Biology:Carnitinamidase
From HandWiki
| carnitinamidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.5.1.73 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a carnitinamidase (EC 3.5.1.73) is an enzyme that catalyzes the chemical reaction
- L-carnitinamide + H2O [math]\displaystyle{ \rightleftharpoons }[/math] L-carnitine + NH3
Thus, 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.[1]
References
- ↑ "Carnitinamidase". Enzyme Handbook. 16. Heidelberg: Springer, Berlin. 1998. pp. 609–612. doi:10.1007/978-3-642-58903-4_118. ISBN 978-3-642-58903-4.
Further reading
- Nakayama K, Honda H, Ogawa Y, Ozawa T, Ohta T, "Method for producing carnitine, L-carnitinamide hydrolase and method for producing same", US patent 4918012, issued 17 April 1990, assigned to Kyowa Hakko Kogyo Co Ltd.
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