- acetyl phosphate + NH3 + thioredoxin disulfide + H2O glycine + phosphate + 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).
- IUBMB entry for 126.96.36.199
- BRENDA references for 188.8.131.52 (Recommended.)
- PubMed references for 184.108.40.206
- PubMed Central references for 220.127.116.11
- Google Scholar references for 18.104.22.168
- Andreesen JR (1999). "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". Eur. J. Biochem. 260: 38&ndash, 49. 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&ndash, 44. PMID 11422384.