Biology:Alanine—oxomalonate transaminase
From HandWiki
| alanine-oxomalonate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.47 | ||||||||
| CAS number | 37277-96-6 | ||||||||
| 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 | ||||||||
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In enzymology, an alanine-oxomalonate transaminase (EC 2.6.1.47) is an enzyme that catalyzes the chemical reaction
- L-alanine + oxomalonate [math]\displaystyle{ \rightleftharpoons }[/math] pyruvate + aminomalonate
Thus, the two substrates of this enzyme are L-alanine and oxomalonate, whereas its two products are pyruvate and aminomalonate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:oxomalonate aminotransferase. Other names in common use include alanine-oxomalonate aminotransferase, L-alanine-ketomalonate transaminase, and alanine-ketomalonate (mesoxalate) transaminase. It employs one cofactor, pyridoxal phosphate.
References
- "Enzymatic formation of aminomalonic acid from ketomalonic acid". Nature 181 (4606): 417–418. 1958. doi:10.1038/181417a0. PMID 13504217.
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