Asparagine-oxo-acid transaminase

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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 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.

[edit] References

• IUBMB entry for 2.6.1.14
• BRENDA references for 2.6.1.14 (Recommended.)
• PubMed references for 2.6.1.14
• PubMed Central references for 2.6.1.14
• Google Scholar references for 2.6.1.14
• MEISTER A, FRASER PE (1954). "Enzymatic formation of L-asparagine by transamination". J. Biol. Chem. 210: 37–43. PMID 13201567. 

[edit] External links

The CAS registry number for this enzyme class is 9030-43-7.

• IUBMB entry for 2.6.1.14

• KEGG entry for 2.6.1.14

• BRENDA entry for 2.6.1.14

• NiceZyme view of 2.6.1.14

• EC2PDB: PDB structures for 2.6.1.14

• PRIAM entry for 2.6.1.14

• PUMA2 entry for 2.6.1.14

• IntEnz: Integrated Enzyme entry for 2.6.1.14

• MetaCyc entry for 2.6.1.14

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0047297: asparagine-oxo-acid transaminase

• AMIGO entry for GO code 0047297: asparagine-oxo-acid transaminase