Serine-glyoxylate transaminase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 2.6.1.45
- BRENDA references for 2.6.1.45 (Recommended.)
- PubMed references for 2.6.1.45
- PubMed Central references for 2.6.1.45
- Google Scholar references for 2.6.1.45
- Ireland RJ, Joy KW (1983). "Purification and properties of an asparagine aminotransferase from Pisum sativum leaves". Arch. Biochem. Biophys. 223: 291–6. doi: . PMID 6407397.
- King J, Waygood ER (1968). "Glyoxylate aminotranferases from wheat leaves". Can. J. Biochem. 46: 771–9. PMID 5672858.
- Smith IK (1973). "Purification and characterization of serine:glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris)". Biochim. Biophys. Acta. 321: 156–64. PMID 4750762.
[edit] External links
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- The CAS registry number for this enzyme class is 37259-57-7.