Biology:Aspartyltransferase
From HandWiki
| aspartyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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.
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