Glycine reductase

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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).

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&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.

External links

Gene Ontology (GO) codes

Template:1.21-enzyme-stub


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