Molecular enzymology of carnitine transfer and transport.
@article{Ramsay2001MolecularEO, title={Molecular enzymology of carnitine transfer and transport.}, author={Rona R. Ramsay and Richard D Gandour and Feike R van der Leij}, journal={Biochimica et biophysica acta}, year={2001}, volume={1546 1}, pages={ 21-43 } }
352 Citations
The Carnitine Transporter Network: Interactions with Drugs
- Biology
- 2010
The current knowledge of the characterization of the carnitine transporter network and the interaction with drugs are reviewed with emphasis to the most recent data obtained using the proteoliposome reconstituted systems.
Crystal Structure of Carnitine Acetyltransferase and Implications for the Catalytic Mechanism and Fatty Acid Transport
- Biology, ChemistryCell
- 2003
Structural and Biochemical Studies of the Substrate Selectivity of Carnitine Acetyltransferase*
- BiologyJournal of Biological Chemistry
- 2004
Kinetic studies confirm that the M 564G or M564A mutation is sufficient to increase the activity of the enzyme toward medium-chain substrates with hexanoyl-CoA being the preferred substrate for the M5 64G mutant, and crystal structures of two of these mutants reveal a deep binding pocket that can accommodate the larger acyl group.
Characterization of carnitine and fatty acid metabolism in the long-chain acyl-CoA dehydrogenase-deficient mouse.
- BiologyThe Biochemical journal
- 2005
It is concluded that the cardiomyopathy in the LCAD-/- mouse is caused primarily by a severe energy deficiency in the heart, stressing the important role of LCAD in cardiac fatty acid metabolism in the mouse.
A Novel Mitochondrial Carnitine-acylcarnitine Translocase Induced by Partial Hepatectomy and Fasting*
- Biology, Computer ScienceJournal of Biological Chemistry
- 2003
A novel mammalian protein homologous to CACT, designated as CACL (CACT-like), is localized to the mitochondria and has palmitoylcarnitine transporting activity and may be specialized for the metabolism of a distinct class of fatty acids involved in brain function.
Structure and Function of Carnitine Acyltransferases
- Biology, ChemistryAnnals of the New York Academy of Sciences
- 2004
The crystal structures of murine CrAT are determined, providing a molecular basis for understanding the catalysis by carnitine acyltransferases and for designing their inhibitors, and structural information suggests that the substrate Carnitine may assist theCatalysis by stabilizing the oxyanion in the reaction intermediate.
Structure of Human Carnitine Acetyltransferase
- Biology, ChemistryThe Journal of Biological Chemistry
- 2003
The x-ray structure of human carnitine acetyltransferase provides critical insights into the molecular basis for fatty acyl chain transfer and a possible common mechanism among a wide range of acyltransferases utilizing a catalytic dyad.
Carnitine acyltransferases and their influence on CoA pools in health and disease.
- BiologyMolecular aspects of medicine
- 2004
References
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The kinetic mechanisms and kinetic parameters for the carnitine acyl transferases purified from peroxisomes and from the mitochondrial inner membrane were determined and support the concept of three binding domains for the acyltransferases, a CoA site, an acyl site and a Carnitine site.
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Molecular Biology of Carnitine Palmitoyltransferases and Role of Carnitine in Gene Transcription
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It is concluded that the mechanism of action of carnitine acetyltransferase involves four binary and two or more ternary enzyme complexes in rapid equilibrium with free substrates, the interconversion of the ternARY complexes being the rate-limiting step.
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The last group has been unequivocally identified as the 3'-phosphate of CoA, by showing that the K(m) of carnitine acetyltransferase for the substrate acetyl-3'-dephospho-CoA is independent of pH in the range 6.0-7.8.
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Key developments of the last 20 years that have led to the current understanding of the physiology of the CPT system, the structure of theCPT isoforms, the chromosomal localization of their respective genes, and the identification of mutations in the human population are reviewed.