| asparagine-oxo-acid transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.14 | ||||||||
| CAS no. | 9030-43-7 | ||||||||
| 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, an asparagine-oxo-acid transaminase (EC 2.6.1.14) is an enzyme that catalyzes the chemical reaction
- L-asparagine + a 2-oxo acid 2-oxosuccinamate + an amino acid
Thus, the two substrates of this enzyme are L-asparagine and 2-oxo acid, whereas its two products are 2-oxosuccinamate and amino acid.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-asparagine:2-oxo-acid aminotransferase. This enzyme is also called asparagine-keto acid aminotransferase. This enzyme participates in alanine and aspartate metabolism and tetracycline biosynthesis. It employs one cofactor, pyridoxal phosphate.
References
- MEISTER A, FRASER PE (1954). "Enzymatic formation of L-asparagine by transamination". J. Biol. Chem. 210 (1): 37–43. PMID 13201567.
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