In
enzymology, a
glycine reductase 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).
References
- Andreesen JR "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". Eur. J. Biochem. 260 38–49.
- Bednarski B, Andreesen JR, Pich A "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.
External links
Gene Ontology (GO) codes