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Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.
Gene References into Functions
To identify the active site of MCD, molecular docking and molecular dynamics simulations were performed to explore the interactions of human mitochondrial MCD (HmMCD) and CoA derivatives. The findings reveal that the active site of HmMCD indeed resides in the prominent groove which resembles that of curacin A. PMID: 26948533
Our result expands the phenotype of malonyl-CoA decarboxylase deficiency and suggests attentions should be paid to the mild form of disorders, for example, malonyl-CoA decarboxylase deficiency, which usually present a severe disease course. PMID: 26858006
The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily. PMID: 23791943
Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase. PMID: 23482565
Our case emphasizes the need for ongoing cardiac disease screening in patients with MCD deficiency and the benefits and limitations of current dietary interventions. PMID: 22778304
This study of fatty acid oxidation and malonyl-CoA decarboxylase identifies a critical role for metabolism in both the normal pulmonary circulation (hypoxic pulmonary vasoconstriction) and pulmonary hypertension PMID: 20702857
Malonyl-CoA decarboxylase deficiency may result from MLYCD mutations that result in protein mistargeting. PMID: 12955715
The concentration of malonyl-CoA is diminished in muscle after physical training, most likely because of PGC-1alpha-mediated increases in MCD expression and activity. PMID: 16434556
analysis of nine novel MLYCD mutations in patients with malonyl-coenzyme A decarboxylase deficiency PMID: 17186413
MCD silencing suppresses lipid uptake and enhances glucose uptake in primary human myotubes. PMID: 18314420
Data suggest that increased expression of malonyl CoA decarboxylase, and the decreased expression of acetyl CoA carboxylase and 5'-AMP activated protein kinase are important regulators of the maturation of fatty acid oxidation in the newborn human heart. PMID: 18614968
Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine.