We tested the hypothesis that the level of malonyl-CoA, as well as the corresponding rate of total fatty acid oxidation of the heart, is regulated by the opposing actions of acetyl-CoA carboxylase (ACC) and malonyl-CoA decarboxylase (MCD). We used isolated working rat hearts perfused under physiological conditions. MCD in heart homogenates was measured specifically by14CO2production from [3-14C...

The protein substrates of sirtuin 5-regulated lysine malonylation (Kmal) remain unknown, hindering its functional analysis. In this study, we carried out proteomic screening, which identified 4042 Kmal sites on 1426 proteins in mouse liver and 4943 Kmal sites on 1822 proteins in human fibroblasts. Increased malonyl-CoA levels in malonyl-CoA decarboxylase (MCD)-deficient cells induces Kmal level...

Goodwin, Gary W., and Heinrich Taegtmeyer. Regulation of fatty acid oxidation of the heart by MCD and ACC during contractile stimulation. Am. J. Physiol. 277 (Endocrinol. Metab. 40): E772–E777, 1999.—We tested the hypothesis that the level of malonyl-CoA, as well as the corresponding rate of total fatty acid oxidation of the heart, is regulated by the opposing actions of acetyl-CoA carboxylase ...

Kinetic studies of the pigeon liver fatty acid synthetase have revealed that the enzyme is sensitive to inhibition by malonyl coenzyme A, one of the substrates of fatty acid synthesis. The inhibition is of the mixed type with respect to acetyl-CoA, and is competitive with respect to TPNH. Malonyl-CoA most markedly affects the K, for TPNH, increasing it 19-fold over a malonyl-CoA concentration r...

Autotrophic members of the Sulfolobales (Crenarchaeota) contain acetyl-coenzyme A (CoA)/propionyl-CoA carboxylase as the CO2 fixation enzyme and use a modified 3-hydroxypropionate cycle to assimilate CO2 into cell material. In this central metabolic pathway malonyl-CoA, the product of acetyl-CoA carboxylation, is further reduced to 3-hydroxypropionate. Extracts of Metallosphaera sedula containe...

A number of laboratories (l-4) have investigated the biosynthesis of mevalonic acid from acetate or acetyl coenzyme ,4 by yeast and animal enzyme systems. These investigations have indicated that acetoacetyl coenzyme A and P-hydroxy-P-methylglutaryl coenzyme A glutaryl are intermediates in the formation of mevalonic acid. However, the synthesis in vitro of sterols from acetate by subcellular, r...

Myocardial fatty acid oxidation is regulated by carnitine palmitoyltransferase I (CPT I), which is inhibited by malonyl-CoA. Increased cardiac power causes a fall in malonyl-CoA content and accelerated fatty acid oxidation; however, the mechanism for the decrease in malonyl-CoA is unclear. Malonyl-CoA is formed by acetyl-CoA carboxylase (ACC) and degraded by malonyl-CoA decarboxylase (MCD); thu...

This multienzyme complex behaves during protein fractionation, centrifugation, and electrophoresis as a single protein particle of molecular weight 2.3 x 106 (ref. [ 11). The synthesis of fatty acids requires at least six different enzymatic steps which have been demonstrated with the help of model substrates [2]. After transfer of acetyland malonyl-residues from acetylCoA and malonyl-CoA to th...

Malonyl coenzyme A (malonyl-CoA) is an important precursor for the synthesis of natural products, such as polyketides and flavonoids. The majority of this cofactor often is consumed for producing fatty acids and phospholipids, leaving only a small amount of cellular malonyl-CoA available for producing the target compound. The tuning of malonyl-CoA into heterologous pathways yields significant p...