Reaction participants Show >> << Hide
- Name help_outline (R)-carnitine Identifier CHEBI:16347 (Beilstein: 4292315,5732837; CAS: 541-15-1) help_outline Charge 0 Formula C7H15NO3 InChIKeyhelp_outline PHIQHXFUZVPYII-ZCFIWIBFSA-N SMILEShelp_outline C[N+](C)(C)C[C@H](O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 48 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,190 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-dehydrocarnitine Identifier CHEBI:57885 Charge 0 Formula C7H13NO3 InChIKeyhelp_outline YNOWULSFLVIUDH-UHFFFAOYSA-N SMILEShelp_outline C[N+](C)(C)CC(=O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,120 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:25330 | RHEA:25331 | RHEA:25332 | RHEA:25333 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Purification and properties of carnitine dehydrogenase from Pseudomonas putida.
Goulas P.
Carnitine dehydrogenase (carnitine:NAD+ oxidoreductase, EC 1.1.1.108) from Pseudomonas putida IFP 206 catalyzes the oxidation of L-carnitine to 3-dehydrocarnitine. The enzyme was purified 72-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The molecular mass of this enzyme is 6 ... >> More
Carnitine dehydrogenase (carnitine:NAD+ oxidoreductase, EC 1.1.1.108) from Pseudomonas putida IFP 206 catalyzes the oxidation of L-carnitine to 3-dehydrocarnitine. The enzyme was purified 72-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The molecular mass of this enzyme is 62 kDa and consists of two identical subunits. The isoelectric point was found to be 4.7. the carnitine dehydrogenase is specific for L-carnitine and NAD+. The optimum pH for enzymatic activity in the oxidation reaction was found to be 9.0 and 7.0 in the reduction reaction. The optimal temperature is 30 degrees C. The Km values for substrates were determined. << Less
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Purification and properties of L(-)-carnitine dehydrogenase from Agrobacterium sp.
Hanschmann H., Ehricht R., Kleber H.P.
L(-)-Carnitine:NAD+ oxidoreductase, EC 1.1.1.108, from Agrobacterium sp. catalyzes the oxidation of L(-)-carnitine to 3-dehydrocarnitine as initial step of L(-)-carnitine degradation. The enzyme was purified 76-fold by four chromatographic steps. A high substrate specificity for L(-)-carnitine and ... >> More
L(-)-Carnitine:NAD+ oxidoreductase, EC 1.1.1.108, from Agrobacterium sp. catalyzes the oxidation of L(-)-carnitine to 3-dehydrocarnitine as initial step of L(-)-carnitine degradation. The enzyme was purified 76-fold by four chromatographic steps. A high substrate specificity for L(-)-carnitine and NAD+ was observed. The molecular mass of the native enzyme is 114 kDa and it consists of two identical subunits as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The isoelectric point was found to be 5.2-5.4. The optimum temperature is 45 degrees C and the optimum pH for the oxidation and the reduction reaction are 9.5 and 5.5-6.5, respectively. Kinetic parameters and amino-terminal sequence were determined. The oxidation reaction is inhibited by D(+)-carnitine, trimethylamine, several metal ions and cetyltrimethylammoniumbromide (CTAB). << Less
Biochim Biophys Acta 1290:177-183(1996) [PubMed] [EuropePMC]