Aspartyltransferase

From Wikipedia, the free encyclopedia

In enzymology, an aspartyltransferase (EC 2.3.2.7) is an enzyme that catalyzes the chemical reaction

L-asparagine + hydroxylamine NH₃ + L-aspartylhydroxamate

Thus, the two substrates of this enzyme are L-asparagine and hydroxylamine, whereas its two products are NH₃ and L-aspartylhydroxamate.

This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-asparagine:hydroxylamine gamma-aspartyltransferase. Other names in common use include beta-aspartyl transferase, and aspartotransferase.

[edit] References

• IUBMB entry for 2.3.2.7
• BRENDA references for 2.3.2.7 (Recommended.)
• PubMed references for 2.3.2.7
• PubMed Central references for 2.3.2.7
• Google Scholar references for 2.3.2.7
• Jayaram HN, Ramakrishnan T and Vaidyanathan CS (1969). "Aspartotransferase from Mycobacterium tuberculosis H37Ra". Indian J. Biochem. 6: 106–110. 

[edit] External links

The CAS registry number for this enzyme class is 37257-23-1.

• IUBMB entry for 2.3.2.7

• KEGG entry for 2.3.2.7

• BRENDA entry for 2.3.2.7

• NiceZyme view of 2.3.2.7

• EC2PDB: PDB structures for 2.3.2.7

• PRIAM entry for 2.3.2.7

• PUMA2 entry for 2.3.2.7

• IntEnz: Integrated Enzyme entry for 2.3.2.7

• MetaCyc entry for 2.3.2.7

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0047690: aspartyltransferase

• AMIGO entry for GO code 0047690: aspartyltransferase