| carnitinamidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.73 | ||||||||
| CAS no. | 117444-04-9 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a carnitinamidase (EC 3.5.1.73) is an enzyme that catalyzes the chemical reaction
- L-carnitinamide + H2O L-carnitine + NH3
L-carnitine + NH3Thus, the two substrates of this enzyme are L-carnitinamide and H2O, whereas its two products are L-carnitine and NH3.
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 L-carnitinamide amidohydrolase. Other names in common use include L-carnitinamidase, carnitine amidase, and L-carnitine amidase.
References
- Schomburg D, Stephan D (1998). "Carnitinamidase". Enzyme Handbook. Vol. 16. Heidelberg: Springer, Berlin. pp. 609–612. doi:10.1007/978-3-642-58903-4_118. ISBN 978-3-642-58903-4.
Further reading
- US 4918012, Nakayama K, Honda H, Ogawa Y, Ozawa T, Ohta T, "Method for producing carnitine, L-carnitinamide hydrolase and method for producing same", issued 17 April 1990, assigned to Kyowa Hakko Kogyo Co Ltd.
| 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 | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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