Enzymes
| UniProtKB help_outline | 4 proteins |
Reaction participants Show >> << Hide
- Name help_outline (R)-carnitine Identifier CHEBI:16347 (Beilstein: 5732837,4292315; 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 47 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O-acyl-(R)-carnitine Identifier CHEBI:75659 Charge 0 Formula C8H14NO4R SMILEShelp_outline C[N+](C)(C)C[C@@H](CC([O-])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 46 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:49924 | RHEA:49925 | RHEA:49926 | RHEA:49927 | |
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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
Specific form(s) of this reaction
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RHEA:49920
(R)-carnitine(out) + O-octanoyl-(R)-carnitine(in) = (R)-carnitine(in) + O-octanoyl-(R)-carnitine(out)
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RHEA:49916
(R)-carnitine(out) + O-hexadecanoyl-(R)-carnitine(in) = (R)-carnitine(in) + O-hexadecanoyl-(R)-carnitine(out)
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RHEA:49912
(R)-carnitine(out) + O-propanoyl-(R)-carnitine(in) = (R)-carnitine(in) + O-propanoyl-(R)-carnitine(out)
- RHEA:49908
Publications
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Bacterial overexpression, purification, and reconstitution of the carnitine/acylcarnitine carrier from rat liver mitochondria.
Indiveri C., Iacobazzi V., Giangregorio N., Palmieri F.
The carnitine/acylcarnitine carrier from rat liver mitochondria was overexpressed in Escherichia coli. The expressed protein, recovered as inclusion bodies, was solubilized with sarkosyl and purified by Sephadex G-200 and celite chromatography. A yield of 15 mg of purified transport protein per li ... >> More
The carnitine/acylcarnitine carrier from rat liver mitochondria was overexpressed in Escherichia coli. The expressed protein, recovered as inclusion bodies, was solubilized with sarkosyl and purified by Sephadex G-200 and celite chromatography. A yield of 15 mg of purified transport protein per liter of cell culture was obtained. Upon reconstitution into liposomes, the purified carrier catalyzed a [3H]carnitine/carnitine exchange inhibited by maleimides, mercurials, and sulfobetaines. Carnitine esters of various lengths were also transported. The Km for carnitine uptake was 0.47 +/-0.11 mM, the Vmax of the exchange was 0.78 +/-0.24 mmol/min per gram of protein, and the Ki for octanoylcarnitine was 13.5 +/-4.3 microM. The transport properties of the recombinant carrier were virtually identical to those of the native transporter. These studies represent the first overexpression of the functionally active mitochondrial carnitine/acylcarnitine carrier, thus enabling structure/function analysis of this protein by site-directed mutagenesis. << Less
Biochem. Biophys. Res. Commun. 249:589-594(1998) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.