Biology:Serine—glyoxylate transaminase
From HandWiki
| serine-glyoxylate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.45 | ||||||||
| CAS number | 37259-57-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a serine-glyoxylate transaminase (EC 2.6.1.45) is an enzyme that catalyzes the chemical reaction
- L-serine + glyoxylate [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Purification and properties of an asparagine aminotransferase from Pisum sativum leaves". Arch. Biochem. Biophys. 223 (1): 291–6. 1983. doi:10.1016/0003-9861(83)90594-5. PMID 6407397.
- "Glyoxylate aminotranferases from wheat leaves". Can. J. Biochem. 46 (8): 771–9. 1968. 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.
 |  |
