// Workers AI · dad joke modeWhat did aspartyltransferase say? I'm bonding with you.
| Aspartyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.2.7 | ||||||||
| CAS no. | 37257-23-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Aspartyltransferase (EC 2.3.2.7) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme characterised from Mycobacterium tuberculosis are L-asparagine and hydroxylamine, which are converted to the hydroxamate, β-L-aspartylhydroxamic acid and ammonia.[1]
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.[2]
References
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