Biology:N-acyl-D-aspartate deacylase
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N-acyl-D-aspartate deacylase | |||||||||
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Identifiers | |||||||||
EC number | 3.5.1.83 | ||||||||
CAS number | 9031-86-1 | ||||||||
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, a N-acyl-D-aspartate deacylase (EC 3.5.1.83) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-aspartate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] a carboxylate + D-aspartate
Thus, the two substrates of this enzyme are N-acyl-D-aspartate and H2O, whereas its two products are carboxylate and D-aspartate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-aspartate amidohydrolase. It employs one cofactor, zinc.
References
- "Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". Biosci. Biotechnol. Biochem. 57 (7): 1145–8. 1993. doi:10.1271/bbb.57.1145. PMID 7763985.
- "Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". J. Ferment. Bioeng. 80 (4): 311–317. 1995. doi:10.1016/0922-338X(95)94197-Y.
Original source: https://en.wikipedia.org/wiki/N-acyl-D-aspartate deacylase.
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