Serine—glyoxylate transaminase

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serine-glyoxylate transaminase
Identifiers
EC number2.6.1.45
CAS number37259-57-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a serine-glyoxylate transaminase (EC 2.6.1.45) is an enzyme that catalyzes the chemical reaction

L-serine + glyoxylate 3-hydroxypyruvate + glycine

Thus, the two substrates of this enzyme are L-serine and glyoxylate, whereas its two products are 3-hydroxypyruvate and glycine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:glyoxylate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

References[edit]

  • Ireland RJ, Joy KW (1983). "Purification and properties of an asparagine aminotransferase from Pisum sativum leaves". Arch. Biochem. Biophys. 223 (1): 291–6. doi:10.1016/0003-9861(83)90594-5. PMID 6407397.
  • King J, Waygood ER (1968). "Glyoxylate aminotranferases from wheat leaves". Can. J. Biochem. 46 (8): 771–9. doi:10.1139/v68-127. PMID 5672858.
  • Smith IK (1973). "Purification and characterization of serine:glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris)". Biochim. Biophys. Acta. 321 (1): 156–64. doi:10.1016/0005-2744(73)90069-7. PMID 4750762.