Glycine transaminase
| Glycine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.4 | ||||||||
| CAS no. | 9032-99-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Glycine transaminase (EC 2.6.1.4) is an enzyme characterised from liver that catalyzes a reversible chemical reaction to interconvert glycine and α-ketoglutaric acid with glycolic acid and L-glutamic acid:[1][2]
Although reversible, the reaction strongly favours the synthesis of glycine.[3] This enzyme is a transferase, 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. It employs one cofactor, pyridoxal phosphate.[4]
References
- ↑ Nakada HI (1964). "Glutamic-glycine transaminase from rat liver". J. Biol. Chem. 239 (2): 468–471. doi:10.1016/S0021-9258(18)51703-8. PMID 14169146.
- ↑ Thompson JS, Richardson KE (1966). "Isolation and characterization of a glutamate-glycine transaminase from human liver". Arch. Biochem. Biophys. 117 (3): 599–603. doi:10.1016/0003-9861(66)90101-9.
- ↑ Textbook of Biochemistry for Medical Students, by DM Vasudevan, Sreekumari S, Kannan Vaidyanathan, 9th edition, page 283.
- ↑ Enzyme 2.6.1.4 at KEGG Pathway Database.