Glycine reductase

Glycine reductase

In enzymology, a glycine reductase is an enzyme that catalyzes the chemical reaction

acetyl phosphate + NH3 + thioredoxin disulfide + H2O rightleftharpoons 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

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