| glycine reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.4.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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, 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; Sonntag, D; Grimm, R; Pich, A; Eckerskorn, C; Söhling, B; Andreesen, JR (1999). "Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis". Eur. J. Biochem. 260 (1): 38–49. doi:10.1046/j.1432-1327.1999.00107.x. 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 (12): 3538–44. doi:10.1046/j.1432-1327.2001.02257.x. PMID 11422384.
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