N-benzyloxycarbonylglycine hydrolase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.58 | ||||||||
CAS no. | 91930-69-7 | ||||||||
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-benzyloxycarbonylglycine hydrolase (EC 3.5.1.58) is an enzyme that catalyzes the chemical reaction
- N-benzyloxycarbonylglycine + H2O benzyl alcohol + CO2 + glycine
Thus, the two substrates of this enzyme are N-benzyloxycarbonylglycine and H2O, whereas its 3 products are benzyl alcohol, CO2, and glycine.
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-benzyloxycarbonylglycine urethanehydrolase. Other names in common use include benzyloxycarbonylglycine hydrolase, Nalpha-carbobenzoxyamino acid amidohydrolase, Nalpha-benzyloxycarbonyl amino acid urethane hydrolase, and Nalpha-benzyloxycarbonyl amino acid urethane hydrolase I. It has 2 cofactors: zinc, and Cobalt.
References
- Murao S, Matsumura E, Kawano T (1985). "Isolation and Characterization of a Novel Enzyme, Nα-Benzyloxycarbonyl Amino Acid Urethane Hydrolase, from Streptococcus faecalis R ATCC 8043". Agricultural and Biological Chemistry. 49 (4): 967–72. doi:10.1271/bbb1961.49.967.
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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