High impact information on ACACA

• Carboxylation of this labeled propionyl-CoA by propionyl-CoA carboxylase from pig heart and acetyl-CoA carboxylase from the uropygial gland completely removed 3H [1].
• These results show that: (a) the decarboxylase is stereospecific, (b) replacement of the carboxyl group by hydrogen occurs with retention of configuration, (c) acetyl-CoA carboxylase of the uropygial gland generates (S)-methylmalonyl-CoA from propionyl-CoA, and (d) fatty acid synthetase is not stereospecific for methylmalonyl-CoA [1].
• Stereospecificity of malonyl-CoA decarboxylase, acetyl-CoA carboxylase, and fatty acid synthetase from the uropygial gland of goose [1].
• Association between hydrogen peroxide-dependent byproducts of ascorbic acid and increased hepatic acetyl-CoA carboxylase activity [2].
• However, the decrease in malonyl CoA cannot be explained by a decrease in ACC activity [3].

Biological context of ACACA

• Assignment of acetyl-coenzyme A carboxylase alpha (ACACA) to pig chromosome 12 (12p13-->p12) by fluorescence in situ hybridization and confirmation by genetic mapping [4].
• Porcine somatotropin decreases acetyl-CoA carboxylase gene expression in porcine adipose tissue [5].
• Diet M increased lipogenesis (estimated from the activities of acetyl-CoA-carboxylase, malic enzyme and glucose-6-phosphate dehydrogenase), and decreased delta 9-desaturase activity, in comparison to the other diets [6].
• Pig coronary smooth muscle cells contain a highly active fatty acid beta-oxidation system as well as significant activities of other enzymes involved in lipid metabolism, i.e. palmitoyl-CoA synthetase, glycerophosphate acyl transferase, acetyl-CoA carboxylase and fatty acid synthetase [7].

Anatomical context of ACACA

• The acitivity of acetyl CoA carboxylase, fatty acid synthetase, citrate cleavage enzyme, nicotinamide adenine dinucleotide phosphat-malate dehydrogenase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase was considerably higher in adipose tissue than in other tissues tested, paralleling its high lipogenic capacity [8].
• Subcutaneous adipose tissue samples were taken from the shoulder area of nonfasted animals at 28-day intervals from 3 to 6 months of age for determination of in vitro lipogenic, lipolytic and acetyl CoA carboxylase activities [9].

Associations of ACACA with chemical compounds

• The activity of AMP-dependent protein kinase (AMPK), which phosphorylates and inactivates ACC, was also not significantly different in the dobutamine hearts compared to the saline hearts (322 +/- 26 vs. 338 +/- 39 pmol. min-1. mg protein-1, respectively) [3].
• Malonyl CoA is produced from acetyl CoA in a reaction catalyzed by acetyl CoA carboxylase (ACC) [3].
• The transcripts of the lipogenic enzymes fatty acid synthase, acetyl-CoA carboxylase, and stearoyl-CoA desaturase were elevated in the ethanol-fed groups, and each was positively correlated to liver homocysteine levels [10].
• Acetyl-CoA carboxylase, malic enzyme and glucose-6-phosphate dehydrogenase are more active in the inner layer, while 6-phosphogluconate and isocitrate dehydrogenases are distinguishable in the two layers of adipose tissue as well if age, sex, and breeding line are taken into consideration [11].

Other interactions of ACACA

• The activities of beta-hydroxy-beta-methylglutaryl coenzyme A (HMG-CoA) reductase, cholesterol 7 alpha-hydroxylase, acetyl-CoA carboxylase (ACX), fatty acid synthetase (FAS) and other lipogenic enzymes in several tissues were determined [12].

References