| 4-acetamidobutyryl-CoA deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.51 | ||||||||
| 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 4-acetamidobutyryl-CoA deacetylase (EC 3.5.1.51) is an enzyme that catalyzes the chemical reaction
- 4-acetamidobutanoyl-CoA + H2O acetate + 4-aminobutanoyl-CoA
acetate + 4-aminobutanoyl-CoAThus, the two substrates of this enzyme are 4-acetamidobutanoyl-CoA and H2O, whereas its two products are acetate and 4-aminobutanoyl-CoA.
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 4-acetamidobutanoyl-CoA amidohydrolase. Other names in common use include aminobutyryl-CoA thiolesterase, and deacetylase-thiolesterase.
References
- Ohsugi M, Kahn J, Hensley C, Chew S, Barker HA (1981). "Metabolism of L-beta-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds". J. Biol. Chem. 256 (14): 7642–51. PMID 6788773.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 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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