N-acyl-D-aspartate deacylase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.83 | ||||||||
CAS no. | 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 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
- Moriguchi M, Sakai K, Katsuno Y, Maki T, Wakayama M (1993). "Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". Biosci. Biotechnol. Biochem. 57 (7): 1145–8. doi:10.1271/bbb.57.1145. PMID 7763985.
- Sakai K, Moriguchi M (1995). "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. doi:10.1016/0922-338X(95)94197-Y.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
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3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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