Hysteretic behaviour of carnitine palmitoyltransferase. The effect of preincubation with malonyl-CoA.

No abstract is available for this paper.

• Publication year

  1986

• Venue

  Biochemical Journal

• Publication date

  1986-06-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1042/BJ2360917PMID 3790097PMCID PMC1146927
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Alteration of the apparent Ki of carnitine palmitoyltransferase for malonyl-CoA by the diabetic state and reversal by insulin.

  1985cited by this paper
• Effects of the mode of addition of acyl-CoA on the initial rate of formation of acylcarnitine in the presence of carnitine by intact rat liver mitochondria in vitro.

  1985cited by this paper
• Phosphorylation of carnitine palmitoyltransferase and activation by glucagon in isolated rat hepatocytes

  1985cited by this paper
• Differences in the sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA are due to differences in Ki values.

  1984cited by this paper
• Time-dependence of inhibition of carnitine palmitoyltransferase I by malonyl-CoA in mitochondria isolated from livers of fed or starved rats. Evidence for transition of the enzyme between states of low and high affinity for malonyl-CoA.

  1984cited by this paper
• Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA.

  1984cited by this paper
• Increased sensitivity of carnitine palmitoyltransferase I activity to malonyl-CoA inhibition after preincubation of intact rat liver mitochondria with micromolar concentrations of malonyl-CoA in vitro.

  1983cited by this paper
• Sensitivity of carnitine acyltransferase I to malonly-CoA inhibition in isolated rat liver mitochondria is quantitatively related to hepatic malonyl-CoA concentration in vivo.

  1982cited by this paper
• Carnitine acyltransferase activities in rat liver and heart measured with palmitoyl-CoA and octanoyl-CoA. Latency, effects of K+, bivalent metal ions and malonyl-CoA.

  1982cited by this paper
• Evaluation of malonyl-CoA in the regulation of long-chain fatty acid oxidation in the liver. Evidence for an unidentified regulatory component of the system.

  1980cited by this paper
• Differential inhibition of ketogenesis by malonyl-CoA in mitochondria from fed and starved rats.

  1980cited by this paper
• Ketogenesis and malonyl coenzyme A content of isolated rat hepatocytes.

  1978cited by this paper
• Effect of glucagon on hepatic malonyl coenzyme A concentration and on lipid synthesis.

  1977cited by this paper

• Fatty Acid Chain Elongation in Palmitate-perfused Working Rat Heart

  2014cites this paper
• The Role of Carnitine in Cell Metabolism

  1997cites this paper
• Regulation of fatty acid oxidation in mammalian liver.

  1993cites this paper
• Regulation of mitochondrial carnitine palmitoyl transferases from liver and extrahepatic tissues.

  1992cites this paper
• Cholate separates the catalytic and malonyl-CoA-binding components of carnitine palmitoyltransferase from liver outer mitochondrial membranes.

  1991cites this paper
• L-carnitine acyltransferase in intact peroxisomes is inhibited by malonyl-CoA.

  1989cites this paper
• Carnitine.

  1988cites this paper
• Effect of malonyl-CoA on the kinetics and substrate cooperativity of membrane-bound carnitine palmitoyltransferase of rat heart mitochondria.

  1987cites this paper
• Studies on the activation in vitro of carnitine palmitoyltransferase I in liver mitochondria from normal, diabetic and glucagon-treated rats.

  1987cites this paper