Glycine transaminase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 2.6.1.4
- BRENDA references for 2.6.1.4 (Recommended.)
- PubMed references for 2.6.1.4
- PubMed Central references for 2.6.1.4
- Google Scholar references for 2.6.1.4
- Nakada HI (1964). "Glutamic-glycine transaminase from rat liver". J. Biol. Chem. 239: 468–471.
- Thompson JS and Richardson KE (1966). "Isolation and chracterization of a glutamate-glycine transaminase from human liver". Arch. Biochem. Biophys. 117: 599–603. doi: .
[edit] External links
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- The CAS registry number for this enzyme class is 9032-99-9.