Biology:Aspartyltransferase
From HandWiki
aspartyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.3.2.7 | ||||||||
CAS number | 37257-23-1 | ||||||||
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 aspartyltransferase (EC 2.3.2.7) is an enzyme that catalyzes the chemical reaction
- L-asparagine + hydroxylamine [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Aspartotransferase from Mycobacterium tuberculosis H37Ra". Indian J. Biochem. 6: 106–110. 1969.
![]() | Original source: https://en.wikipedia.org/wiki/Aspartyltransferase.
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