EC Number   |
General Information |
Reference |
|---|
    4.1.1.9 | evolution |
the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis |
-, 728812 |
| 4.1.1.9 | malfunction |
decreased fat oxidation in enzyme-deficient mice results in the accumulation of lipid intermediates in peripheral tissues, but this is not associated with a worsening of age-associated insulin resistance and, conversely, improves longevity. This improvement is associated with reduced oxidative stress and reduced acetylation of the antioxidant enzyme superoxide dismutase 2 in muscle but not the liver |
747635 |
| 4.1.1.9 | malfunction |
enzyme inhibition by an ultrasound-mediated injection of miRNA into the rat myocardium increases energy reserves in the left ventricle after myocardial infarction |
747464 |
| 4.1.1.9 | malfunction |
impact of loss-of-function alleles in hereditary MCD deficiency |
728812 |
| 4.1.1.9 | malfunction |
MLYCD deficiency, OMIM 248360, also known as malonic aciduria, is a rare autosomal recessively inherited inborn error of fatty acid metabolism. A patient with this enzyme deficiency shows signs of neonatal hypoglycemia, mental retardation, developmental delay and rheumatoid arthritis. The brain shows patchy, symmetrical hyperintensity of the deep white matter with periventricular white matter and subcortical arcuate fibers being spared. Protein mislocalization to the nucleus is a characteristic feature of MLYCD deficiency in the patient. Phenotype, overview. The phenotype probably involves mutations H152N and M1K |
727260 |
| 4.1.1.9 | malfunction |
pharmacological inhibition of malonyl-CoA decarboxylase reduces the inflammatory response associated with insulin resistance. Additionally, inhibition of MCD strongly diminishes lipopolysaccharide-induced activation of palmitate oxidation and prevents lipopolysaccharide-induced collapse of total cellular antioxidant capacity and prevents increases in the level of ceramide in cardiomyocytes and macrophages while also ameliorating LPS-initiated decreases in PPAR binding. Genetic inactivation of malonyl-CoA decarboxylase protects mice against high-fat diet-induced insulin resistance |
726656 |
| 4.1.1.9 | more |
catalytic domain structure and active site structure comparisons, overview |
-, 728812 |
| 4.1.1.9 | more |
catalytic domain structure and active site structure, with His-Ser/Thr dyad, comparisons, overview. The catalytic domain of MCD contains a central eight-stranded, mostly antiparallel etab sheet (beta1-beta8) that is surrounded by at least 11 alpha helices. The substrate can position its thioester carbonyl, bridging the carboxylate leaving group and CoA backbone, in the vicinity of Ser329 and His423 |
728812 |
| 4.1.1.9 | more |
structural asymmetry and disulfide bridges among subunits modulate the activity of the enzyme. The molecular organization of dimer of structural heterodimers, in which the two subunits present markedly different conformations, is consistent with half-of-the-sites reactivity. Interactions extend beyond the C-terminal targeting motif. Active site structure, overview |
727943 |
| 4.1.1.9 | physiological function |
a two week induction of the enzyme in skeletal muscle does not alter body weight or ameliorate glucose intolerance, conversely it further impairs insulin signaling in the skeletal muscle of diet-induced obese mice. Furthermore, an acute induction of the enzyme leads to a suppression of fatty acid oxidative genes suggesting a redundant and metabolite driven regulation of gene expression |
747402 |
