| Post Translational Modifications | Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 by SIRT4 represses activity, leading to promote lipogenesis. Interchain disulfide bonds may form in peroxisomes (Potential). Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria. |
| Function | 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. |
| Protein Name | Malonyl-Coa Decarboxylase - MitochondrialMcd |
| Database Links | Reactome: R-HSA-390247 O95822-2Reactome: R-HSA-9033241 O95822-2 |
| Cellular Localisation | CytoplasmMitochondrion MatrixPeroxisomePeroxisome MatrixEnzymatically Active In All Three Subcellular Compartments |
| Alternative Protein Names | Malonyl-Coa Decarboxylase - Mitochondrial proteinMcd proteinMLYCD protein |
Information sourced from Uniprot.org
