Serine—glyoxylate transaminase
| serine-glyoxylate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.45 | ||||||||
| CAS no. | 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 3-hydroxypyruvate + glycine
Thus, the two substrates of this enzyme are L-serine and glyoxylate, whereas its two products are 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 . It employs one cofactor, pyridoxal phosphate.
References[]
- 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.
Categories:
- EC 2.6.1
- Pyridoxal phosphate enzymes
- Enzymes of unknown structure
- EC 2.6 stubs