Kinetic, Circular Dichroism and Fluorescence Studies on Heterologously Expressed Carnitine Palmitoyltransferase II
| Autor: | Carol J. Dragland, William R. Mann, Philip A. Bell, Bing Yan |
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| Rok vydání: | 1995 |
| Předmět: |
Reaction mechanism
Circular dichroism Protein Conformation Stereochemistry Kinetics Mitochondria Liver Biochemistry Carnitine medicine Animals Carnitine palmitoyltransferase II Alkyl chemistry.chemical_classification Carnitine O-Palmitoyltransferase Palmitoyl Coenzyme A Chemistry Circular Dichroism Recombinant Proteins Rats Dissociation constant Spectrometry Fluorescence Enzyme Molecular Medicine lipids (amino acids peptides and proteins) medicine.drug |
| Zdroj: | Journal of Enzyme Inhibition. 9:303-308 |
| ISSN: | 8755-5093 |
| DOI: | 10.3109/14756369509036559 |
| Popis: | Km estimates for carnitine and palmitoyl-CoA of heterologously expressed rat liver carnitine palmitoyl-transferase-II (rCPT-II) were 950 +/- 27 microM and 34 +/- 6 microM, respectively. Vmax for the enzyme was 1.8 mumol/min/mg purified protein. Consistent with an ordered reaction mechanism in which palmitoyl-CoA binds first, SDZ CPI 975, a reversible carnitine palmitoyltransferase inhibitor containing both carnitine and alkyl moieties, inhibited rCPT-II competitively with carnitine and uncompetitively with palmitoyl-CoA. Substrate-enzyme interactions were examined by circular dichroism (CD) and fluorescence. Both carnitine and palmitoyl-CoA alone induced conformational changes in the enzyme; dissociation constant estimates by CD for carnitine and palmitoyl-CoA were 41 +/- 5 microM and 7 +/- 2 microM, respectively. |
| Databáze: | OpenAIRE |
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