Glycine transaminase
| glycine transaminase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 2.6.1.4 | ||||||
| CAS number | 9032-99-9 | ||||||
| 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 / EGO | ||||||
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In enzymology, a glycine transaminase (EC 2.6.1.4) is an enzyme that catalyzes the chemical reaction
- glycine + 2-oxoglutarate
glyoxylate + L-glutamate
Thus, the two substrates of this enzyme are glycine and 2-oxoglutarate, whereas its two products are glyoxylate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is glycine:2-oxoglutarate aminotransferase. Other names in common use include glutamic-glyoxylic transaminase, glycine aminotransferase, glyoxylate-glutamic transaminase, L-glutamate:glyoxylate aminotransferase, and glyoxylate-glutamate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
References
- Nakada HI (1964). "Glutamic-glycine transaminase from rat liver". J. Biol. Chem. 239: 468–471. PMID 14169146.
- Thompson JS and Richardson KE (1966). "Isolation and chracterization of a glutamate-glycine transaminase from human liver". Arch. Biochem. Biophys. 117 (3): 599–603. doi:10.1016/0003-9861(66)90101-9.