methylarsonate reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.20.4.2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a methylarsonate reductase (EC 1.20.4.2) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are methylarsonate and glutathione, whereas its 3 products are methylarsonite, glutathione disulfide, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is gluthathione:methylarsonate oxidoreductase. This enzyme is also called MMA(V) reductase.
Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules.
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene. Glutathione reductase catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell. Glutathione reductase functions as dimeric disulfide oxidoreductase and utilizes an FAD prosthetic group and NADPH to reduce one molar equivalent of GSSG to two molar equivalents of GSH:
Glutaredoxins are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose metabolism. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Instead, glutaredoxins are reduced by the oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system.
In enzymology, a glycine reductase (EC 1.21.4.2) is an enzyme that catalyzes the chemical reaction
Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction
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Glutathione amide reductase (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
Glutathione amide-dependent peroxidase (EC 1.11.1.17) is an enzyme with systematic name glutathione amide:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction
Arsenite methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:arsenite As-methyltransferase. This enzyme catalyses the following chemical reaction