FEBS letters, 2000-01, Vol.466 (1), p.183-186
2000
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- Autor(en) / Beteiligte
- Titel
- Identification of the two histidine residues responsible for the inhibition by malonyl-CoA in peroxisomal carnitine octanoyltransferase from rat liver
- Ist Teil von
- FEBS letters, 2000-01, Vol.466 (1), p.183-186
- Ort / Verlag
- England: Elsevier B.V
- Erscheinungsjahr
- 2000
- Quelle
- Wiley-Blackwell Journals
- Beschreibungen/Notizen
- Carnitine octanoyltransferase (COT), an enzyme that facilitates the transport of medium chain fatty acids through peroxisomal membranes, is inhibited by malonyl-CoA. cDNAs encoding full-length wild-type COT and one double mutant variant from rat peroxisomal COT were expressed in Saccharomyces cerevisiae. Both expressed forms were expressed similarly in quantitative terms and exhibited full enzyme activity. The wild-type-expressed COT was inhibited by malonyl-CoA like the liver enzyme. The activity of the enzyme encoded by the double mutant H131A/H340A was completely insensitive to malonyl-CoA in the range assayed (2–200 μM). These results indicate that the two histidine residues, H131 and H340, are the sites responsible for inhibition by malonyl-CoA. Another mutant variant, H327A, abolishes the enzyme activity, from which it is concluded that it plays an important role in catalysis.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0014-5793eISSN: 1873-3468DOI: 10.1016/S0014-5793(99)01788-3Titel-ID: cdi_crossref_primary_10_1016_S0014_5793_99_01788_3
- Format
- –
- Schlagworte
- Amino Acid Sequence, Animals, Base Sequence, Carnitine Acyltransferases - antagonists & inhibitors, Carnitine Acyltransferases - chemistry, Carnitine Acyltransferases - genetics, Carnitine octanoyltransferase, Catalytic Domain - genetics, CM(−ura), complete minimal medium lacking uracil, COT, carnitine octanoyltransferase, CPT, carnitine palmitoyltransferase, DNA Primers - genetics, DNA, Complementary - genetics, Gene Expression, Histidine - chemistry, Humans, In Vitro Techniques, Inhibitory kinetics, Kinetics, Liver - enzymology, Malonyl Coenzyme A - pharmacology, Malonyl-coenzyme A, Mutagenesis, Site-Directed, Peroxisome, Peroxisomes - enzymology, Point Mutation, Rat liver, Rats, Recombinant Proteins - antagonists & inhibitors, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Saccharomyces cerevisiae - genetics, Sequence Homology, Amino Acid, Site-directed mutagenesis