Glycine reductase
From Wikipedia, the free encyclopedia
In enzymology, a glycine reductase (EC 1.21.4.2) is an enzyme that catalyzes the chemical reaction
- acetyl phosphate + NH3 + thioredoxin disulfide + H2O glycine + phosphate + thioredoxin
The 4 substrates of this enzyme are acetyl phosphate, NH3, thioredoxin disulfide, and H2O, whereas its 3 products are glycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase (glycine-forming).
[edit] References
- IUBMB entry for 1.21.4.2
- BRENDA references for 1.21.4.2 (Recommended.)
- PubMed references for 1.21.4.2
- PubMed Central references for 1.21.4.2
- Google Scholar references for 1.21.4.2
- Andreesen JR (1999). "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". Eur. J. Biochem. 260: 38–49. doi: . PMID 10091582.
- Bednarski B, Andreesen JR, Pich A (2001). "In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue". Eur. J. Biochem. 268: 3538–44. doi: . PMID 11422384.