Biology:Asparagine—oxo-acid transaminase
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asparagine-oxo-acid transaminase | |||||||||
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Identifiers | |||||||||
EC number | 2.6.1.14 | ||||||||
CAS number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Enzymatic formation of L-asparagine by transamination". J. Biol. Chem. 210 (1): 37–43. 1954. PMID 13201567.
![]() | Original source: https://en.wikipedia.org/wiki/Asparagine—oxo-acid transaminase.
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