Recombinant Human Malonyl-CoA decarboxylase, mitochondrial (MLYCD)
Description
Purity > 90% as determined by SDS-PAGE. MW: 55.9kDa. Full Length of Mature Protein: 40-493aa. N-terminal 10xHis-tagged and C-terminal Myc-tagged. Homo sapiens (Human). 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.