Acetyl-CoA carboxylase is thought to be absent in the heart since the latter is highly catabolic and nonlipogenic. It has been suggested that the high level of malonyl-CoA that is found in the heart is derived from mitochondrial propionyl-CoA carboxylase, which also uses acetyl-CoA. In the present study, acetyl-CoA carboxylase was identified and purified from homogenates of rat heart. The isola...

The isolation and biochemical properties of a Saccharomyces cerevisiae mutant (acc1-167) defective in acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP forming), EC 6.4.1.2] activity are described. The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth. Fatty acid synthetase ...

A protein kinase which phosphorylates and inactivates acetyl-CoA carboxylase has been purified to apparent homogeneity from rat liver. The kinase was found to exist in two forms: bound to carboxylase in a complex or in a free form that is in different stages of aggregation over a wide range of molecular weights. The purification of the kinase involved first partial purification of acetyl-CoA ca...

Acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] is activated by physiological concentrations of CoA. The CoA concentration dependency of this activation is sigmoidal; below 60 microM there is little or no activation, but the activation observed between 60 and 120 microM indicates that small changes in the concentration of CoA can cause significant changes in ...

Acetyl-CoA Carboxylase catalyzes the first committed step in fatty acid synthesis. Escherichia coli acetyl-CoA carboxylase is composed of biotin carboxylase, carboxyltransferase and biotin carboxyl carrier protein functions. The accA and accD genes that code for the alpha- and beta-subunits, respectively, are not in an operon, yet yield an alpha(2)beta(2) carboxyltransferase. Here, we report th...

The activation of hepatic acetyl-CoA carboxylase by Na(+)-cotransported amino acids such as glutamine has been attributed mainly to the stimulation of its dephosphorylation by accumulating dicarboxylic acids, e.g. glutamate. We report here on a hepatic species of protein phosphatase-2A that activates acetyl-CoA carboxylase in the presence of physiological concentrations of glutamate or Mg2+ and...

Acetyl-CoA carboxylase from yeast was isolated in homogeneous form and compared in its properties with pyruvate carboxylase from yeast. Both enzymes have very similar sedimentation coefficients and molecular weights. Both enzymes are composed of four protomers. Acetyl-CoA carboxylase and pyruvate carboxylase split under identical conditions into a variety of aggregates; besides the protomer, di...

Acetyl-coenzyme A carboxylase α (ACC-alpha) is considered as the key regulatory enzyme in fatty acid biosynthesis. ACC-alpha gene is located on Caprine chromosome 11 and is polymorphic in many goat breeds. In the current study, we aimed to find possible single nucleotide polymorphisms (SNPs) in the exon 1 region of the ACC-alpha gene in Iranian Mahabadi goat breed. Genomic DNA was extracted fro...

Pseudomonas putida is evolutionarily endowed with features relevant for bioproduction, especially under harsh operating conditions. The rich metabolic versatility of this species, however, comes at the price limited formation acetyl-coenzyme A (CoA) from sugar substrates. Since acetyl-CoA a key precursor number added-value products, in work we deployed an silico-guided rewiring program central ...