Rat liver glucokinase is specifically inhibited by palmitoyl-CoA and other long chain acyl-CoAs at concentrations well below their critical micelle concentrations (Tippett, P. S., and Neet, K. E. (1982) J. Biol. Chem. 257, 12839-12845). Kinetic studies of this inhibition indicate that the long chain acyl-CoAs act on glucokinase through an allosteric site. The inhibition is competitive with both...

The boronated nucleosides with varying bases and sugar moieties were shown to be potent hypolipidemic agents in rodents. The 3'- aminocynaoborane dideoxythymidine derivative caused reductions in serum cholesterol and triglyceride levels, tissue lipids, VLDL and LDL cholesterol levels while elevating HDL cholesterol levels in rodents. The agents suppressed rat hepatic acetyl CoA synthetase, HMG-...

1. The effect of nutritional status on fatty acid synthesis in brown adipose tissue was compared with the effect of cold-exposure. Fatty acid synthesis was measured in vivo by 3H2O incorporation into tissue lipids. The activities of acetyl-CoA carboxylase and fatty acid synthetase and the tissue concentrations of malonyl-CoA and citrate were assayed. 2. In brown adipose tissue of control mice, ...

In eukaryotes, L-carnitine is involved in energy metabolism by facilitating beta-oxidation of fatty acids. Carnitine acetyltransferases (CrAT) catalyze the reversible conversion of acetyl-CoA and carnitine to acetylcarnitine and free CoA. To redesign the specificity of rat CrAT toward its substrates, we mutated Met564. The M564G mutated CrAT showed higher activity toward longer chain acyl-CoAs:...

The enoyl reductase from Mycobacterium tuberculosis (MtInhA) was shown to be a major target for isoniazid, the most prescribed first-line anti-tuberculosis agent. MtInhA (EC 1.3.1.9) protein catalyzes hydride transfer 4S hydrogen of β-NADH carbon-3 long-chain 2-trans-enoyl thioester substrates (enoyl-ACP or enoyl-CoA) yield NAD+ and acyl-ACP acyl-CoA products. latter are long carbon chains mero...

We describe the enzymic determination of free fatty acids in serum with use of acyl-CoA synthetase (EC l.2.1.3), acyl-CoA oxidase (no EC no. assigned) and peroxidase (EC 1.11.1.7). The free fatty acids are activated by acyl-CoA synthetase in the presence of ATP and coenzyme A. The acyl-CoA formed is oxidized by acyl-CoA oxidase to enoyl-CoA with simultaneous production of hydrogen peroxide, whi...