated aqueous solution in its dihydrate , BaBr2·2H2O. Heating this dihydrate to 120 °C gives the anhydrous salt.
Uses
Barium bromide is a precursor to chemicals used in photography and to other bromides.
Historically, barium bromide was used to purify radium in a process of fractional crystallization devised by Marie Curie. Since radium precipitates preferentially in a solution of barium bromide, the ratio of radium to barium in the precipitate would be higher than the ratio in the solution.
Safety
Barium bromide, along with other water-soluble barium salts (e.g. barium chloride), is toxic. However, there is no conclusive data available on its hazards.
In |
https://en.wikipedia.org/wiki/Aminolevulinate%20transaminase | In enzymology, an aminolevulinate transaminase () is an enzyme that catalyzes the chemical reaction
5-aminolevulinate + pyruvate 4,5-dioxopentanoate + L-alanine
Thus, the two substrates of this enzyme are 5-aminolevulinate and pyruvate, whereas its two products are 4,5-dioxopentanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 5-aminolevulinate:pyruvate aminotransferase. Other names in common use include . This enzyme participates in porphyrin and chlorophyll metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arginine%E2%80%94pyruvate%20transaminase | In enzymology, an arginine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-arginine + pyruvate 5-guanidino-2-oxopentanoate + L-alanine
Thus, the two substrates of this enzyme are L-arginine and pyruvate, whereas its two products are 5-guanidino-2-oxopentanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arginine:pyruvate aminotransferase. Other names in common use include arginine:pyruvate transaminase, and AruH.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aromatic-amino-acid%E2%80%94glyoxylate%20transaminase | In enzymology, an aromatic-amino-acid-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction
an aromatic amino acid + glyoxylate an aromatic oxo acid + glycine
Thus, the two substrates of this enzyme are aromatic amino acid and glyoxylate, whereas its two products are aromatic oxo acid and glycine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is aromatic-amino-acid:glyoxylate aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aromatic-amino-acid%20transaminase | In enzymology, an aromatic-amino-acid transaminase () is an enzyme that catalyzes the chemical reaction
an aromatic amino acid + 2-oxoglutarate an aromatic oxo acid + L-glutamate
Thus, the two substrates of this enzyme are aromatic amino acid and 2-oxoglutarate, whereas its two products are aromatic oxo acid and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is aromatic-amino-acid:2-oxoglutarate aminotransferase. Other names in common use include aromatic amino acid aminotransferase, aromatic aminotransferase, and ArAT. This enzyme participates in 6 metabolic pathways: methionine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, novobiocin biosynthesis, and alkaloid biosynthesis i. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Asparagine%E2%80%94oxo-acid%20transaminase | In enzymology, an asparagine-oxo-acid transaminase () is an enzyme that catalyzes the chemical reaction
L-asparagine + a 2-oxo acid 2-oxosuccinamate + an amino acid
Thus, the two substrates of this enzyme are L-asparagine and 2-oxo acid, whereas its two products are 2-oxosuccinamate and amino acid.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-asparagine:2-oxo-acid aminotransferase. This enzyme is also called asparagine-keto acid aminotransferase. This enzyme participates in alanine and aspartate metabolism and tetracycline biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%E2%80%94phenylpyruvate%20transaminase | In enzymology, an aspartate-phenylpyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-aspartate + phenylpyruvate oxaloacetate + L-phenylalanine
Thus, the two substrates of this enzyme are L-aspartate and phenylpyruvate, whereas its two products are oxaloacetate and L-phenylalanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-aspartate:phenylpyruvate aminotransferase. This enzyme is also called aspartate-phenylpyruvate aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%E2%80%94prephenate%20aminotransferase | In enzymology, an aspartate-prephenate aminotransferase () is an enzyme that catalyzes the chemical reaction
L-arogenate + oxaloacetate prephenate + L-aspartate
Thus, the two substrates of this enzyme are L-arogenate and oxaloacetate, whereas its two products are prephenate and L-aspartate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:oxaloacetate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ourmiavirus | Ourmiavirus is a genus of positive-strand RNA viruses. Cucurbits, cherry, and cassava serve as natural hosts. There are three species in this genus. Diseases associated with this genus include: OuMV: yellowing and chlorotic spot symptoms.
Structure
Viruses in the genus Ourmiavirus are non-enveloped, with icosahedral and bacilliform geometries, and T=1 symmetry. The diameter is around 18 nm, with a length of 30 nm.
Genome
Genomes are linear and segmented, around 2.8kb in length.
Life cycle
Viral replication is cytoplasmic. Entry into the host cell is achieved by penetration into the host cell. Replication follows the positive stranded RNA virus replication model. Positive stranded RNA virus transcription is the method of transcription. The virus exits the host cell by tubule-guided viral movement. Cucurbits, cherry, and cassava serve as the natural host.
Taxonomy
The genus has three species:
Cassava virus C
Epirus cherry virus
Ourmia melon virus
References
External links
ICTV Report: Ourmiavirus
Viralzone: Ourmiavirus
Positive-sense single-stranded RNA viruses
Virus genera |
https://en.wikipedia.org/wiki/Beta-alanine%E2%80%94pyruvate%20transaminase | In enzymology, a beta-alanine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-alanine + 3-oxopropanoate pyruvate + beta-alanine
Thus, the two substrates of this enzyme are L-alanine and 3-oxopropanoate, whereas its two products are pyruvate and beta-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:3-oxopropanoate aminotransferase. Other names in common use include beta-alanine-pyruvate aminotransferase, and beta-alanine-alpha-alanine transaminase. This enzyme participates in 4 metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine metabolism, and propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cephalosporin-C%20transaminase | In enzymology, a cephalosporin-C transaminase () is an enzyme that catalyzes the chemical reaction
(7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate + D-glutamate cephalosporin C + 2-oxoglutarate
Thus, the two substrates of this enzyme are (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate and D-glutamate, whereas its two products are cephalosporin C and 2-oxoglutarate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is cephalosporin-C:2-oxoglutarate aminotransferase. Other names in common use include cephalosporin C aminotransferase, and L-alanine:cephalosporin-C aminotransferase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cysteine-conjugate%20transaminase | In enzymology, a cysteine-conjugate transaminase () is an enzyme that catalyzes the chemical reaction
S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate S-(4-bromophenyl)mercaptopyruvate + L-glutamate
Thus, the two substrates of this enzyme are S-(4-bromophenyl)-L-cysteine and 2-oxoglutarate, whereas its two products are S-(4-bromophenyl)mercaptopyruvate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is S-(4-bromophenyl)-L-cysteine:2-oxoglutarate aminotransferase. Other names in common use include cysteine conjugate aminotransferase, and cysteine-conjugate alpha-ketoglutarate transaminase (CAT-1).
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cysteine%20transaminase | In enzymology, a cysteine transaminase () is an enzyme that catalyzes the chemical reaction
L-cysteine + 2-oxoglutarate mercaptopyruvate + L-glutamate
Thus, the two substrates of this enzyme are L-cysteine and 2-oxoglutarate, whereas its two products are mercaptopyruvate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-cysteine:2-oxoglutarate aminotransferase. Other names in common use include cysteine aminotransferase, L-cysteine aminotransferase, and CGT. This enzyme participates in cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-4-hydroxyphenylglycine%20transaminase | In enzymology, a D-4-hydroxyphenylglycine transaminase () is an enzyme that catalyzes the chemical reaction
D-4-hydroxyphenylglycine + 2-oxoglutarate 4-hydroxyphenylglyoxylate + L-glutamate
Thus, the two substrates of this enzyme are D-4-hydroxyphenylglycine and 2-oxoglutarate, whereas its two products are 4-hydroxyphenylglyoxylate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase. This enzyme is also called D-hydroxyphenylglycine aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-amino-acid%20transaminase | In enzymology, a D-amino-acid transaminase () is an enzyme that catalyzes the chemical reaction:
D-alanine + 2-oxoglutarate pyruvate + D-glutamate
Thus, the two substrates of this enzyme are D-alanine and 2-oxoglutarate, whereas its two products are pyruvate and D-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is D-alanine:2-oxoglutarate aminotransferase. Other names in common use include D-aspartate transaminase, D-alanine aminotransferase, D-aspartic aminotransferase, D-alanine-D-glutamate transaminase, D-alanine transaminase, and D-amino acid aminotransferase. This enzyme participates in 6 metabolic pathways: lysine degradation, arginine and proline metabolism, phenylalanine metabolism, D-arginine and D-ornithine metabolism, D-alanine metabolism, and peptidoglycan biosynthesis. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Diamine%20transaminase | In enzymology, a diamine transaminase () is an enzyme that catalyzes the chemical reaction:
an alpha,omega-diamine + 2-oxoglutarate an omega-aminoaldehyde + L-glutamate
Thus, the two substrates of this enzyme are alpha,omega-diamine and 2-oxoglutarate, whereas its two products are omega-aminoaldehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is diamine:2-oxoglutarate aminotransferase. Other names in common use include amine transaminase, amine-ketoacid transaminase, diamine aminotransferase, and diamine-ketoglutaric transaminase. This enzyme participates in urea cycle and metabolism of amino groups.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diaminobutyrate%E2%80%942-oxoglutarate%20transaminase | In enzymology, a diaminobutyrate-2-oxoglutarate transaminase () is an enzyme that catalyzes the chemical reaction
L-2,4-diaminobutanoate + 2-oxoglutarate L-aspartate 4-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are L-2,4-diaminobutanoate and 2-oxoglutarate, whereas its two products are L-aspartate 4-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase. Other names in common use include L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, 2,4-diaminobutyrate 4-aminotransferase, diaminobutyrate aminotransferase, DABA aminotransferase, DAB aminotransferase, EctB, diaminibutyric acid aminotransferase, and L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase. This enzyme participates in glycine, serine and threonine metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diaminobutyrate%E2%80%94pyruvate%20transaminase | In enzymology, a diaminobutyrate-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-2,4-diaminobutanoate + pyruvate L-aspartate 4-semialdehyde + L-alanine
Thus, the two substrates of this enzyme are L-2,4-diaminobutanoate and pyruvate, whereas its two products are L-aspartate 4-semialdehyde and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2,4-diaminobutanoate:pyruvate aminotransferase. Other names in common use include diaminobutyrate-pyruvate aminotransferase, and L-diaminobutyric acid transaminase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydroxyphenylalanine%20transaminase | In enzymology, a dihydroxyphenylalanine transaminase () is an enzyme that catalyzes the chemical reaction
3,4-dihydroxy-L-phenylalanine + 2-oxoglutarate 3,4-dihydroxyphenylpyruvate + L-glutamate
Thus, the two substrates of this enzyme are 3,4-dihydroxy-L-phenylalanine and 2-oxoglutarate, whereas its two products are 3,4-dihydroxyphenylpyruvate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase. Other names in common use include dopa transaminase, dihydroxyphenylalanine aminotransferase, aspartate-DOPP transaminase (ADT), L-dopa transaminase, dopa aminotransferase, glutamate-DOPP transaminase (GDT), phenylalanine-DOPP transaminase (PDT), DOPA 2-oxoglutarate aminotransferase, and DOPAATS. This enzyme participates in tyrosine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diiodotyrosine%20transaminase | In enzymology, a diiodotyrosine transaminase () is an enzyme that catalyzes the chemical reaction
3,5-diiodo-L-tyrosine + 2-oxoglutarate 4-hydroxy-3,5-diiodophenylpyruvate + L-glutamate
Thus, the two substrates of this enzyme are 3,5-diiodo-L-tyrosine and 2-oxoglutarate, whereas its two products are 4-hydroxy-3,5-diiodophenylpyruvate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 3,5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase. Other names in common use include diiodotyrosine aminotransferase, halogenated tyrosine aminotransferase, and halogenated tyrosine transaminase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-methionine%E2%80%94pyruvate%20transaminase | In enzymology, a D-methionine—pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
D-methionine + pyruvate 4-methylthio-2-oxobutanoate + L-alanine
Thus, the two substrates of this enzyme are D-methionine and pyruvate, whereas its two products are 4-methylthio-2-oxobutanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is D-methionine:pyruvate aminotransferase. Other names in common use include D-methionine transaminase, and D-methionine aminotransferase. This enzyme participates in d-alanine metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-amino-4%2C6-dideoxy-D-glucose%20transaminase | In enzymology, a dTDP-4-amino-4,6-dideoxy-D-glucose transaminase () is an enzyme that catalyzes the chemical reaction
dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate
Thus, the two substrates of this enzyme are dTDP-4-amino-4,6-dideoxy-D-glucose and 2-oxoglutarate, whereas its two products are dTDP-4-dehydro-6-deoxy-D-glucose and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is dTDP-4-amino-4,6-dideoxy-D-glucose:2-oxoglutarate aminotransferase. Other names in common use include thymidine diphospho-4-amino-4,6-dideoxyglucose aminotransferase, thymidine diphospho-4-amino-6-deoxyglucose aminotransferase, thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase, thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase, and TDP-4-keto-6-deoxy-D-glucose transaminase. This enzyme participates in nucleotide sugars metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-amino-4%2C6-dideoxygalactose%20transaminase | In enzymology, a dTDP-4-amino-4,6-dideoxygalactose transaminase () is an enzyme that catalyzes the chemical reaction
dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate dTDP-4-dehydro-6-deoxy-D-galactose + L-glutamate
Thus, the two substrates of this enzyme are dTDP-4-amino-4,6-dideoxy-D-galactose and 2-oxoglutarate, whereas its two products are dTDP-4-dehydro-6-deoxy-D-galactose and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase. Other names in common use include thymidine diphosphoaminodideoxygalactose aminotransferase, and thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%E2%80%94prephenate%20aminotransferase | In enzymology, glutamate-prephenate aminotransferase (, also known as prephenate transaminase, PAT, and L-glutamate:prephenate aminotransferase) is an enzyme that catalyzes the chemical reaction
L-arogenate + 2-oxoglutarate prephenate + L-glutamate
Thus, the two substrates of this enzyme are L-arogenate and 2-oxoglutarate, whereas its two products are prephenate and L-glutamate. However, in most plant species utilizing this enzyme, the left side of the reaction is strongly favored. Therefore, glutamate is used as the amino donor to convert prephenate into arogenate.
Nomenclature
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:2-oxoglutarate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), and L-glutamate:prephenate aminotransferase. It operates in the phenylalanine and tyrosine biosynthesis pathway.
Species distribution
The gene which encodes this enzyme has recently been identified in various plant species and microorganisms, meaning that all genes in the pathway have now been identified and accounted for. This pathway occurs in many different plant species. As phenylalanine is an essential amino acid, humans (and other animals) have lost the ability to produce it themselves and must therefore obtain it from their diet. As such, the activity of this enzyme in various plant species af |
https://en.wikipedia.org/wiki/Glutamine%E2%80%94fructose-6-phosphate%20transaminase%20%28isomerizing%29 | In enzymology, a glutamine-fructose-6-phosphate transaminase (isomerizing) () is an enzyme that catalyzes the chemical reaction
L-glutamine + D-fructose 6-phosphate L-glutamate + D-glucosamine 6-phosphate
Thus, the two substrates of this enzyme are L-glutamine and D-fructose 6-phosphate, whereas its two products are L-glutamate and D-glucosamine 6-phosphate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:D-fructose-6-phosphate isomerase (deaminating). This enzyme participates in glutamate metabolism and aminosugars metabolism.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
EC 2.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Niphidium | Niphidium is a genus of ferns in the family Polypodiaceae, subfamily Polypodioideae, according to the Pteridophyte Phylogeny Group classification of 2016 (PPG I). They are native to tropical America.
Species
, Checklist of Ferns and Lycophytes of the World accepted the following species:
Niphidium albopunctatissimum (J.Sm.) Lellinger
Niphidium anocarpos (Kunze) Lellinger
Niphidium carinatum Lellinger
Niphidium crassifolium (L.) Lellinger
Niphidium longifolium (Cav.) C.V.Morton & Lellinger
Niphidium macbridei Lellinger
Niphidium mortonianum Lellinger
Niphidium nidulare (Rosenst.) Lellinger
Niphidium oblanceolatum A.Rojas
Niphidium rufosquamatum Lellinger
Niphidium vittaria (Mett.) Lellinger
References
External links
Niphidium species
Polypodiaceae
Fern genera |
https://en.wikipedia.org/wiki/Glutamine%E2%80%94phenylpyruvate%20transaminase | In enzymology, a glutamine-phenylpyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-glutamine + phenylpyruvate 2-oxoglutaramate + L-phenylalanine
Thus, the two substrates of this enzyme are L-glutamine and phenylpyruvate, whereas its two products are 2-oxoglutaramate and L-phenylalanine.
This enzyme belongs to the family of transferases, to be specific, the transaminases, that transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:phenylpyruvate aminotransferase. Other names in common use include glutamine transaminase K, and glutamine-phenylpyruvate aminotransferase. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamine%E2%80%94pyruvate%20transaminase | In enzymology, a glutamine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-glutamine + pyruvate 2-oxoglutaramate + L-alanine
Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutaramate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:pyruvate aminotransferase. Other names in common use include glutaminase II, L-glutamine transaminase L, and glutamine-oxo-acid transaminase. This enzyme participates in glutamate metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamine%E2%80%94scyllo-inositol%20transaminase | In enzymology, a glutamine-scyllo-inositol transaminase () is an enzyme that catalyzes the chemical reaction
L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone 2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol
Thus, the two substrates of this enzyme are L-glutamine and 2,4,6/3,5-pentahydroxycyclohexanone, whereas its two products are 2-oxoglutaramate and 1-amino-1-deoxy-scyllo-inositol.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase. Other names in common use include glutamine scyllo-inosose aminotransferase, L-glutamine-keto-scyllo-inositol aminotransferase, glutamine-scyllo-inosose transaminase, and L-glutamine-scyllo-inosose transaminase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%E2%80%94oxaloacetate%20transaminase | In enzymology, a glycine-oxaloacetate transaminase () is an enzyme that catalyzes the chemical reaction
glycine + oxaloacetate glyoxylate + L-aspartate
Thus, the two substrates of this enzyme are glycine and oxaloacetate, whereas its two products are glyoxylate and L-aspartate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is glycine:oxaloacetate aminotransferase. This enzyme is also called glycine-oxaloacetate aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20transaminase | In enzymology, a glycine transaminase () is an enzyme that catalyzes the chemical reaction
glycine + 2-oxoglutarate glyoxylate + L-glutamate
Thus, the two substrates of this enzyme are glycine and 2-oxoglutarate, whereas its two products are glyoxylate and L-glutamate.
This reactions strongly favours synthesis of glycine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is glycine:2-oxoglutarate aminotransferase. Other names in common use include glutamic-glyoxylic transaminase, glycine aminotransferase, glyoxylate-glutamic transaminase, L-glutamate:glyoxylate aminotransferase, and glyoxylate-glutamate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Histidine%20transaminase | In enzymology, a histidine transaminase () is an enzyme that catalyzes the chemical reaction
L-histidine + 2-oxoglutarate (imidazol-5-yl)pyruvate + L-glutamate
Thus, the two substrates of this enzyme are L-histidine and 2-oxoglutarate, whereas its two products are (imidazol-5-yl)pyruvate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-histidine:2-oxoglutarate aminotransferase. Other names in common use include histidine aminotransferase, and histidine-2-oxoglutarate aminotransferase. This enzyme participates in histidine metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Histidinol-phosphate%20transaminase | In enzymology, a histidinol-phosphate transaminase () is an enzyme that catalyzes the chemical reaction
L-histidinol phosphate + 2-oxoglutarate 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Thus, the two substrates of this enzyme are L-histidinol phosphate and 2-oxoglutarate, whereas its two products are 3-(imidazol-4-yl)-2-oxopropyl phosphate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-histidinol-phosphate:2-oxoglutarate aminotransferase. Other names in common use include imidazolylacetolphosphate transaminase, glutamic-imidazoleacetol phosphate transaminase, histidinol phosphate aminotransferase, imidazoleacetol phosphate transaminase, L-histidinol phosphate aminotransferase, histidine:imidazoleacetol phosphate transaminase, IAP transaminase, and imidazolylacetolphosphate aminotransferase. This enzyme participates in 5 metabolic pathways: histidine metabolism, tyrosine metabolism, phenylalanine metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and novobiocin biosynthesis. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Kynurenine%E2%80%94glyoxylate%20transaminase | In enzymology, a kynurenine-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction:
L-kynurenine + glyoxylate 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
Thus, the two substrates of this enzyme are L-kynurenine and glyoxylate, whereas its two products are 4-(2-aminophenyl)-2,4-dioxobutanoate and glycine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-kynurenine:glyoxylate aminotransferase (cyclizing). This enzyme is also called kynurenine-glyoxylate aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Kynurenine%E2%80%94oxoglutarate%20transaminase | In enzymology, a kynurenine-oxoglutarate transaminase () is an enzyme that catalyzes the chemical reaction
-kynurenine + 2-oxoglutarate 4-(2-aminophenyl)-2,4-dioxobutanoate + -glutamate
Thus, the two substrates of this enzyme are -kynurenine and 2-oxoglutarate, whereas its two products are 4-(2-aminophenyl)-2,4-dioxobutanoate and -glutamate. The former product is an unstable α-oxo acid that quickly undergoes intramolecular cyclization to form kynurenic acid.
This enzyme belongs to the family of transferases, to be specific, the transaminases, that transfer nitrogenous groups. The systematic name of this enzyme class is -kynurenine:2-oxoglutarate aminotransferase. Other names in common use include kynurenine transaminase (cyclizing), kynurenine 2-oxoglutarate transaminase, kynurenine aminotransferase, and -kynurenine aminotransferase. This enzyme participates in tryptophan metabolism. It employs one cofactor, pyridoxal phosphate.
KYAT1, AADAT (aka KYAT2), and KYAT3 are examples of enzymes of this class. GOT2 (aka KYAT4) is also believed to catalyze the above reaction.
Structural studies
As of early 2009, 18 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , and .
References
Further reading
EC 2.6.1
Enzymes of known structure
Pyridoxal phosphate enzymes |
https://en.wikipedia.org/wiki/Leucine%20transaminase | In enzymology, a leucine transaminase () is an enzyme that catalyzes the chemical reaction
L-leucine + 2-oxoglutarate 4-methyl-2-oxopentanoate + L-glutamate
Thus, the two substrates of this enzyme are L-leucine and 2-oxoglutarate, whereas its two products are 4-methyl-2-oxopentanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-leucine:2-oxoglutarate aminotransferase. Other names in common use include L-leucine aminotransferase, leucine 2-oxoglutarate transaminase, leucine aminotransferase, and leucine-alpha-ketoglutarate transaminase. This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, valine, leucine and isoleucine biosynthesis, and pantothenate and coa biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L%2CL-diaminopimelate%20aminotransferase | In enzymology, a L,L-diaminopimelate aminotransferase () is an enzyme that catalyzes the chemical reaction
LL-2,6-diaminoheptanedioate + 2-oxoglutarate (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
Thus, the two substrates of this enzyme are LL-2,6-diaminoheptanedioate and 2-oxoglutarate, whereas its 3 products are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, L-glutamate, and H2O.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include LL-diaminopimelate transaminase, LL-DAP aminotransferase, and LL-DAP-AT. This enzyme participates in lysine biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-lysine%206-transaminase | In enzymology, a L-lysine 6-transaminase () is an enzyme that catalyzes the chemical reaction
L-lysine + 2-oxoglutarate 2-aminoadipate 6-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are L-lysine and 2-oxoglutarate, whereas its two products are 2-aminoadipate 6-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate.
Nomenclature
The systematic name of this enzyme class is L-lysine:2-oxoglutarate 6-aminotransferase. Other names in common use include
lysine 6-aminotransferase,
lysine epsilon-aminotransferase,
lysine epsilon-transaminase,
lysine:2-ketoglutarate 6-aminotransferase,
L-lysine-alpha-ketoglutarate aminotransferase, and
L-lysine-alpha-ketoglutarate 6-aminotransferase.
Structure
L-lysine 6-transaminase belongs to the aminotransferase class-III family. Crystal structures of L-lysine 6-transaminase reveal a Glu243 “switch” through which the enzyme changes substrate specificities.
References
Further reading
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysine%E2%80%94pyruvate%206-transaminase | In enzymology, a lysine-pyruvate 6-transaminase () is an enzyme that catalyzes the chemical reaction
L-lysine + pyruvate ⇌ L-2-aminoadipate 6-semialdehyde + L-alanine
Thus, the two substrates of this enzyme are L-lysine and pyruvate, whereas its two products are L-2-aminoadipate 6-semialdehyde and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-lysine:pyruvate aminotransferase. Other names in common use include lysine-pyruvate aminotransferase, and Lys-AT.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methionine%E2%80%94glyoxylate%20transaminase | In enzymology, a methionine-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction
L-methionine + glyoxylate 4-methylthio-2-oxobutanoate + glycine
Thus, the two substrates of this enzyme are L-methionine and glyoxylate, whereas its two products are 4-methylthio-2-oxobutanoate and glycine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-methionine:glyoxylate aminotransferase. Other names in common use include methionine-glyoxylate aminotransferase, and MGAT.
References
Further reading
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N6-acetyl-beta-lysine%20transaminase | In enzymology, a N6-acetyl-beta-lysine transaminase () is an enzyme that catalyzes the chemical reaction
6-acetamido-3-aminohexanoate + 2-oxoglutarate 6-acetamido-3-oxohexanoate + L-glutamate
Thus, the two substrates of this enzyme are 6-acetamido-3-aminohexanoate and 2-oxoglutarate, whereas its two products are 6-acetamido-3-oxohexanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 6-acetamido-3-aminohexanoate:2-oxoglutarate aminotransferase. This enzyme is also called epsilon-acetyl-beta-lysine aminotransferase. This enzyme participates in lysine degradation. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nicotianamine%20aminotransferase | In enzymology, a nicotianamine aminotransferase () is an enzyme that catalyzes the chemical reaction
nicotianamine + 2-oxoglutarate 3"-deamino-3"-oxonicotianamine + L-glutamate
Thus, the two substrates of this enzyme are nicotianamine and 2-oxoglutarate, whereas its two products are 3-deamino-3-oxonicotianamine and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is nicotianamine:2-oxoglutarate aminotransferase; nicotianamine transaminase. Other names in common use include NAAT, NAAT-I, NAAT-II, and NAAT-III.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ornithine%28lysine%29%20transaminase | In enzymology, an ornithine(lysine) transaminase () is an enzyme that catalyzes the chemical reaction
L-ornithine + 2-oxoglutarate 3,4-dihydro-2H-pyrrole-2-carboxylate + L-glutamate + H2O
Thus, the two substrates of this enzyme are L-ornithine and 2-oxoglutarate, whereas its 3 products are 3,4-dihydro-2H-pyrrole-2-carboxylate, L-glutamate, and H2O.
This enzyme belongs to the family of transferases, specifically the transaminases, which run really fast to nitrogenous groups. The systematic name of this enzyme class is L-ornithine:2-oxoglutarate-aminotransferase. Other names in common use include ornithine(lysine) aminotransferase, lysine/ornithine:2-oxoglutarate aminotransferase, and L-ornithine(L-lysine):2-oxoglutarate-aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylalanine%28histidine%29%20transaminase | In enzymology, a phenylalanine(histidine) transaminase () is an enzyme that catalyzes the chemical reaction
L-phenylalanine + pyruvate phenylpyruvate + L-alanine
Thus, the two substrates of this enzyme are L-phenylalanine and pyruvate, whereas its two products are phenylpyruvate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-phenylalanine:pyruvate aminotransferase. Other names in common use include phenylalanine (histidine) aminotransferase, phenylalanine(histidine):pyruvate aminotransferase, histidine:pyruvate aminotransferase, and L-phenylalanine(L-histidine):pyruvate aminotransferase.
References
Further reading
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxamine%E2%80%94oxaloacetate%20transaminase | In enzymology, a pyridoxamine-oxaloacetate transaminase () is an enzyme that catalyzes the chemical reaction:
pyridoxamine + oxaloacetate pyridoxal + L-aspartate
Thus, the two substrates of this enzyme are pyridoxamine and oxaloacetate, whereas its two products are pyridoxal and L-aspartate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine:oxaloacetate aminotransferase. This enzyme participates in vitamin B6 metabolism.
References
Further reading
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxamine-phosphate%20transaminase | In enzymology, a pyridoxamine-phosphate transaminase () is an enzyme that catalyzes the chemical reaction
pyridoxamine 5'-phosphate + 2-oxoglutarate pyridoxal 5'-phosphate + D-glutamate
Thus, the two substrates of this enzyme are pyridoxamine 5'-phosphate and 2-oxoglutarate, whereas its two products are pyridoxal 5'-phosphate and D-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine-5'-phosphate:2-oxoglutarate aminotransferase (D-glutamate-forming). Other names in common use include pyridoxamine phosphate aminotransferase, pyridoxamine 5'-phosphate-alpha-ketoglutarate transaminase, and pyridoxamine 5'-phosphate transaminase. This enzyme participates in vitamin B6 metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyridoxamine%E2%80%94pyruvate%20transaminase | In enzymology, a pyridoxamine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
pyridoxamine + pyruvate pyridoxal + L-alanine
Thus, the two substrates of this enzyme are pyridoxamine and pyruvate, whereas its two products are pyridoxal and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine:pyruvate aminotransferase. This enzyme is also called pyridoxamine-pyruvic transaminase. This enzyme participates in vitamin B6 metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-3-amino-2-methylpropionate%E2%80%94pyruvate%20transaminase | In enzymology, a (R)-3-amino-2-methylpropionate—pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
(R)-3-amino-2-methylpropanoate + pyruvate 2-methyl-3-oxopropanoate + L-alanine
Thus, the two substrates of this enzyme are (R)-3-amino-2-methylpropanoate and pyruvate, whereas its two products are 2-methyl-3-oxopropanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is (R)-3-amino-2-methylpropanoate:pyruvate aminotransferase. Other names in common use include D-3-aminoisobutyrate-pyruvate transaminase, beta-aminoisobutyrate-pyruvate aminotransferase, D-3-aminoisobutyrate-pyruvate aminotransferase, D-3-aminoisobutyrate-pyruvate transaminase, (R)-3-amino-2-methylpropionate transaminase, and D-beta-aminoisobutyrate:pyruvate aminotransferase. But some additional information is that this enzyme catalyzed it transamination with L isomer, but D isomer in natural form, inactive as substrate. Also other names of enzymes similar to this contains, L-3-aminoisobutyrate transaminase, beta-aminobutyric transaminase, L-3-aminoisobutyric aminotransferase, and beta-aminoisobutyrate-alpha-ketoglutarate transaminase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-3-amino-2-methylpropionate%20transaminase | In enzymology, a (S)-3-amino-2-methylpropionate transaminase () is an enzyme that catalyzes the chemical reaction
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate 2-methyl-3-oxopropanoate + L-glutamate
Thus, the two substrates of this enzyme are (S)-3-amino-2-methylpropanoate and 2-oxoglutarate, whereas its two products are 2-methyl-3-oxopropanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is (S)-3-amino-2-methylpropanoate:2-oxoglutarate aminotransferase. Other names in common use include L-3-aminoisobutyrate transaminase, beta-aminobutyric transaminase, L-3-aminoisobutyric aminotransferase, and beta-aminoisobutyrate-alpha-ketoglutarate transaminase. This enzyme participates in valine, leucine and isoleucine degradation.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Serine%E2%80%94glyoxylate%20transaminase | In enzymology, a serine-glyoxylate transaminase () is an enzyme that catalyzes the chemical reaction
L-serine + glyoxylate 3-hydroxypyruvate + glycine
Thus, the two substrates of this enzyme are L-serine and glyoxylate, whereas its two products are 3-hydroxypyruvate and glycine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:glyoxylate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Serine%E2%80%94pyruvate%20transaminase | In enzymology, a serine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-serine + pyruvate 3-hydroxypyruvate + L-alanine
Thus, the two substrates of this enzyme are L-serine and pyruvate, whereas its two products are 3-hydroxypyruvate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:pyruvate aminotransferase. Other names in common use include SPT, and hydroxypyruvate:L-alanine transaminase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Succinyldiaminopimelate%20transaminase | In enzymology, a succinyldiaminopimelate transaminase () is an enzyme that catalyzes the chemical reaction
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate
Thus, the two substrates of this enzyme are N-succinyl-L-2,6-diaminoheptanedioate and 2-oxoglutarate, whereas its two products are N-succinyl-L-2-amino-6-oxoheptanedioate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is N-succinyl-L-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include succinyldiaminopimelate aminotransferase, and N-succinyl-L-diaminopimelic glutamic transaminase. This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinylornithine%20transaminase | In enzymology, a succinylornithine transaminase () is an enzyme that catalyzes the chemical reaction
N2-succinyl-L-ornithine + 2-oxoglutarate N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are N2-succinyl-L-ornithine and 2-oxoglutarate, whereas its two products are N-succinyl-L-glutamate 5-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Other names in common use include succinylornithine aminotransferase, N2-succinylornithine 5-aminotransferase, AstC, SOAT, and 2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase. This enzyme participates in arginine and proline metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taurine%E2%80%942-oxoglutarate%20transaminase | In enzymology, a taurine-2-oxoglutarate transaminase () is an enzyme that catalyzes the chemical reaction.
taurine + 2-oxoglutarate sulfoacetaldehyde + L-glutamate
Thus, the two substrates of this enzyme are taurine and 2-oxoglutarate, whereas its two products are sulfoacetaldehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is taurine:2-oxoglutarate aminotransferase. Other names in common use include taurine aminotransferase, taurine transaminase, taurine-alpha-ketoglutarate aminotransferase, and taurine-glutamate transaminase. This enzyme participates in beta-alanine metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taurine%E2%80%94pyruvate%20aminotransferase | In enzymology, a taurine-pyruvate aminotransferase () is an enzyme that catalyzes the chemical reaction.
taurine + pyruvate L-alanine + 2-sulfoacetaldehyde
Thus, the two substrates of this enzyme are taurine and pyruvate, whereas its two products are L-alanine and 2-sulfoacetaldehyde.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is taurine:pyruvate aminotransferase. This enzyme is also called Tpa. This enzyme participates in taurine and hypotaurine metabolism.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thyroid-hormone%20transaminase | In enzymology, a thyroid-hormone transaminase () is an enzyme that catalyzes the chemical reaction
L-3,5,3'-triiodothyronine + 2-oxoglutarate 3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]-2-oxopropanoate + L-glutamate
Thus, the two substrates of this enzyme are L-3,5,3'-triiodothyronine and 2-oxoglutarate, whereas its two products are [[3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]-2-oxopropanoate]] and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-3,5,3'-triiodothyronine:2-oxoglutarate aminotransferase. Other names in common use include 3,5-dinitrotyrosine transaminase, and thyroid hormone aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tryptophan%E2%80%94phenylpyruvate%20transaminase | In enzymology, a tryptophan-phenylpyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-tryptophan + phenylpyruvate (indol-3-yl)pyruvate + L-phenylalanine
Thus, the two substrates of this enzyme are L-tryptophan and phenylpyruvate, whereas its two products are (indol-3-yl)pyruvate and L-phenylalanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-tryptophan:phenylpyruvate aminotransferase. This enzyme is also called L-tryptophan-alpha-ketoisocaproate aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tryptophan%20transaminase | In enzymology, a tryptophan transaminase () is an enzyme that catalyzes the chemical reaction
L-tryptophan + 2-oxoglutarate (indol-3-yl)pyruvate + L-glutamate
Thus, the two substrates of this enzyme are L-tryptophan and 2-oxoglutarate, whereas its two products are (indol-3-yl)pyruvate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-tryptophan:2-oxoglutarate aminotransferase. Other names in common use include L-phenylalanine-2-oxoglutarate aminotransferase, tryptophan aminotransferase, 5-hydroxytryptophan-ketoglutaric transaminase, hydroxytryptophan aminotransferase, L-tryptophan aminotransferase, and L-tryptophan transaminase. This enzyme participates in tryptophan metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-2-acetamido-4-amino-2%2C4%2C6-trideoxyglucose%20transaminase | In enzymology, an UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase () is an enzyme that catalyzes the chemical reaction
UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose + 2-oxoglutarate UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose + L-glutamate
Thus, the two substrates of this enzyme are UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose and 2-oxoglutarate, whereas its two products are UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase. Other names in common use include uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose, and aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
EC 2.6.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Valine%E2%80%943-methyl-2-oxovalerate%20transaminase | In enzymology, a valine-3-methyl-2-oxovalerate transaminase () is an enzyme that catalyzes the chemical reaction
L-valine + (S)-3-methyl-2-oxopentanoate 3-methyl-2-oxobutanoate + L-isoleucine
Thus, the two substrates of this enzyme are L-valine and (S)-3-methyl-2-oxopentanoate, whereas its two products are 3-methyl-2-oxobutanoate and L-isoleucine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-valine:(S)-3-methyl-2-oxopentanoate aminotransferase. Other names in common use include valine-isoleucine transaminase, valine-3-methyl-2-oxovalerate aminotransferase, alanine-valine transaminase, valine-2-keto-methylvalerate aminotransferase, and valine-isoleucine aminotransferase.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Valine%E2%80%94pyruvate%20transaminase | In enzymology, a valine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
L-valine + pyruvate 3-methyl-2-oxobutanoate + L-alanine
Thus, the two substrates of this enzyme are L-valine and pyruvate, whereas its two products are 3-methyl-2-oxobutanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-valine:pyruvate aminotransferase. Other names in common use include transaminase C, valine-pyruvate aminotransferase, and alanine-oxoisovalerate aminotransferase. This enzyme participates in valine, leucine and isoleucine biosynthesis.
References
EC 2.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nealbarbital | Nealbarbital (Censedal) is a barbiturate derivative developed by Aktiebolaget Pharmacia in the 1950s. It has sedative and hypnotic effects, and was used for the treatment of insomnia.
References
Barbiturates
Allyl compounds
GABAA receptor positive allosteric modulators |
https://en.wikipedia.org/wiki/GPRC5B | G-protein coupled receptor family C group 5 member B is a protein that in humans is encoded by the GPRC5B gene.
Function
The protein encoded by this gene is a member of the type 3 G protein-coupled receptor family. Members of this superfamily are characterized by a signature 7-transmembrane domain motif. The specific function of this protein is unknown; however, this protein may mediate the cellular effects of retinoic acid on the G protein signal transduction cascade.
See also
Retinoic acid-inducible orphan G protein-coupled receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Secretin%20receptor%20family | Secretin receptor family (class B GPCR subfamily) consists of secretin receptors regulated by peptide hormones from the glucagon hormone family. The family is different from adhesion G protein-coupled receptors.
The secretin-receptor family of GPCRs include vasoactive intestinal peptide receptors and receptors for secretin, calcitonin and parathyroid hormone/parathyroid hormone-related peptides. These receptors activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. The receptors in this family have 7 transmembrane helices, like rhodopsin-like GPCRs. However, there is no significant sequence identity between these two GPCR families and the secretin-receptor family has its own characteristic 7TM signature.
The secretin-receptor family GPCRs exist in many animal species. Data mining with the Pfam signature has identified members in fungi, although due to their presumed non-hormonal function they are more commonly referred to as Adhesion G protein-coupled receptors, making the Adhesion subfamily the more basal group. Three distinct sub-families (B1-B3) are recognized.
Subfamily B1
Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways.
Pituitary adenylate cyclase-activating polypeptide type 1 receptor
PACAPR (ADCYAP1R1)
Calcitonin receptor
CALCR
Corticotropin-releasing hormone receptor
CRHR1; CRHR2
Glucose-dependent insulinotropic polypeptide recept |
https://en.wikipedia.org/wiki/GPRC5C | G-protein coupled receptor family C group 5 member C is a protein that in humans is encoded by the GPRC5C gene.
Function
The protein encoded by this gene is a member of the type 3 G protein-coupled receptor family. Members of this superfamily are characterized by a signature 7-transmembrane domain motif. The specific function of this protein is unknown; however, this protein may mediate the cellular effects of retinoic acid on the G protein signal transduction cascade. Two transcript variants encoding different isoforms have been found for this gene.
See also
Retinoic acid-inducible orphan G protein-coupled receptor
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPRC5D | G-protein coupled receptor family C group 5 member D is a protein that in humans is encoded by the GPRC5D gene.
Function
The protein encoded by this gene is a member of the G protein-coupled receptor family; however, the specific function of this gene has not yet been determined.
See also
Retinoic acid-inducible orphan G protein-coupled receptor
References
Further reading
G protein-coupled receptors |
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