Glycine transaminase

In enzymology, a glycine transaminase (EC 2.6.1.4) is an enzyme that catalyzes the chemical reaction

glycine + 2-oxoglutarate glyoxylate + L-glutamate
glycine transaminase
Identifiers
EC no.2.6.1.4
CAS no.9032-99-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
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NCBIproteins

Thus, the two substrates of this enzyme are glycine and 2-oxoglutarate, whereas its two products are glyoxylate and L-glutamate.

This reactions strongly favours synthesis of glycine.[1] 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

  1. Textbook of Biochemistry for Medical Students, by DM Vasudevan, Sreekumari S, Kannan Vaidyanathan, 9th edition, page 283.
  • Nakada HI (1964). "Glutamic-glycine transaminase from rat liver". J. Biol. Chem. 239: 468–471. 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.


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