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Aspartyltransferase

From Wikipedia, the free encyclopedia
aspartyltransferase
Identifiers
EC no.2.3.2.7
CAS no.37257-23-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

References

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  • Jayaram HN, Ramakrishnan T, Vaidyanathan CS (1969). "Aspartotransferase from Mycobacterium tuberculosis H37Ra". Indian J. Biochem. 6: 106–110.