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https://en.wikipedia.org/wiki/Calpain-3 | Calpain-3 is a protein that in humans is encoded by the CAPN3 gene.
Function
Calpain, a heterodimer consisting of a large and a small subunit, is a major intracellular protease, although its function has not been well established. This gene encodes a muscle-specific member of the calpain large subunit family that specifically binds to titin. Mutations in this gene are associated with limb-girdle muscular dystrophies type 2A. Alternate promoters and alternative splicing result in multiple transcript variants encoding different isoforms and some variants are ubiquitously expressed.
In melanocytic cells CAPN3 gene expression may be regulated by MITF.
Interactions
CAPN3 has been shown to interact with Titin.
References
Further reading
External links
The MEROPS online database for peptidases and their inhibitors: C02.004
GeneReviews/NCBI/NIH/UW entry on Calpainopathy
LOVD mutation database: CAPN3
EF-hand-containing proteins |
https://en.wikipedia.org/wiki/1%2C2-dehydroreticulinium%20reductase%20%28NADPH%29 | In enzymology, a 1,2-dehydroreticulinium reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
(R)-reticuline + NADP 1,2-dehydroreticulinium + NADPH + H
Thus, the two substrates of this enzyme are (R)-reticuline and NADP, whereas its 3 products are 1,2-dehydroreticulinium, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-reticuline:NADP+ oxidoreductase. This enzyme is also called 1,2-dehydroreticulinium ion reductase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-Pyrroline-5-carboxylate%20dehydrogenase | In enzymology, a 1-pyrroline-5-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-1-pyrroline-5-carboxylate + NAD+ + 2 H2O L-glutamate + NADH + H+
The three substrates of this enzyme are (S)-1-pyrroline-5-carboxylate, NAD+, and H2O, whereas its three products are glutamate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-1-pyrroline-5-carboxylate:NAD+ oxidoreductase. Other names in common use include delta-1-pyrroline-5-carboxylate dehydrogenase, 1-pyrroline dehydrogenase, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylic acid dehydrogenase, L-pyrroline-5-carboxylate-NAD+ oxidoreductase, and 1-pyrroline-5-carboxylate:NAD+ oxidoreductase. This enzyme participates in glutamate metabolism and arginine and proline metabolism.
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , and .
Human gene
In human, the protein is encoded by ALDH4A1 gene.
References
EC 1.2.1
Oxidoreductases |
https://en.wikipedia.org/wiki/2%2C4-diaminopentanoate%20dehydrogenase | In enzymology, a 2,4-diaminopentanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
2,4-diaminopentanoate + H2O + NAD(P)+ 2-amino-4-oxopentanoate + NH3 + NAD(P)H + H+
The 4 substrates of this enzyme are 2,4-diaminopentanoate, H2O, NAD+, and NADP+, whereas its 5 products are 2-amino-4-oxopentanoate, NH3, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,4-diaminopentanoate:NAD(P)+ oxidoreductase (deaminating). This enzyme is also called 2,4-diaminopentanoic acid C4 dehydrogenase. This enzyme participates in 3 metabolic pathways: lysine degradation, arginine and proline metabolism, and d-arginine and d-ornithine metabolism.
References
EC 1.4.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxy-1%2C4-benzoquinone%20reductase | In enzymology, a 2-hydroxy-1,4-benzoquinone reductase () is an enzyme that catalyzes the chemical reaction
2-hydroxy-1,4-benzoquinone + NADH + H+ 1,2,4-trihydroxybenzene + NAD+
The 3 substrates of this enzyme are 2-hydroxy-1,4-benzoquinone, NADH, and H+, whereas its two products are 1,2,4-trihydroxybenzene and NAD+.
This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is 2-hydroxy-1,4-benzoquinone:NADH oxidoreductase. Other names in common use include hydroxybenzoquinone reductase, 1,2,4-trihydroxybenzene:NAD oxidoreductase, and NADH:2-hydroxy-1,4-benzoquinone oxidoreductase.
References
EC 1.6.5
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-oxopropyl-CoM%20reductase%20%28carboxylating%29 | In enzymology, a 2-oxopropyl-CoM reductase (carboxylating) () is an enzyme that catalyzes the chemical reaction
2-mercaptoethanesulfonate + acetoacetate + NADP+ 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
The 3 substrates of this enzyme are 2-mercaptoethanesulfonate, acetoacetate, and NADP+, whereas its 3 products are 2-(2-oxopropylthio)ethanesulfonate, CO2, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-mercaptoethanesulfonate, acetoacetate:NADP+ oxidoreductase (decarboxylating). Other names in common use include NADPH:2-(2-ketopropylthio)ethanesulfonate, oxidoreductase/carboxylase, and NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.8.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-aci-nitropropanoate%20oxidase | In enzymology, a 3-aci-nitropropanoate oxidase () is an enzyme that catalyzes the chemical reaction
3-aci-nitropropanoate + O2 + H2O 3-oxopropanoate + nitrite + H2O2
The 3 substrates of this enzyme are 3-aci-nitropropanoate, O2, and H2O, whereas its 3 products are 3-oxopropanoate, nitrite, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is 3-aci-nitropropanoate:oxygen oxidoreductase. This enzyme is also called propionate-3-nitronate oxidase. It employs one cofactor, FMN.
References
External links
EC 1.7.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/SnRNP70 | snRNP70 also known as U1 small nuclear ribonucleoprotein 70 kDa is a protein that in humans is encoded by the SNRNP70 gene. snRNP70 is a small nuclear ribonucleoprotein that associates with U1 spliceosomal RNA, forming the U1snRNP a core component of the spliceosome. The U1-70K protein and other components of the spliceosome complex form detergent-insoluble aggregates in both sporadic and familial human cases of Alzheimer's disease. U1-70K co-localizes with Tau in neurofibrillary tangles in Alzheimer's disease.
Interactions
snRNP70 has been shown to interact with ASF/SF2, SRPK1, and ZRANB2.
Role in autoimmunity
Antibodies towards snRNP70 are associated with mixed connective tissue disease.
References
Further reading
Protein complexes
Spliceosome
RNA splicing |
https://en.wikipedia.org/wiki/4-%28dimethylamino%29phenylazoxybenzene%20reductase | In enzymology, a 4-(dimethylamino)phenylazoxybenzene reductase () is an enzyme that catalyzes the chemical reaction
4-(dimethylamino)phenylazobenzene + NADP+ 4-(dimethylamino)phenylazoxybenzene + NADPH + H+
Thus, the two substrates of this enzyme are 4-(dimethylamino)phenylazobenzene and NADP+, whereas its 3 products are 4-(dimethylamino)phenylazoxybenzene, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-(dimethylamino)phenylazobenzene:NADP+ oxidoreductase. Other names in common use include N,N-dimethyl-p-aminoazobenzene oxide reductase, dimethylaminoazobenzene N-oxide reductase, NADPH-dependent DMAB N-oxide reductase, and NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase.
References
EC 1.7.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/HNF1B | HNF1 homeobox B (hepatocyte nuclear factor 1 homeobox B), also known as HNF1B or transcription factor 2 (TCF2), is a human gene.
Function
HNF1B encodes hepatocyte nuclear factor 1-beta, a protein of the homeobox-containing basic helix-turn-helix family. The HNF1B protein is believed to form heterodimers with another member of this transcription factor family, HNF1A; depending on the HNF1B isoform, the result may be to activate or inhibit transcription of target genes. Deficiency of HNF1B cause abnormal maternal-Zygote transition and early embryogenesis failure. Mutation of HNF1B that disrupts normal function has been identified as the cause of MODY 5 (Maturity-Onset of Diabetes, Type 5). A third human transcript variant is believed to exist based on such a variant in the rat: however, to date such an mRNA species has not been isolated.
See also
Hepatocyte nuclear factors
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/5%2C10-methylenetetrahydromethanopterin%20reductase | In enzymology, a 5,10-methylenetetrahydromethanopterin reductase () is an enzyme that catalyzes the chemical reaction
5-methyltetrahydromethanopterin + coenzyme F420 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
Thus, the two substrates of this enzyme are 5-methyltetrahydromethanopterin and coenzyme F420, whereas its two products are 5,10-methylenetetrahydromethanopterin and reduced coenzyme F420.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is 5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common use include 5,10-methylenetetrahydromethanopterin cyclohydrolase, N5,N10-methylenetetrahydromethanopterin reductase, methylene-H4MPT reductase, coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin, reductase, and N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. This enzyme participates in folate biosynthesis.
References
EC 1.5.98
Enzymes of known structure |
https://en.wikipedia.org/wiki/6%2C7-dihydropteridine%20reductase | In enzymology, 6,7-dihydropteridine reductase (, also Dihydrobiopterin reductase) is an enzyme that catalyzes the chemical reaction
5,6,7,8-tetrahydropteridine + NAD(P)+ 6,7-dihydropteridine + NAD(P)H + H+
The four substrates for this enzyme are a 6,7-dihydropteridine (dihydrobiopterin), NADH, NADPH, and H+ and its three products are 5,6,7,8-tetrahydropteridine (tetrahydrobiopterin), NAD+, and NADP+ This enzyme participates in folate biosynthesis. In the human genome, the enzyme is encoded by the QDPR gene.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase. Other names in common use include 6,7-dihydropteridine:NAD(P)H oxidoreductase, DHPR, NAD(P)H:6,7-dihydropteridine oxidoreductase, NADH-dihydropteridine reductase, NADPH-dihydropteridine reductase, NADPH-specific dihydropteridine reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide), reductase, dihydropteridine reductase, dihydropteridine reductase (NADH), and 5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase.
Clinical significance
Dihydropteridine reductase deficiency is a defect in the regeneration of tetrahydrobiopterin. Many patients have significant developmental delays despite therapy, develop brain abnormalities, and are prone to sudden death. The reason is not completely clear, but might be |
https://en.wikipedia.org/wiki/TP53BP1 | Tumor suppressor p53-binding protein 1 also known as p53-binding protein 1 or 53BP1 is a protein that in humans is encoded by the TP53BP1 gene.
Clinical significance
53BP1 is underexpressed in most cases of triple-negative breast cancer.
DNA repair
DNA double-strand breaks (DSBs) are cytotoxic damages that can be repaired either by the homologous recombinational repair (HR) pathway or by the non-homologous end-joining (NHEJ) pathway. NHEJ, although faster than HR, is less accurate. The early divergent step between the two pathways is end resection, and this step is regulated by numerous factors. In particular, BRCA1 and 53BP1 play a role in determining the balance between the two pathways. 53BP1 restricts resection and promotes NHEJ.
Age-associated deficient repair
Ordinarily during the G1 phase of the cell cycle, when a sister chromatid is unavailable for HR, NHEJ is the predominant pathway for repairing DNA double-strand breaks (DSBs). However, as individuals age, recruitment of 53BP1 to DSBs during G1 becomes deficient. The absence of 53BP1 at such DSBs appears to promote the alternative error-prone repair process Alt-EJ. This repair process, also referred to as microhomology-mediated end joining, is highly inaccurate and likely contributes to the aging process.
Interactions
53BP1 has been shown to physically interact with:
Histone H4 dimethylated or monomethylated at Lysine 20
Histone H2A or Histone H2A.X ubiquitinated at Lysine 15
p53
DYNLL1
Referen |
https://en.wikipedia.org/wiki/Acetylindoxyl%20oxidase | Acetylindoxyl oxidase () is an enzyme that catalyzes the chemical reaction
N-acetylindoxyl + O2 N-acetylisatin + (?)
Thus, the two substrates of this enzyme are N-acetylindoxyl and oxygen, whereas its product is N-acetylisatin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is N-acetylindoxyl:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism.
References
EC 1.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenylyl-sulfate%20reductase | Adenylyl-sulfate reductase () is an enzyme that catalyzes the chemical reaction of the reduction of adenylyl-sulfate/adenosine-5'-phosphosulfate (APS) to sulfite through the use of an electron donor cofactor. The products of the reaction are AMP and sulfite, as well as an oxidized electron donor cofactor.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other acceptors. The systematic name of this enzyme class is AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming). Other names in common use include adenosine phosphosulfate reductase, adenosine 5'-phosphosulfate reductase, APS-reductase, APS reductase, AMP, sulfite:(acceptor) oxidoreductase, and (adenosine-5'-phosphosulfate-forming). This enzyme participates in selenium metabolism and sulfur metabolism.
Mechanism
APS reductase catalyzes the reversible transformation of APS to sulfite and AMP, which is the rate determining step of the overall reaction. The reaction catalyzed by APS reductase is as follows:
Sulfate has to be activated to APS by ATP sulfurylase at the expense of one ATP, hence this reaction requires an input of energy. The reaction above occurs in a strictly anaerobic environment. The two electrons come from a reduced cofactor, in this case reduced FAD. The forward direction requires one AMP molecule; however, research suggests that the reverse reaction requires two AMP molecules (one acting on the substra |
https://en.wikipedia.org/wiki/Adenylyl-sulfate%20reductase%20%28glutathione%29 | Adenylyl-sulfate reductase (glutathione) () is an enzyme that catalyzes the chemical reaction
AMP + sulfite + glutathione disulfide adenylyl sulfate + 2 glutathione
The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and glutathione disulfide, whereas its two products are adenylyl sulfate and glutathione.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). Other names in common use include 5'-adenylylsulfate reductase (also used for, internal_xref(ec_num(1,8,99,2))), AMP,sulfite:oxidized-glutathione oxidoreductase, (adenosine-5'-phosphosulfate-forming), and plant-type 5'-adenylylsulfate reductase. In plants, APS is reduced by the plastidic enzyme APS reductase (APR; EC 1.8.4.9) in the presence of physiological concentrations of reduced glutathione (GSH), which acts as an electron donor.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenylyl-sulfate%20reductase%20%28thioredoxin%29 | Adenylyl-sulfate reductase (thioredoxin) () is an enzyme that catalyzes the chemical reaction
AMP + sulfite + thioredoxin disulfide 5'-adenylyl sulfate + thioredoxin
The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and thioredoxin disulfide, whereas its two products are 5'-adenylyl sulfate and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor.
This enzyme also assists a feature of the Calvin-Benson cycle's light regulation within the ferredoxin-thioredoxin system in the form of reduced thioredoxin. Thioredoxin-type adenylyl-sulfate reductase also uses thioredoxin as an electron donor in reactions related to protein synthesis. Note this is a general pathway and other resemblances are studied in literature to support this.
The enzyme functions in reactions that in the end stabilize Thiols in related bonds that end up forming a dithiol group as a byproduct.
Nomenclature
The systematic name of this enzyme class is AMP, sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). This enzyme is also called thioredoxin-dependent 5'-adenylylsulfate reductase.
Classication
This enzyme (Adenylyl-sulfate reductase) is an oxidoreductase (Class 1) or more specifically a sulfur oxidoreductase (Sub-Class 8) disulfide (Sub-Subclass 4). The enzyme bears the serial number of 10 under the EC naming system. The primary difference that this par |
https://en.wikipedia.org/wiki/ACTR2 | Actin-related protein 2 is a protein that in humans is encoded by the ACTR2 gene.
The specific function of ACTR2 has not yet been determined. However, it is known to be a major constituent of the ARP2/3 complex. This complex is located at the cell surface and is essential to cell shape and motility through lamellipodial actin assembly and protrusion. Two transcript variants encoding different isoforms have been found for this gene.
References
Further reading
External links
Human proteins |
https://en.wikipedia.org/wiki/Alanine%20dehydrogenase | Alanine dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-alanine + H2O + NAD+ pyruvate + NH3 + NADH + H+
The 2 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+ because water is 55M and does not change, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion.
This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle ( fixation).
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase (deaminating). Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. T
Structure
Alanine dehydrogenase contains both a N-terminus and C-terminus domains.
References
Further reading
EC 1.4.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Alanopine%20dehydrogenase | Alanopine dehydrogenase () is an enzyme that catalyzes the chemical reaction
2,2'-iminodipropanoate + NAD+ + H2O L-alanine + pyruvate + NADH + H+
The 2 substrates of this enzyme are 2,2'-iminodipropanoate, and nicotinamide adenine dinucleotide+. water is excluded since water is 55M and does not change. Its 4 products are L-alanine, pyruvate, nicotinamide adenine dinucleotide, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming). Other names in common use include ALPDH, alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase, meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase, alanopine: NAD+ oxidoreductase, ADH, and alanopine:NAD+ oxidoreductase.
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Amine%20oxidase%20%28copper-containing%29 | Amine oxidase (copper-containing) (AOC) ( and ; formerly ) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
RCH2NH2 + H2O + O2 RCHO + NH3 + H2O2
The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2.
Copper-containing amine oxidases are found in bacteria, fungi, plants and animals. In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen.
This enzyme belongs to oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). This enzyme participates in 8 metabolic pathways: urea cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, beta-alanine metabolism, and alkaloid biosynthesis ii. It has 2 cofactors: copper, and PQQ.
Structure
The copper amine oxidase 3-dimensional structure |
https://en.wikipedia.org/wiki/Neutrophil%20cytosolic%20factor%201 | Neutrophil cytosol factor 1, also known as p47phox, is a protein that in humans is encoded by the NCF1 gene.
Function
The protein encoded by this gene is a 47 kDa cytosolic subunit of neutrophil NADPH oxidase. This oxidase is a multicomponent enzyme that is activated to produce superoxide anion. Mutations in this gene have been associated with chronic granulomatous disease.
Genetic variability in the NCF1 gene has been found to be related to a higher chance of getting autoimmune diseases such as Sjögren's syndrome, rheumatoid arthritis and lupus erythematosus.
p47 is vital to the activation of NADPH oxidase. P47 becomes heavily phosphorylated
Interactions
Neutrophil cytosolic factor 1 has been shown to interact with:
Moesin,
Neutrophil cytosolic factor 4, and
RELA.
References
Further reading |
https://en.wikipedia.org/wiki/Asparagusate%20reductase | Asparagusate reductase () is an enzyme that catalyzes the chemical reaction
3-mercapto-2-mercaptomethylpropanoate + NAD+ asparagusate + NADH + H+
Thus, the two substrates of this enzyme are 3-mercapto-2-mercaptomethylpropanoate and nicotinamide adenine dinucleotide ion, whereas its 3 products are asparagusate, nicotinamide adenine dinucleotide, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-mercapto-2-mercaptomethylpropanoate:NAD+ oxidoreductase. Other names in common use include asparagusate dehydrogenase, asparagusic dehydrogenase, asparagusate reductase (NADH2), and NADH2:asparagusate oxidoreductase.
References
EC 1.8.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%20dehydrogenase | Aspartate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-aspartate + H2O + NAD(P)+ oxaloacetate + NH3 + NAD(P)H + H+
The 4 substrates of this enzyme are L-aspartate, water, nicotinamide adenine dinucleotide ion, and nicotinamide adenine dinucleotide phosphate ion, whereas its 5 products are oxaloacetate, ammonia, NADH, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-aspartate:NAD(P)+ oxidoreductase (deaminating). Other names in common use include NAD-dependent aspartate dehydrogenase, NADH2-dependent aspartate dehydrogenase, and NADP+-dependent aspartate dehydrogenase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.4.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Azobenzene%20reductase | Azobenzene reductase also known as azoreductase () is an enzyme that catalyzes the chemical reaction:
N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+ 4-(dimethylamino)azobenzene + NADPH + H+
The 3 substrates of this enzyme are N,N-dimethyl-1,4-phenylenediamine, aniline, and nicotinamide adenine dinucleotide phosphate ion, whereas its 3 products are 4-(dimethylamino)azobenzene, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor.
Mechanism
The reaction catalyzed by this enzyme proceeds via a ping-pong mechanism by using 2 equivalents of NAD(P)H to reduce one equivalent of the azo compound substrate (for example methyl red where Ar = p-dimethylaniline and Ar' = o-benzoic acid) into two equivalents of aniline product:
Ar–N=N–Ar' + 2(NAD(P)H + H+) Ar–NH2 + NH2–Ar' + 2NAD(P)+
Substrate specificity
Most azoreductase isoenzymes can reduce methyl red, but are not able to reduce sulfonated azo dyes. The unique azoreductase isozyme from Bacillus sp. B29 has the ability to reduce sulfonated azo dyes however.
Nomenclature
The systematic name of this enzyme class is N,N-dimethyl-1,4-phenylenediamine, aniline:NADP+ oxidoreductase. Other names in common use include:
azo reductase,
azoreductase,
azo-dye reductase,
dibromopropylaminophenylazobenzoic azoreductase,
dimethylaminobenzene reductase,
methyl |
https://en.wikipedia.org/wiki/Berberine%20reductase | Berberine reductase () is an enzyme that catalyzes the chemical reaction
(R)-canadine + 2 NADP+ berberine + 2 NADPH + H+
Thus, the two substrates of this enzyme are (R)-canadine and nicotinamide adenine dinucleotide phosphate ion, whereas its 3 products are berberine, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-tetrahydroberberine:NADP+ oxidoreductase. This enzyme is also called (R)-canadine synthase.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure
sr:Flavin reduktaza |
https://en.wikipedia.org/wiki/Beta-alanopine%20dehydrogenase | Beta-alanopine dehydrogenase () is an enzyme that catalyzes the chemical reaction
beta-alanopine + NAD+ + H2O beta-alanine + pyruvate + NADH + H+
The 3 substrates of this enzyme are beta-alanopine, nicotinamide adenine dinucleotide ion, and water, whereas its 4 products are beta-alanine, pyruvate, nicotinamide adenine dinucleotide, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-(D-1-carboxyethyl)-beta-alanine:NAD+ oxidoreductase (beta-alanine-forming).
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bis-gamma-glutamylcystine%20reductase | Bis-gamma-glutamylcystine reductase () is an enzyme that catalyzes the chemical reaction
2 gamma-glutamylcysteine + NADP+ bis-gamma-glutamylcystine + NADPH + H+
Thus, the two substrates of this enzyme are gamma-glutamylcysteine and nicotinamide adenine dinucleotide phosphate ion, whereas its 3 products are bis-gamma-glutamylcystine, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is gamma-glutamylcysteine:NADP+ oxidoreductase. This enzyme is also called NADPH2:bis-gamma-glutamylcysteine oxidoreductase. This enzyme participates in glutathione metabolism.
References
EC 1.8.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CoA-disulfide%20reductase | In enzymology, a CoA-disulfide reductase () is an enzyme that catalyzes the chemical reaction
2 CoA + NAD(P)+ CoA-disulfide + NAD(P)H + H+
The 3 substrates of this enzyme are CoA, NAD+, and NADP+, whereas its 4 products are CoA-disulfide, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is CoA:NAD(P)+ oxidoreductase. Other names in common use include CoA-disulfide reductase (NADH2), NADH2:CoA-disulfide oxidoreductase, CoA:NAD+ oxidoreductase, CoADR, and coenzyme A disulfide reductase.
References
EC 1.8.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CoA-glutathione%20reductase | In enzymology, a CoA-glutathione reductase () is an enzyme that catalyzes the chemical reaction
CoA + glutathione + NADP+ CoA-glutathione + NADPH + H+
The 3 substrates of this enzyme are CoA, glutathione, and NADP+, whereas its 3 products are CoA-glutathione, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glutathione:NADP+ oxidoreductase (CoA-acylating). Other names in common use include coenzyme A glutathione disulfide reductase, NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione oxidoreductase. This enzyme participates in cysteine metabolism. It employs one cofactor, FAD.
References
EC 1.8.1
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CoB%E2%80%94CoM%20heterodisulfide%20reductase | In enzymology, a CoB—CoM heterodisulfide reductase () is an enzyme that catalyzes the chemical reaction
coenzyme B + coenzyme M + methanophenazine N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine + dihydromethanophenazine
The 3 substrates of this enzyme are coenzyme B, coenzyme M, and methanophenazine, whereas its two products are [[N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine]] and dihydromethanophenazine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other, known, acceptors. The systematic name of this enzyme class is coenzyme B:coenzyme M:methanophenazine oxidoreductase. Other names in common use include heterodisulfide reductase, and soluble heterodisulfide reductase. This enzyme participates in folate biosynthesis.
References
EC 1.8.98
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexylamine%20oxidase | In enzymology, a cyclohexylamine oxidase () is an enzyme that catalyzes the chemical reaction
cyclohexylamine + O2 + H2O cyclohexanone + NH3 + H2O2
The 3 substrates of this enzyme are cyclohexylamine, O2, and H2O, whereas its 3 products are cyclohexanone, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is cyclohexylamine:oxygen oxidoreductase (deaminating). This enzyme participates in caprolactam degradation. It employs one cofactor, FAD.
References
EC 1.4.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cystine%20reductase | In enzymology, a cystine reductase () is an enzyme that catalyzes the chemical reaction
2 L-cysteine + NAD+ L-cystine + NADH + H+
Thus, the two substrates of this enzyme are L-cysteine and NAD+, whereas its 3 products are L-cystine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-cysteine:NAD+ oxidoreductase. Other names in common use include cystine reductase (NADH), NADH-dependent cystine reductase, cystine reductase (NADH2), and NADH2:L-cystine oxidoreductase. This enzyme participates in cysteine metabolism.
References
EC 1.8.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cytokinin%20dehydrogenase | In enzymology, a cytokinin dehydrogenase () is an enzyme that catalyzes the chemical reaction
N6-dimethylallyladenine + electron acceptor + H2O adenine + 3-methylbut-2-enal + reduced acceptor
The 3 substrates of this enzyme are cytokinin (here represented by N6-dimethylallyladenine), electron acceptor, and H2O, whereas its 3 products are adenine, 3-methylbut-2-enal (or other aldehyde in case of different substrate), and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is N6-dimethylallyladenine:acceptor oxidoreductase. Other names in common use include ''N''6-dimethylallyladenine:(acceptor) oxidoreductase, 6-N-dimethylallyladenine:acceptor oxidoreductase, and cytokinin oxidase/dehydrogenase abbreviated as CKX.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
As of March 2016, there have been 18 structures deposited to PDB. 16 of these were of enzymes from maize and two from Arabidopsis.
References
EC 1.5.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-aspartate%20oxidase | In enzymology, a D-aspartate oxidase () is an enzyme that catalyzes the chemical reaction
D-aspartate + H2O + O2 oxaloacetate + NH3 + H2O2
The 3 substrates of this enzyme are D-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2.
This enzyme belongs to the FAD dependent oxidoreductase family, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-aspartate:oxygen oxidoreductase (deaminating). Other names in common use include aspartic oxidase, and D-aspartic oxidase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, FAD.
The enzyme is encoded by DDO gene.
See also
DAO
Diamine oxidase
D-amino acid oxidase
References
EC 1.4.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta1-piperideine-2-carboxylate%20reductase | In enzymology, a Delta1-piperideine-2-carboxylate reductase () is an enzyme that catalyzes the chemical reaction
L-pipecolate + NADP+ Delta1-piperideine-2-carboxylate + NADPH + H+
Thus, the two substrates of this enzyme are L-pipecolate and NADP+, whereas its 3 products are Delta1-piperideine-2-carboxylate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-pipecolate:NADP+ 2-oxidoreductase. Other names in common use include 1,2-didehydropipecolate reductase, P2C reductase, and 1,2-didehydropipecolic reductase. This enzyme participates in lysine degradation.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-glutamate%28D-aspartate%29%20oxidase | In enzymology, a D-glutamate(D-aspartate) oxidase () is an enzyme that catalyzes the chemical reaction
D-glutamate + H2O + O2 2-oxoglutarate + NH3 + H2O2
The 3 substrates of this enzyme are D-glutamate, H2O, and O2, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-glutamate(D-aspartate):oxygen oxidoreductase (deaminating). Other names in common use include D-glutamic-aspartic oxidase, and D-monoaminodicarboxylic acid oxidase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, FAD.
References
EC 1.4.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-glutamate%20oxidase | In enzymology, a D-glutamate oxidase () is an enzyme that catalyzes the chemical reaction
D-glutamate + H2O + O2 2-oxoglutarate + NH3 + H2O2
The 3 substrates of this enzyme are D-glutamate, H2O, and O2, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-glutamate:oxygen oxidoreductase (deaminating). Other names in common use include D-glutamic oxidase, and D-glutamic acid oxidase. This enzyme participates in d-glutamine and d-glutamate metabolism.
References
EC 1.4.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diaminopimelate%20dehydrogenase | In enzymology, a diaminopimelate dehydrogenase () is an enzyme that catalyzes the chemical reaction
meso-2,6-diaminoheptanedioate + H2O + NADP+ L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+
The 3 substrates of this enzyme are meso-2,6-diaminoheptanedioate, H2O, and NADP+, whereas its 4 products are L-2-amino-6-oxoheptanedioate, NH3, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is meso-2,6-diaminoheptanedioate:NADP+ oxidoreductase (deaminating). Other names in common use include meso-alpha,epsilon-diaminopimelate dehydrogenase, and meso-diaminopimelate dehydrogenase. This enzyme participates in lysine biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.4.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dimethylamine%20dehydrogenase | In enzymology, a dimethylamine dehydrogenase () is an enzyme that catalyzes the chemical reaction
dimethylamine + H2O + electron-transferring flavoprotein methylamine + formaldehyde + reduced electron-transferring flavoprotein
The 3 substrates of this enzyme are dimethylamine, H2O, and electron-transferring flavoprotein, whereas its 3 products are methylamine, formaldehyde, and reduced electron-transferring flavoprotein.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a flavin as acceptor. The systematic name of this enzyme class is dimethylamine:electron-transferring flavoprotein oxidoreductase. This enzyme participates in methane metabolism. It employs one cofactor, FMN.
References
EC 1.5.8
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylglycine%20dehydrogenase | In enzymology, a dimethylglycine dehydrogenase () is an enzyme that catalyzes the chemical reaction
N,N-dimethylglycine + acceptor + H2O sarcosine + formaldehyde + reduced acceptor
The 3 substrates of this enzyme are N,N-dimethylglycine, acceptor, and H2O, whereas its 3 products are sarcosine, formaldehyde, and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is N,N-dimethylglycine:acceptor oxidoreductase (demethylating). Other names in common use include N,N-dimethylglycine oxidase, and N,N-dimethylglycine:(acceptor) oxidoreductase (demethylating). This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, FAD.
References
EC 1.5.8
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylglycine%20oxidase | In enzymology, a dimethylglycine oxidase () is an enzyme that catalyzes the chemical reaction
N,N-dimethylglycine + H2O + O2 sarcosine + formaldehyde + H2O2
The 3 substrates of this enzyme are N,N-dimethylglycine, H2O, and O2, whereas its 3 products are sarcosine, formaldehyde, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N,N-dimethylglycine:oxygen oxidoreductase (demethylating). It employs one cofactor, FAD.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.5.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-lysopine%20dehydrogenase | In enzymology, a D-lysopine dehydrogenase () is an enzyme that catalyzes the chemical reaction
N2-(D-1-carboxyethyl)-L-lysine + NADP+ + H2O L-lysine + pyruvate + NADPH + H+
The 3 substrates of this enzyme are N2-(D-1-carboxyethyl)-L-lysine, NADP+, and H2O, whereas its 4 products are L-lysine, pyruvate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N2-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming). Other names in common use include D-lysopine synthase, lysopine dehydrogenase, D(+)-lysopine dehydrogenase, 2-N-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase, and (L-lysine-forming). This enzyme participates in lysine degradation.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-nopaline%20dehydrogenase | In enzymology, a D-nopaline dehydrogenase () is an enzyme that catalyzes the chemical reaction
N2-(D-1,3-dicarboxypropyl)-L-arginine + NADP+ + H2O L-arginine + 2-oxoglutarate + NADPH + H+
The 3 substrates of this enzyme are N2-(D-1,3-dicarboxypropyl)-L-arginine, NADP+, and H2O, whereas its 4 products are L-arginine, 2-oxoglutarate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N2-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming). Other names in common use include D-nopaline synthase, nopaline dehydrogenase, nopaline synthase, NOS, 2-N-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase, and (L-arginine-forming). This enzyme participates in arginine and proline metabolism.
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-octopine%20dehydrogenase | Octopine dehydrogenase (N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase, OcDH, ODH) is a dehydrogenase enzyme in the opine dehydrogenase family that helps maintain redox balance under anaerobic conditions. It is found largely in aquatic invertebrates, especially mollusks, sipunculids, and coelenterates, and plays a role analogous to lactate dehydrogenase (found largely in vertebrates)
. In the presence of NADH, OcDH catalyzes the reductive condensation of an α-keto acid with an amino acid to form N-carboxyalkyl-amino acids (opines). The purpose of this reaction is to reoxidize glycolytically formed NADH to NAD+, replenishing this important reductant used in glycolysis and allowing for the continued production of ATP in the absence of oxygen.
L-arginine + pyruvate + NADH + H+ D-octopine + NAD+ + H2O
Structure
OcDH is a monomer with a molecular weight of 38kD made of two functionally distinct subunits. The first, Domain I, is composed of 199 amino acids and contains a Rossmann fold. Domain II is composed of 204 amino acids and is connected to the Rossmann fold of Domain I via its N-terminus.
Mechanism
Isothermal titration calorimetry (ITR), nuclear magnetic resonance (NMR)
crystallography, and clonal studies of OcDH and its substrates have led to the identification of the enzyme reaction mechanism. First, the Rossmann fold in Domain I of OcDH binds NADH. Binding of NADH to the Rossmann fold triggers small conformational change typical in the binding of NADH to most |
https://en.wikipedia.org/wiki/Enzyme-thiol%20transhydrogenase%20%28glutathione-disulfide%29 | In enzymology, an enzyme-thiol transhydrogenase (glutathione-disulfide) () is an enzyme that catalyzes the chemical reaction
[xanthine dehydrogenase] + glutathione disulfide [xanthine oxidase] + 2 glutathione
Thus, the two substrates of this enzyme are xanthine dehydrogenase and glutathione disulfide, whereas its two products are xanthine oxidase and glutathione.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase. Other names in common use include [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase, enzyme-thiol transhydrogenase (oxidized-glutathione), glutathione-dependent thiol:disulfide oxidoreductase, and thiol:disulfide oxidoreductase. This enzyme participates in glutathione metabolism.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ethanolamine%20oxidase | In enzymology, an ethanolamine oxidase () is an enzyme that catalyzes the chemical reaction
ethanolamine + H2O + O2 glycolaldehyde + NH3 + H2O2
The 3 substrates of this enzyme are ethanolamine, H2O, and O2, whereas its 3 products are glycolaldehyde, NH3, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is ethanolamine:oxygen oxidoreductase (deaminating). It has 2 cofactors: cobalt, and Cobamide.
References
EC 1.4.3
Cobalt enzymes
Cobamide enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ferredoxin%E2%80%94nitrate%20reductase | In enzymology, a ferredoxin—nitrate reductase () is an enzyme that catalyzes the chemical reaction
nitrite + H2O + 2 oxidized ferredoxin nitrate + 2 reduced ferredoxin + 2 H+
The 3 substrates of this enzyme are nitrite, H2O, and oxidized ferredoxin, whereas its 3 products are nitrate, reduced ferredoxin, and H+. Nitrate Reductase is an essential enzyme present in most biological systems such as green plants, certain fungi, yeasts and bacteria that aids in the reduction of nitrate to ammonium.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is nitrite:ferredoxin oxidoreductase. Other names in common use include assimilatory nitrate reductase, nitrate (ferredoxin) reductase, and assimilatory ferredoxin-nitrate reductase. This enzyme participates in nitrogen metabolism. It has 4 cofactors: iron, Sulfur, Molybdenum, and Iron-sulfur. The Iron-Sulfur cluster ([4FE-4S]) in this enzyme has a variety of different functions that contribute to the growth of aerobic cells. Some of the functions include but are not limited to the following: involved in photosynthetic processes, electron-transfer reactions and the binding of certain substrates, resulting in activation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
Further reading
|
https://en.wikipedia.org/wiki/Ferredoxin%E2%80%94nitrite%20reductase | In enzymology, a ferredoxin—nitrite reductase () is an enzyme that catalyzes the chemical reaction
NH3 + 2 H2O + 6 oxidized ferredoxin nitrite + 6 reduced ferredoxin + 7 H+
The 3 substrates of this enzyme are NH3, H2O, and oxidized ferredoxin, whereas its 3 products are nitrite, reduced ferredoxin, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is ammonia:ferredoxin oxidoreductase. This enzyme participates in nitrogen metabolism and nitrogen assimilation. It has 3 cofactors: iron, Siroheme, and Iron-sulfur.
This enzyme can use many different isoforms of ferredoxin. In photosynthesizing tissues, it uses ferredoxin that is reduced by PSI and in the root it uses a form of ferredoxin (FdIII) that has a less negative midpoint potential and can be reduced easily by NADPH.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
Literature
EC 1.7.7
Iron enzymes
Siroheme enzymes
Iron-sulfur enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Flavin%20reductase | Flavin reductase a class of enzymes. There are a variety of flavin reductases, (i.e. FRP, FRE, FRG, etc.) which bind free flavins and through hydrogen bonding, catalyze the reduction of these molecules to a reduced flavin. Riboflavin, or vitamin B, and flavin mononucleotide are two of the most well known flavins in the body and are used in a variety of processes which include metabolism of fat and ketones and the reduction of methemoglobin in erythrocytes. Flavin reductases are similar and often confused for ferric reductases because of their similar catalytic mechanism and structures.
In enzymology, a flavin reductase () is an enzyme that catalyzes the chemical reaction
riboflavin + NADPH + H+ reduced riboflavin + NADP + H+
Thus, the two products of this enzyme are reduced riboflavin and NADP+, whereas its 3 substrates are riboflavin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is reduced-riboflavin:NADP+ oxidoreductase. Other names in common use include NADPH:flavin oxidoreductase, riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide, phosphate) reductase, flavin mononucleotide reductase, flavine mononucleotide reductase, FMN reductase (NADPH), NADPH-dependent FMN reductase, NADPH-flavin reductase, NADPH-FMN reductase, NADPH-specific FMN reductase, riboflavin mononucleotide reductase, riboflavine mon |
https://en.wikipedia.org/wiki/FMN%20reductase | In enzymology, an FMN reductase () is an enzyme that catalyzes the chemical reaction
FMNH2 + NAD(P)+ FMN + NAD(P)H + H+
The 3 substrates of this enzyme are FMNH2, NAD+, and NADP+, whereas its 4 products are FMN, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is FMNH2:NAD(P)+ oxidoreductase. Other names in common use include NAD(P)H-FMN reductase, NAD(P)H-dependent FMN reductase, NAD(P)H:FMN oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H2 dehydrogenase (FMN), NAD(P)H2:FMN oxidoreductase, SsuE, riboflavin mononucleotide reductase, flavine mononucleotide reductase, riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide, (phosphate)) reductase, flavin mononucleotide reductase, and riboflavine mononucleotide reductase.
References
EC 1.5.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formyltetrahydrofolate%20dehydrogenase | In enzymology, a formyltetrahydrofolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
10-formyltetrahydrofolate + NADP+ + H2O tetrahydrofolate + CO2 + NADPH + H+
The 3 substrates of this enzyme are 10-formyltetrahydrofolate, NADP+, and H2O, whereas its 4 products are tetrahydrofolate, CO2, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-formyltetrahydrofolate:NADP+ oxidoreductase. Other names in common use include 10-formyl tetrahydrofolate:NADP oxidoreductase, 10-formyl-H2PtGlu:NADP oxidoreductase, 10-formyl-H4folate dehydrogenase, N10-formyltetrahydrofolate dehydrogenase, and 10-formyltetrahydrofolate dehydrogenase. This enzyme participates in one carbon pool by folate.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 1.5.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamate%20synthase%20%28ferredoxin%29 | In enzymology, a glutamate synthase (ferredoxin) () is an enzyme that catalyzes the chemical reaction
2 L-glutamate + 2 oxidized ferredoxin L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Thus, the two substrates of this enzyme are L-glutamate and oxidized ferredoxin, whereas its 4 products are L-glutamine, 2-oxoglutarate, reduced ferredoxin, and H+.
Classification
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with an iron-sulfur protein as acceptor.
Nomenclature
The systematic name of this enzyme class is L-glutamate:ferredoxin oxidoreductase (transaminating). Other names in common use include:
ferredoxin-dependent glutamate synthase,
ferredoxin-glutamate synthase,
glutamate synthase (ferredoxin-dependent), and
ferredoxin-glutamine oxoglutarate aminotransferase (Fd-GOGAT).
Biological role
This enzyme participates in nitrogen metabolism. It has 5 cofactors: FAD, iron, sulfur, iron-sulfur, and flavoprotein.
See also
Glutamate synthase (NADH)
Glutamate synthase (NADPH)
References
Flavoproteins
Iron enzymes
Sulfur enzymes
Iron-sulfur enzymes
Enzymes of known structure
EC 1.4.7 |
https://en.wikipedia.org/wiki/Glutamate%20synthase%20%28NADH%29 | In enzymology, a glutamate synthase (NADH) () is an enzyme that catalyzes the chemical reaction
2 L-glutamate + NAD+ L-glutamine + 2-oxoglutarate + NADH + H+
Glutamate synthase facilitates the ammonium assimilation pathway, which follows the enzymes, nitrite reductase and glutamine synthase. An ammonium produced by the nitrite reductase reaction will be incorporated into carbon skeleton backbone by glutamine synthase. Glutamine will be produced because of the introduction of ammonium in the carbon backbone, which can be converted into glutamate by glutamate synthase of another pathway.
These processes are common in plant roots due to the fact that if the nitrogen deficient conditions exist (with access to ammonium and nitrate ions), there will be a first priority of ammonium uptake. Thus, the two substrates of this enzyme are L-glutamate and NAD+, whereas its 4 products are L-glutamine, 2-oxoglutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in glutamate metabolism and nitrogen assimilation. It employs one cofactor, FMN.
Nomenclature
The systematic name of this enzyme class is L-glutamate:NAD+ oxidoreductase (transaminating). Other names in common use include:
glutamate (reduced nicotinamide adenine dinucleotide) synthase,
glutamate synthase (NADH),
L-glutamate synthetase(NADH),
NADH-dependent glutamate synthase,
NADH-g |
https://en.wikipedia.org/wiki/Glutamate%20synthase%20%28NADPH%29 | In enzymology, a glutamate synthase (NADPH) () is an enzyme that catalyzes the chemical reaction
L-glutamine + 2-oxoglutarate + NADPH + H+ 2 L-glutamate + NADP+
Thus, the four substrates of this enzyme are L-glutamine, 2-oxoglutarate (α-ketoglutarate), NADPH, and H+, whereas the two products are L-glutamate and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in glutamate metabolism and nitrogen metabolism. It has 5 cofactors: FAD, Iron, FMN, Sulfur, and Iron-sulfur.
It occurs in bacteria and plants but not animals, and is important as it provides glutamate for the glutamine synthetase reaction.
Nomenclature
The systematic name of this enzyme class is L-glutamate:NADP+ oxidoreductase (transaminating). Other names in common use include:
glutamate (reduced nicotinamide adenine dinucleotide phosphate), synthase,
glutamate synthase (NADPH),
glutamate synthetase (NADP),
glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP),
glutamine-ketoglutaric aminotransferase,
L-glutamate synthase,
L-glutamate synthetase,
L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing,
NADPH-dependent glutamate synthase,
NADPH-glutamate synthase, and
NADPH-linked glutamate synthase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
See also
Glutamate s |
https://en.wikipedia.org/wiki/Glutathione%E2%80%94CoA-glutathione%20transhydrogenase | In enzymology, a glutathione—CoA-glutathione transhydrogenase () is an enzyme that catalyzes the chemical reaction
CoA + glutathione disulfide CoA-glutathione + glutathione
Thus, the two substrates of this enzyme are CoA and glutathione disulfide, whereas its two products are CoA-glutathione and glutathione.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is CoA:glutathione-disulfide oxidoreductase. Other names in common use include glutathione-coenzyme A glutathione disulfide transhydrogenase, glutathione-coenzyme A glutathione disulfide transhydrogenase, glutathione coenzyme A-glutathione transhydrogenase, glutathione:coenzyme A-glutathione transhydrogenase, coenzyme A:oxidized-glutathione oxidoreductase, and coenzyme A:glutathione-disulfide oxidoreductase. This enzyme participates in cysteine metabolism and glutathione metabolism.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutathione%E2%80%94cystine%20transhydrogenase | In enzymology, a glutathione—cystine transhydrogenase () is an enzyme that catalyzes the chemical reaction
2 glutathione + cystine glutathione disulfide + 2 cysteine
Thus, the two substrates of this enzyme are glutathione and cystine, whereas its two products are glutathione disulfide and cysteine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine transhydrogenase, and NADPH-dependent GSH-cystine transhydrogenase. This enzyme participates in cysteine metabolism and glutathione metabolism.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutathione%20dehydrogenase%20%28ascorbate%29 | In enzymology, a glutathione dehydrogenase (ascorbate) () is an enzyme that catalyzes the chemical reaction
2 glutathione + dehydroascorbate glutathione disulfide + ascorbate
Thus, the two substrates of this enzyme are glutathione and dehydroascorbate, whereas its two products are glutathione disulfide and ascorbate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a quinone or similar compound as acceptor. The systematic name of this enzyme class is glutathione:dehydroascorbate oxidoreductase. Other names in common use include dehydroascorbic reductase, dehydroascorbic acid reductase, glutathione dehydroascorbate reductase, DHA reductase, dehydroascorbate reductase, GDOR, and glutathione:dehydroascorbic acid oxidoreductase. This enzyme participates in 3 metabolic pathways: ascorbate and aldarate metabolism, glutamate metabolism, and glutathione metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.8.5
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutathione%E2%80%94homocystine%20transhydrogenase | In enzymology, a glutathione—homocystine transhydrogenase () is an enzyme that catalyzes the chemical reaction
2 glutathione + homocystine glutathione disulfide + 2 homocysteine
Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two products are glutathione disulfide and homocysteine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. This enzyme participates in methionine metabolism and glutathione metabolism.
References
EC 1.8.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutathione%20oxidase | In enzymology, a glutathione oxidase () is an enzyme that catalyzes the chemical reaction
2 glutathione + O2 glutathione disulfide + H2O2
Thus, the two substrates of this enzyme are glutathione and O2, whereas its two products are glutathione disulfide and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione metabolism. It employs one cofactor, FAD.
References
EC 1.8.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20dehydrogenase | In enzymology, a glycine dehydrogenase () is an enzyme that catalyzes the chemical reaction
glycine + H2O + NAD+ glyoxylate + NH3 + NADH + H+
The 3 substrates of this enzyme are glycine, H2O, and NAD+, whereas its 4 products are glyoxylate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycine:NAD+ oxidoreductase (deaminating).
This should not be confused with:
the glycine dehydrogenase (decarboxylating), which is another name for the Glycine cleavage system P-protein ().
or the glycine dehydroganse (cyanide forming)().
or the glycine dehydrogenase (cytochrome) ().
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20dehydrogenase%20%28cyanide-forming%29 | In enzymology, a glycine dehydrogenase (cyanide-forming) () is an enzyme that catalyzes the chemical reaction
glycine + 2 A hydrogen cyanide + CO2 + 2 AH2
Thus, the two substrates of this enzyme are glycine and A, whereas its 3 products are hydrogen cyanide, CO2, and AH2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other acceptors. The systematic name of this enzyme class is glycine:acceptor oxidoreductase (hydrogen-cyanide-forming). Other names in common use include hydrogen cyanide synthase, and HCN synthase.
References
EC 1.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20dehydrogenase%20%28cytochrome%29 | In enzymology, a glycine dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction
glycine + H2O + 2 ferricytochrome c glyoxylate + NH3 + 2 ferrocytochrome c + 2 H+
The 3 substrates of this enzyme are glycine, H2O, and ferricytochrome c, whereas its 4 products are glyoxylate, NH3, ferrocytochrome c, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is glycine:ferricytochrome-c oxidoreductase (deaminating). This enzyme is also called glycine---cytochrome c reductase. This enzyme participates in glycine, serine and threonine metabolism.
References
EC 1.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20dehydrogenase%20%28decarboxylating%29 | Glycine decarboxylase also known as glycine cleavage system P protein or glycine dehydrogenase is an enzyme that in humans is encoded by the GLDC gene.
Reaction
Glycine decarboxylase () is an enzyme that catalyzes the following chemical reaction:
glycine + H-protein-lipoyllysine H-protein-S-aminomethyldihydrolipoyllysine + CO2
Thus, the two substrates of this enzyme are glycine and H-protein-lipoyllysine, whereas its two products are H-protein-S-aminomethyldihydrolipoyllysine and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a disulfide as acceptor. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Function
Glycine decarboxylase is the P-protein of the glycine cleavage system in eukaryotes. The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor. Carbon dioxide is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Degradation of glycine is brought about by the glycine cleavage system, which is composed of four mitochondrial protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein), T protein (a tetrahydrofolate-requiring enzyme), and L protein (a lipoamide dehydrogenase).
Clinical significa |
https://en.wikipedia.org/wiki/Hydrogensulfite%20reductase | In enzymology, a hydrogensulfite reductase () is an enzyme that catalyzes the chemical reaction
trithionate + acceptor + 2 H2O + OH- 3 bisulfite + reduced acceptor
The 4 substrates of this enzyme are trithionate, acceptor, H2O, and OH-, whereas its two products are bisulfite and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other acceptors. The systematic name of this enzyme class is trithionate:acceptor oxidoreductase. Other names in common use include bisulfite reductase, dissimilatory sulfite reductase, desulfoviridin, desulforubidin, desulfofuscidin, dissimilatory-type sulfite reductase, and trithionate:(acceptor) oxidoreductase. It has 4 cofactors: iron, sulfur, siroheme, and iron-sulfur.
References
EC 1.8.99
Iron enzymes
Sulfur enzymes
Siroheme enzymes
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxylamine%20oxidoreductase | Hydroxylamine oxidoreductase (HAO) is an enzyme found in the prokaryotic genus Nitrosomonas. It plays a critically important role in the biogeochemical nitrogen cycle as part of the metabolism of ammonia-oxidizing bacteria.
The substrate is hydroxylamine (NH2OH), a chemical produced biologically by the enzyme Ammonia monooxygenase. The products of the catalyzed reaction are debated, but recent work shows compelling evidence for the production of nitric oxide.
Structural studies
Crystallographic methods show that HAO (PDB code: ) is a cross-linked trimer of polypeptides containing 24 heme cofactors.
Reactivity
For many decades the enzyme was thought to catalyze the following reaction:
NH2OH + H2O -> NO2^- + 5 H+ + 4e^-
Recent work in the field, however, reveals that this enzyme catalyzes an entirely different reaction:
NH2OH -> NO + 3H+ + 3e^-
Subsequent oxidation of the nitric oxide to nitrite caused by reaction with oxygen accounts for the reactivity previous described by Hooper et al.
Environmental Impact
Nitric oxide, the product of HAO catalysis, is a potent greenhouse gas. Additionally, the oxidized product of nitric oxide in the presence of oxygen is nitrite - a common pollutant in agricultural run-off.
References
EC 1.7.3
Heme enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hydroxylamine%20reductase | In enzymology, a hydroxylamine reductase () is an enzyme that catalyzes the chemical reaction
NH3 + H2O + acceptor hydroxylamine + reduced acceptor
The 3 substrates of this enzyme are NH3, H2O, and acceptor, whereas its two products are hydroxylamine and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with other acceptors. The systematic name of this enzyme class is ammonia:acceptor oxidoreductase. Other names in common use include hydroxylamine (acceptor) reductase, and ammonia:(acceptor) oxidoreductase. This enzyme participates in nitrogen metabolism. It has 2 cofactors: FAD, and Flavoprotein.
References
EC 1.7.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxylamine%20reductase%20%28NADH%29 | In enzymology, a hydroxylamine reductase (NADH) () is an enzyme that catalyzes the chemical reaction.
NH3 + NAD+ + H2O hydroxylamine + NADH + H+
The 3 substrates of this enzyme are NH3, NAD+, and H2O, whereas its 3 products are hydroxylamine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ammonium:NAD+ oxidoreductase. Other names in common use include hydroxylamine reductase, ammonium dehydrogenase, NADH-hydroxylamine reductase, N-hydroxy amine reductase, hydroxylamine reductase (NADH2), and NADH2:hydroxylamine oxidoreductase. This enzyme participates in nitrogen metabolism.
References
EC 1.7.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hyponitrite%20reductase | In enzymology, a hyponitrite reductase is an enzyme that catalyzes the oxidation of hydroxylamine by the nicotinamide adenine dinucleotide cation (NAD+) into hyponitrous acid HON=NOH:
2 + 2 NAD+ HON=NOH + 2 NADH + 2 H+
This systematic name of this enzyme class hydroxylamine:NAD+ oxidoreductase. It is also called NADH2:hyponitrite oxidoreductase.
This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. It employs one cofactor, metal.
References
EC 1.7.1
NADH-dependent enzymes
Metal enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hypotaurine%20dehydrogenase | In enzymology, a hypotaurine dehydrogenase () is an enzyme that catalyzes the chemical reaction
hypotaurine + H2O + NAD+ taurine + NADH + H+
The 3 substrates of this enzyme are hypotaurine, H2O, and NAD+, whereas its 3 products are taurine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hypotaurine:NAD+ oxidoreductase. This enzyme participates in taurine and hypotaurine metabolism. It has 2 cofactors: heme, and Molybdenum.
References
EC 1.8.1
NADH-dependent enzymes
Heme enzymes
Molybdenum enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Iron%E2%80%94cytochrome-c%20reductase | In enzymology, an iron—cytochrome-c reductase (created 1972 as , transferred 2014 to ) is an enzyme that catalyzes the chemical reaction
ferrocytochrome c + Fe3+ ferricytochrome c + Fe2+
Thus, the two substrates of this enzyme are ferrocytochrome c and Fe3+, whereas its two products are ferricytochrome c and Fe2+.
Classification
This enzyme belongs to the family of oxidoreductases, specifically those acting on a heme group of donors with other acceptors.
Nomenclature
The systematic name of this enzyme class is ferrocytochrome-c:Fe3+ oxidoreductase. This enzyme is also called iron-cytochrome c reductase.
Structure and function
This enzyme is part of the electron transport system of Ferrobacillus ferrooxidans. It employs one cofactor, iron.
References
EC 1.9.98
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-amino-acid%20dehydrogenase | In enzymology, a L-amino-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction
an L-amino acid + H2O + NAD+ a 2-oxo acid + NH3 + NADH + H+
The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-amino-acid:NAD+ oxidoreductase (deaminating).
References
EC 1.4.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hexbug | HEXBUG is a brand of infrared and automaton toys developed and distributed by Spin Master Inc. . HEXBUG uses many elements used in BEAM robotics. First piloted in the US through RadioShack, HEXBUG is now sold in most major retail stores. The original HEXBUGs are based on six-legged arthropods but now come in several different varieties. The name "HEXBUG" relates to the six-sided packaging it is sold in, rather than to its number of legs.
History
HEXBUG was founded in 2007 in Greenville, Texas, by Innovation First International, Inc., a company that was founded in 1996 developing small-scale robotic products, mostly for FIRST Robotics Competition. HEXBUG was designed to expand the company's presence in the retail toy market, as well as add to the experience created by VEX Robotics, a subsidiary brand of Innovation First International, Inc. that specializes in robotics built in a fashion similar to Erector Sets, and Rack Solutions, which is an engineering firm that specializes in information technology products. In 2023, HEXBUG was acquired by Spin Master, meaning Innovation First no longer has anything to do with HEXBUG.
Some products of HEXBUG have been sold abroad, such as in Japan by toymaker Bandai. The packaging in these international versions differs slightly, as the HEXBUG logo is blue instead of its signature orange and grey appearance, but the products still retain their signature hexagonal packaging.
Various product lines have been sold under the HEXBUG name, s |
https://en.wikipedia.org/wiki/NNT | NNT could refer to:
Nan Airport, Thailand; IATA airport code NNT
The Nakai–Nam Theun National Biodiversity Conservation Area in Laos
Nassim Nicholas Taleb
Number needed to treat, an epidemiological measure
Nunthorpe railway station, England; National Rail station code NNT
NAD(P) transhydrogenase, a human mitochondria|mitochondrial enzyme encoded by the NNT gene |
https://en.wikipedia.org/wiki/Ephrin%20B1 | Ephrin B1 is a protein that in humans is encoded by the EFNB1 gene. It is a member of the ephrin family. The encoded protein is a type I membrane protein and a ligand of Eph-related receptor tyrosine kinases. It may play a role in cell adhesion and function in the development or maintenance of the nervous system.
Clinical significance
Mutations in this protein are responsible for most cases of craniofrontonasal syndrome.
Interactions
EFNB1 has been shown to interact with SDCBP.
References
Further reading
External links
Genes on human chromosome X |
https://en.wikipedia.org/wiki/EIF5A | Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.
It is the only known protein to contain the unusual amino acid hypusine [Nε-(4-amino-2-hydroxybutyl)-lysine], which is synthesized on eIF5A at a specific lysine residue from the polyamine spermidine by two catalytic steps.
EF-P is the bacterial homolog of eIF5A, which is modified post-translationally in a similar but distinct way. Both proteins are believed to catalyze peptide bond formation and help resolve ribosomal stalls, making them elongation factors despite the "initiation factor" name originally assigned.
Clinical relevance
Germline deleterious heterozygous EIF5A variants cause Faundes-Banka syndrome. This rare human disorder is characterized by variable combinations of developmental delay, microcephaly, micrognathia and dysmorphic features.
References
Further reading
Rare diseases |
https://en.wikipedia.org/wiki/ERCC1 | DNA excision repair protein ERCC-1 is a protein that in humans is encoded by the ERCC1 gene. Together with ERCC4, ERCC1 forms the ERCC1-XPF enzyme complex that participates in DNA repair and DNA recombination.
Many aspects of these two gene products are described together here because they are partners during DNA repair. The ERCC1-XPF nuclease is an essential activity in the pathway of DNA nucleotide excision repair (NER). The ERCC1-XPF nuclease also functions in pathways to repair double-strand breaks in DNA, and in the repair of “crosslink” damage that harmfully links the two DNA strands.
Cells with disabling mutations in ERCC1 are more sensitive than normal to particular DNA damaging agents, including ultraviolet (UV) radiation and to chemicals that cause crosslinking between DNA strands. Genetically engineered mice with disabling mutations in ERCC1 have defects in DNA repair, accompanied by metabolic stress-induced changes in physiology that result in premature aging. Complete deletion of ERCC1 is incompatible with viability of mice, and no human individuals have been found with complete (homozygous) deletion of ERCC1. Rare individuals in the human population harbor inherited mutations that impair the function of ERCC1. When the normal genes are absent, these mutations can lead to human syndromes, including Cockayne syndrome (CS) and COFS.
ERCC1 and ERCC4 are the gene names assigned in mammalian genomes, including the human genome (Homo sapiens). Similar genes with si |
https://en.wikipedia.org/wiki/FLI1 | Friend leukemia integration 1 transcription factor (FLI1), also known as transcription factor ERGB, is a protein that in humans is encoded by the FLI1 gene, which is a proto-oncogene.
Function
Fli-1 is a member of the ETS transcription factor family that was first identified in erythroleukemias induced by Friend Murine Leukemia Virus (F-MuLV). Fli-1 is activated through retroviral insertional mutagenesis in 90% of F-MuLV-induced erythroleukemias. The constitutive activation of fli-1 in erythroblasts leads to a dramatic shift in the Epo/Epo-R signal transduction pathway, blocking erythroid differentiation, activating the Ras pathway, and resulting in massive Epo-independent proliferation of erythroblasts. These results suggest that Fli-1 overexpression in erythroblasts alters their responsiveness to Epo and triggers abnormal proliferation by switching the signaling event(s) associated with terminal differentiation to proliferation.
Clinical significance
In addition to Friend erythroleukemia, proviral integration at the fli-1 locus also occurs in leukemias induced by the 10A1, Graffi, and Cas-Br-E viruses. Fli-1 aberrant expression is also associated with chromosomal abnormalities in humans. In pediatric Ewing’s sarcoma a chromosomal translocation generates a fusion of the 5’ transactivation domain of EWSR1 (also known as EWS) with the 3’ Ets domain of Fli-1. The resulting fusion oncoprotein, EWS/Fli-1, acts as an aberrant transcriptional activator. with strong transformi |
https://en.wikipedia.org/wiki/Importin%20subunit%20alpha-6 | Importin subunit alpha-6 is a protein that in humans is encoded by the KPNA5 gene.
The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs).
KPNA5 protein belongs to the importin alpha protein family and is thought to be involved in NLS-dependent protein import into the nucleus
References
Further reading
Armadillo-repeat-containing proteins |
https://en.wikipedia.org/wiki/NEUROD1 | Neurogenic differentiation 1 (Neurod1), also called β2, is a transcription factor of the NeuroD-type. It is encoded by the human gene NEUROD1.
In mice, Neurod1 expression is first seen at embryonic day 12 (E12).
It is a member of the Neurod family of basic helix-loop-helix (bHLH) transcription factors, composed of Neurod1, Neurod2, Neurod4, and Neurod6. The protein forms heterodimers with other bHLH proteins and activates transcription of genes that contain a specific DNA sequence known as the E-box. It regulates expression of the insulin gene, and mutations in this gene result in type II diabetes mellitus in mouse models and in human clinical patients.
Neurod1 is found to convert reactive glial cells into functional neurons in the mouse brain in vivo In the adult cortex, Neurod1 expression is a marker of mature excitatory pyramidal neurons in the upper-most layers of the cortex.
Interactions
Neurod1 has been shown to interact with MAP3K10, MAFA and Cyclin D1.
References
Further reading
External links
Transcription factors
Human proteins |
https://en.wikipedia.org/wiki/MAP2K6 | Dual specificity mitogen-activated protein kinase kinase 6 also known as MAP kinase kinase 6 (MAPKK 6) or MAPK/ERK kinase 6 is an enzyme that in humans is encoded by the MAP2K6 gene, on chromosome 17.
Function
MAPKK 6 is a member of the dual specificity protein kinase family, which functions as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This protein phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. As an essential component of p38 MAP kinase mediated signal transduction pathway, this gene is involved in many cellular processes such as stress-induced cell cycle arrest, transcription activation and apoptosis.
Interactions
MAP2K6 has been shown to interact with TAOK2, ASK1, MAPK14 and MAP3K7.
References
Further reading
EC 2.7.12 |
https://en.wikipedia.org/wiki/PABPC1 | Polyadenylate-binding protein 1 is a protein that in humans is encoded by the PABPC1 gene. The protein PABP1 binds mRNA and facilitates a variety of functions such as transport into and out of the nucleus, degradation, translation, and stability. There are two separate PABP1 proteins, one which is located in the nucleus (PABPN1) and the other which is found in the cytoplasm (PABPC1). The location of PABP1 affects the role of that protein and its function with RNA.
Function
The poly(A)-binding protein (PAB or PABP), which is found complexed to the 3' poly(A) tail of eukaryotic mRNA, is required for poly(A) lengthening and the termination of translation. In humans, the PABPs comprise a small nuclear isoform and a conserved gene family of other poly(A)-binding proteins.[supplied by OMIM]
PABPC1 is usually diffused within the cytoplasm and concentrated at sites of high mRNA concentration such as stress granules, processing bodies, and locations of high translational activity. PABPC1 is also associated with nonsense-mediated mRNA decay (NMD). PABPC1 binds to the poly(A) tail and interact with eIF4G, which stabilizes the circularization of mRNAs. This structure is required for the prevention of mRNA degradation via NMD.
In the nucleus PABP1 binds to the poly(A) tails of pre-mRNAs to facilitate stability, export, transport, and degradation. PABP1 binding is also required for nuclear-mediated degradation. PABPC1 contains four RNA-recognition motifs (RRMs). The first two, RRM1 an |
https://en.wikipedia.org/wiki/RACGAP1 | Rac GTPase-activating protein 1 is an enzyme that in humans is encoded by the RACGAP1 gene.
Function
Rho GTPases control a variety of cellular processes. There are 3 subtypes of Rho GTPases in the Ras superfamily of small G proteins: RHO (see MIM 165370), RAC (see RAC1; MIM 602048), and CDC42 (MIM 116952). GTPase-activating proteins (GAPs) bind activated forms of Rho GTPases and stimulate GTP hydrolysis. Through this catalytic function, Rho GAPs negatively regulate Rho-mediated signals. GAPs may also serve as effector molecules and play a role in signaling downstream of Rho and other Ras-like GTPases.[supplied by OMIM]. Over-expression of RACGAP1 is observed in multiple human cancers including breast cancer, gastric cancer and colorectal cancer. Evidence show that RACGAP1 can modulate mitochondrial quality control by stimulating mitopahy and mitochondrial biogenesis in breast cancer. Knocking out RACGAP1 in vitro using CRISPR/Cas9 leads to cytokinesis failure.
Interactions
RACGAP1 has been shown to interact with ECT2, Rnd2 and SLC26A8.
During cytokinesis, RACGAP1 has been shown to interact with KIF23 to form the centralspindlin complex. This complex is essential for the formation of the central spindle. RACGAP1 also interacts with PRC1 to stabilize and maintain the central spindle as anaphase proceeds. RACGAP1 can also interact with ECT2 during anaphase of cytokinesis, loss of RACGAP1 leads to cytokinesis failure.
References
Further reading |
https://en.wikipedia.org/wiki/KLF6 | Krueppel-like factor 6 is a protein that in humans is encoded by the KLF6 gene.
It is a tumor suppressor gene.
Function
This gene encodes a nuclear protein that has three zinc fingers at the end of its C-terminal domain, a serine/threonine-rich central region, and an acidic domain lying within the N-terminal region. The zinc fingers of this protein are responsible for the specific DNA binding with the guanine-rich core promoter elements. The central region might be involved in activation or posttranslational regulatory pathways, and the acidic N-terminal domain might play an important role in the process of transcriptional activation. It is capable of activating transcription approximately 4-fold either on homologous or heterologous promoters. The DNA binding and transcriptional activity of this protein, in conjunction with its expression pattern, suggests that this protein may participate in the regulation and/or maintenance of the basal expression of pregnancy-specific glycoprotein genes and possibly other TATA box-less genes. Two transcript variants encoding the same protein have been found for this gene.
Interactions
KLF6 has been shown to interact with Sp1 transcription factor.
See also
Kruppel-like factors
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/FADS2 | Fatty acid desaturase 2 (FADS2) is encoded by the FADS2 gene, the associated enzyme is sometimes known as FADS2 as well. Its main associated enzyme is Delta 6 desaturase (D6D) however the human enzyme was shown to also catalyze some delta-8 and delta-4 desaturation reactions despite naming conventions.
Function
Fatty acid desaturase 2 is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes cause desaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization.
Clinical significance
It was reported the FADS2 interacts with breastfeeding such that breast-fed children with the "C" version of the gene appear about 7 intelligence quotient (IQ) points higher than those with the less common "G" version (less than this when adjusted for maternal IQ).
An attempt to replicate this study in 5934 8-year-old children failed: No relationship of the common C allele to negative effects of formula feeding was apparent, and contra to the original report, the rare GG homozygote children perfo |
https://en.wikipedia.org/wiki/TGFB1I1 | Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene. Often put together with and studied alongside TGFB1I1 is the mouse homologue HIC-5 ( Hydrogen Peroxide-Inducible Clone-5). As the name suggests, TGFB1I1 is an induced form of the larger family of TGFB1. Studies suggest TGFB1I1 plays a role in processes of cell growth, proliferation, migration, differentiation and senescence. TGFB1I1 is most localized at focal adhesion complexes of cells, although it may be found active in the cytosol, nucleus and cell membrane as well.
Functions
Transforming growth factor beta-1-induced transcript 1 plays a role in a number of cell functions. Originally, TGFB1I1 was isolated as a senescence-inducing gene from mouse osteoblastic cells through treatment with transforming growth factor beta-1 and hydrogen peroxide. During this, TGFB1I1 was also being independently discovered by numerous other groups and was characterized as a focal adhesion protein, an androgen and glucocorticoid receptor co-activator, a negative regulator of muscle differentiation, and major player in the recovery of arterial media.
Interactions
TGFB1I1 has been shown to interact with:
Androgen receptor,
Dopamine transporter
Hsp27,
PTK2B,
PTK2, and
PTPN12.
Model organisms
Model organisms have been used in the study of TGFB1I1 function. A conditional knockout mouse line called Tgfb1i1tm1b(KOMP)Wtsi was generated at the Wellcome Trust Sange |
https://en.wikipedia.org/wiki/Integrin%20alpha%205 | Integrin alpha-5 is a protein that in humans is encoded by the ITGA5 gene.
The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes the integrin alpha 5 chain. Alpha chain 5 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains that join with beta 1 to form a fibronectin receptor. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.
Interactions
ITGA5 has been shown to interact with GIPC1.
See also
Cluster of differentiation
Integrin
References
Further reading
External links
ITGA5 Info with links in the Cell Migration Gateway
Clusters of differentiation
Integrins |
https://en.wikipedia.org/wiki/Proto-oncogene%20Wnt-1 | Proto-oncogene Wnt-1, or Proto-oncogene Int-1 homolog is a protein that in humans is encoded by the () gene.
The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It is very conserved in evolution, and the protein encoded by this gene is known to be 98% identical to the mouse Wnt1 protein at the amino acid level. The studies in mouse indicate that the Wnt1 protein functions in the induction of the mesencephalon and cerebellum. This gene was originally considered as a candidate gene for Joubert syndrome, an autosomal recessive disorder with cerebellar hypoplasia as a leading feature. However, further studies suggested that the gene mutations might not have a significant role in Joubert syndrome. This gene is clustered with another family member, WNT10B, in the chromosome 12q13 region.
See also
Wnt signaling pathway
References
Further reading |
https://en.wikipedia.org/wiki/NOD1 | Nucleotide-binding oligomerization domain-containing protein 1 (NOD1) is a protein receptor that in humans is encoded by the NOD1 gene. It recognizes bacterial molecules and stimulates an immune reaction .
NOD1 protein contains a caspase recruitment domain (CARD). NOD1 is a member of NOD-like receptor protein family and is a close relative of NOD2. NOD1 is an intracellular pattern recognition receptor, which is similar in structure to resistant proteins of plants, and mediates innate and acquired immunity by recognizing molecules containing D-glutamyl-meso-diaminopimelic acid (iE-DAP) moiety, including bacterial peptidoglycan. Nod1 interacts with RIPK2 through the CARDs of both molecules (See the structure of the NOD1 CARD in the right panel). Stimulation of NOD1 by iE-DAP containing molecules results in activation of the transcription factor NF-κB.
References
Further reading
External links
LRR proteins
NOD-like receptors |
https://en.wikipedia.org/wiki/ATF3 | Cyclic AMP-dependent transcription factor ATF-3 is a protein that, in humans, is encoded by the ATF3 gene.
Function
Activating transcription factor 3 is a member of the mammalian activation transcription factor/cAMP responsive element-binding (CREB) protein family of transcription factors. Multiple transcript variants encoding two different isoforms have been found for this gene. The longer isoform represses rather than activates transcription from promoters with ATF binding elements. The shorter isoform (deltaZip2) lacks the leucine zipper protein-dimerization motif and does not bind to DNA, and it stimulates transcription, it is presumed, by sequestering inhibitory co-factors away from the promoter. It is possible that alternative splicing of the ATF3 gene may be physiologically important in the regulation of target genes.
Clinical significance
ATF-3 is induced upon physiological stress in various tissues. It is also a marker of regeneration following injury of dorsal root ganglion neurons, as injured regenerating neurons activate this transcription factor. Functional validation studies have shown that ATF3 can promote regeneration of peripheral neurons, but is not capable of promoting regeneration of central nervous system neurons.
See also
Activating transcription factor
Interactions
ATF3 has been shown to interact with:
C-jun,
DDIT3
JunD,
P53, and
SMAD3.
References
Further reading
External links
Transcription factors |
https://en.wikipedia.org/wiki/MEF2C | Myocyte-specific enhancer factor 2C also known as MADS box transcription enhancer factor 2, polypeptide C is a protein that in humans is encoded by the MEF2C gene. MEF2C is a transcription factor in the Mef2 family.
Genomics
The gene is located at 5q14.3 on the minus (Crick) strand and is 200,723 bases in length. The encoded protein has 473 amino acids with a predicted molecular weight of 51.221 kiloDaltons. Three isoforms have been identified. Several post translational modifications have been identified including phosphorylation on serine-59 and serine-396, sumoylation on lysine-391, acetylation on lysine-4 and proteolytic cleavage.
Interactions
MEF2C has been shown to interact with:
EP300,
HDAC4, HDAC7, HDAC9,
MAPK7,
SOX18
SP1, and
TEAD1.
SETD1A
Biological significance
This gene is involved in cardiac morphogenesis and myogenesis and vascular development. It may also be involved in neurogenesis and in the development of cortical architecture. Mice without a functional copy of the Mef2c gene die before birth and have abnormalities in the heart and vascular system. It is one of the targets of an oncomiR, MIRN21.
In humans mutations of this gene result in autosomal dominant mental retardation 20 (MRD20), characterised by severe psychomotor impairment, periodic tremor and an abnormal motor pattern with mirror movement of the upper limbs observed during infancy, hypotonia, abnormal EEG, epilepsy, absence of speech, autistic behavior, bruxism, and mild dysm |
https://en.wikipedia.org/wiki/PGK1 | Phosphoglycerate kinase 1 is an enzyme that in humans is encoded by the PGK1 gene.
Interactive pathway map
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Phosphoglycerate kinase 1 |
https://en.wikipedia.org/wiki/LRP1 | Low density lipoprotein receptor-related protein 1 (LRP1), also known as alpha-2-macroglobulin receptor (A2MR), apolipoprotein E receptor (APOER) or cluster of differentiation 91 (CD91), is a protein forming a receptor found in the plasma membrane of cells involved in receptor-mediated endocytosis. In humans, the LRP1 protein is encoded by the LRP1 gene. LRP1 is also a key signalling protein and, thus, involved in various biological processes, such as lipoprotein metabolism and cell motility, and diseases, such as neurodegenerative diseases, atherosclerosis, and cancer.
Structure
The LRP1 gene encodes a 600 kDa precursor protein that is processed by furin in the trans-Golgi complex, resulting in a 515 kDa alpha-chain and an 85 kDa beta-chain associated noncovalently. As a member of the LDLR family, LRP1 contains cysteine-rich complement-type repeats, EGF (gene) repeats, β-propeller domains, a transmembrane domain, and a cytoplasmic domain. The extracellular domain of LRP1 is the alpha-chain, which comprises four ligand-binding domains (numbered I-IV) containing two, eight, ten, and eleven cysteine-rich complement-type repeats, respectively. These repeats bind extracellular matrix proteins, growth factors, proteases, protease inhibitor complexes, and other proteins involved in lipoprotein metabolism. Of the four domains, II and IV bind the majority of the protein's ligands. The EGF repeats and β-propeller domains serve to release ligands in low pH conditions, such as inside |
https://en.wikipedia.org/wiki/TRAF5 | TNF receptor-associated factor 5 is a protein that in humans is encoded by the TRAF5 gene.
Function
The scaffold protein encoded by this gene is a member of the tumor necrosis factor receptor-associated factor (TRAF) protein family and contains a meprin and TRAF homology (MATH) domain, a RING-type zinc finger, and two TRAF-type zinc fingers. TRAF proteins are associated with, and mediate signal transduction from members of the TNF receptor superfamily. This protein is one of the components of a multiple protein complex which binds to tumor necrosis factor (TNF) receptor cytoplasmic domains and mediates TNF-induced activation. Alternate transcriptional splice variants have been characterized.
Interactions
TRAF5 has been shown to interact with:
ASK1,
CD134,
CD30,
CD40,
RANK
TNFRSF13B, and
TNFRSF14.
References
Further reading |
https://en.wikipedia.org/wiki/POLI | DNA polymerase iota is an enzyme that in humans is encoded by the POLI gene. It is found in higher eukaryotes, and is believed to have arisen from a gene duplication from Pol η. Pol ι, is a Y family polymerase that is involved in translesion synthesis. It can bypass 6-4 pyrimidine adducts and abasic sites and has a high frequency of wrong base incorporation. Like many other Y family polymerases Pol ι, has low processivity, a large DNA binding pocket and doesn't undergo conformational changes when DNA binds. These attributes are what allow Pol ι to carry out its task as a translesion polymerase. Pol ι only uses Hoogsteen base pairing, during DNA synthesis, it will add adenine opposite to thymine in the syn conformation and can add both cytosine and thymine in the anti conformation across guanine, which it flips to the syn conformation.
References
Further reading
DNA replication
DNA-binding proteins |
https://en.wikipedia.org/wiki/ADH1C | Alcohol dehydrogenase 1C is an enzyme that in humans is encoded by the ADH1C gene.
Function
This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol (beverage alcohol), retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibit high activity for ethanol oxidation and play a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Afadin | Afadin is a protein that in humans is encoded by the AFDN gene.
Function
Afadin is a Ras (see HRAS; MIM 190020) target that regulates cell–cell adhesions downstream of Ras activation. It is fused with MLL (MIM 159555) in leukemias caused by t(6;11) translocations (Taya et al., 1998).[supplied by OMIM]
Interactions
Afadin has been shown to interact with:
BCR gene,
EPHB3,
F11 receptor,
HRAS and
LMO2,
PVRL1,
PVRL3,
Profilin 1,
RAP1A,
RAP1GAP,
SORBS1,
SSX2IP,
Tight junction protein 1, and
USP9X.
References
Further reading |
https://en.wikipedia.org/wiki/FLNA | Filamin A, alpha (FLNA) is a protein that in humans is encoded by the FLNA gene.
Function
Actin-binding protein, or filamin, is a 280-kD protein that crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. Filamin A, encoded by the FLNA gene, is a widely expressed filamin that regulates the reorganization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes, and secondary messengers. At least 31 disease-causing mutations in this gene have been discovered.
Structure
The protein structure includes an actin binding N terminal domain, 24 internal repeats and 2 hinge regions.
Interactions
Filamin has been shown to interact with:
BRCA2,
CD29
CASR,
FBLIM1,
FILIP1,
FLNB,
NPHP1,
RALA,
SH2B3,
TRIO, and
VHL.
RNA editing
The edited residue was previously recorded as a single nucleotide polymorphism(SNP) in dbSNP.
Type
A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs and deaminate them to inosine. Inosines are recognised as guanosine by the cells translational machinery. There are three members of the ADAR family ADARs 1-3 with ADAR 1 and ADAR 2 being the only enzymatically active members.ADAR3 is thought to h |
https://en.wikipedia.org/wiki/NRF1 | Nuclear respiratory factor 1, also known as Nrf1, Nrf-1, NRF1 and NRF-1, encodes a protein that homodimerizes and functions as a transcription factor which activates the expression of some key metabolic genes regulating cellular growth and nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication. The protein has also been associated with the regulation of neurite outgrowth. Alternate transcriptional splice variants, which encode the same protein, have been characterized. Additional variants encoding different protein isoforms have been described but they have not been fully characterized. Confusion has occurred in bibliographic databases due to the shared symbol of NRF1 for this gene and for "nuclear factor (erythroid-derived 2)-like 1" which has an official symbol of NFE2L1.
Function
Nrf1 functions as a transcription factor that activates the expression of some key metabolic genes regulating cellular growth and nuclear genes required for mitochondrial respiration, and mitochondrial DNA transcription and replication. Nrf1, together with Nrf2, mediates the biogenomic coordination between nuclear and mitochondrial genomes by directly regulating the expression of several nuclear-encoded ETC proteins, and indirectly regulating the three mitochondrial-encoded COX subunit genes by activating mtTFA, mtTFB1, and mtTFB2.
Nrf1 is associated with the regulation of neurite outgrowth.
Alternate transcriptional splice variants, whic |
https://en.wikipedia.org/wiki/STAT5A | Signal transducer and activator of transcription 5A is a protein that in humans is encoded by the STAT5A gene. STAT5A orthologs have been identified in several placentals for which complete genome data are available.
Structure
STAT5a shares the same six functional domains as the other members of the STAT family. It contains 20 amino acids unique to its C-terminal domain and is 96% similar to its homolog, STAT5b. The six functional domains and their corresponding amino acid positions are as follows:
N-Terminal domain (aa1-144): stabilized interactions to form tetramers
Coiled-coil domain (aa145-330): interacts with chaperones and facilitates protein-protein interactions for transcriptional regulation
DNA binding domain (aa331-496): permits binding to consensus gamma-interferon activation sequence (GAS)
Linker domain (aa497-592): stabilizes DNA binding
Src Homology 2 domain (aa593-685): mediates receptor-specific recruitment and STAT dimerization via phosphorylated tyrosine residue
Transcriptional activation domain (aa702-794): interacts with critical co-activators
In addition to the six functional domains, specific amino acids have been identified as key mediators of STAT5a function. Phosphorylation of tyrosine 694 and glycosylation of threonine 92 are important for STAT5a activity. Mutation of serine 710 to phenylalanine results in constitutive activation.
Function
The protein encoded by this gene is a member of the STAT family of transcription factors. In response |
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