Asparagine—oxo-acid transaminase

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asparagine-oxo-acid transaminase
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

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[edit]

  • MEISTER A, FRASER PE (1954). "Enzymatic formation of L-asparagine by transamination". J. Biol. Chem. 210 (1): 37–43. PMID 13201567.