Conditions have been developed for the solubilization of hepatic microsomal carnitine acyltransferase activity in good yield, with excellent long-term stability and with retention of malonyl-CoA sensitivity. Solubilized microsomal carnitine acyltransferase activity can be separated into malonyl-CoA-sensitive and -insensitive activities either by gel filtration on Superdex 200 or by anion-exchan...

Blackcurrant leaves are an essential source of phenolic compounds and this study investigated their variation relative to leaf positions and harvest date. The phenolic content varied between harvest dates, although leaf position on the shoot and interactions also played an important role. The contents of quercetin-malonyl-glucoside, kaempferol-malonyl-glucoside isomer and kaempferol-malonyl-glu...

We have investigated the extent to which membrane environment affects the catalytic properties of the malonyl-CoA-sensitive carnitine acyltransferase of liver microsomal membranes. Arrhenius-type plots of activity were linear in the absence and presence of malonyl-CoA (2.5 microM). Sensitivity to malonyl-CoA increased with decreasing assay temperature. Partly purified enzyme displayed an increa...

F atty a cid s ynthase ( FAS) inhibition initiates selective ap optosis o f can cer cel ls b oth in vivo and in vitro, which m ay i nvolve malonyl-CoA metabolism. T hese findings l ed to exploration of malonyl-CoA decarboxylase ( MCD) as a p otential novel target for cancer treatment. M CD regulates the levels of cellular malonyl-CoA through the decarboxylation of malonyl-CoA to acetyl-CoA. Mal...

1. [14C]Malonyl-CoA bound to intact mitochondria isolated from rat liver and heart in a manner consistent with the presence of two independent classes of binding sites in each tissue. 2. The binding characteristics for mitochondria obtained from fed male rats were: for heart, KD(1) = 1 -l8 nM, KD(2) = 30uM, N1 = 7pmol/mg of protein, N2 = approx. 660pmol/mg of protein; for liver, KD(1) = 0.1 M, ...

We have measured rates of ketogenesis and malonyl-CoA contents of hepatocytes isolated from meal-fed rats under a variety of incubation conditions in order to determine the relationship between the intracellular malonyl-CoA level and the rate of ketogenesis. Evidence obtained from rat liver homogenates suggested that malonyl-CoA, which is a major determinant of fatty acid synthesis in vivo, als...

Participation of cytochrome b5 in the liver microsomal elongation of fatty acids in the rat is suggested by (a) an increase in the rate of reoxidation of liver microsomal cytochrome b5, following reduction by NADH, in the presence of both malonyl coenzyme A and ATP, and (b) a 60% inhibition of incorporation of malonyl-CoA into microsomal fatty acids in the presence of anti-cytochrome b6 IgG; co...

Malonyl-CoA acutely regulates fatty acid oxidation in liver in vivo by inhibiting carnitine palmitoyltransferase. Thus rapid increases in the concentration of malonyl-CoA, accompanied by decreases in long-chain fatty acyl carnitine (LCFA-carnitine) and fatty acid oxidation have been observed in liver of fasted-refed rats. It is less clear that it plays a similar role in skeletal muscle. To exam...

Pig and rat liver carnitine palmitoyltransferase I (L-CPTI) share common K(m) values for palmitoyl-CoA and carnitine. However, they differ widely in their sensitivity to malonyl-CoA inhibition. Thus, pig l-CPTI has an IC(50) for malonyl-CoA of 141 nm, while that of rat L-CPTI is 2 microm. Using chimeras between rat L-CPTI and pig L-CPTI, we show that the entire C-terminal region behaves as a si...

Malonyl-CoA is the building block for fatty acid biosynthesis and also a precursor to various pharmaceutically and industrially valuable molecules, such as polyketides and biopolymers. However, intracellular malonyl-CoA is usually maintained at low levels, which poses great challenges to efficient microbial production of malonyl-CoA derived molecules. Inactivation of the malonyl-CoA consumption...