Glycine reductase explained

glycine reductase
Ec Number:	1.21.4.2
Go Code:	0030699

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, to be specific, 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 . 1999 . Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis . Eur. J. Biochem. . 260 . 38 - 49 . 10091582 . 10.1046/j.1432-1327.1999.00107.x . Sonntag . D . Grimm . R . Pich . A . Eckerskorn . C . Söhling . B . Andreesen . JR . 1 .
• 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 . 11422384 . 10.1046/j.1432-1327.2001.02257.x . 12 . free .