Recombinant Human Malonyl-CoA decarboxylase, mitochondrial (MLYCD), Truncated

Uniprot Id

O95822

Target Species

Human

Target Name

MLYCD

Target Full Name

Malonyl-CoA decarboxylase, mitochondrial

Target 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.

Target Involvement

Malonyl-CoA decarboxylase deficiency (MLYCD deficiency)

Target Subcellular Location

Cytoplasm. Mitochondrion matrix. Peroxisome. Peroxisome matrix.

Target Tissue Specificity

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.

Target Research Area

others

Target Synonyms

DCMC_HUMAN; hMCD; Malonyl CoA decarboxylase; Malonyl CoA decarboxylase mitochondrial; Malonyl coenzyme A decarboxylase; Malonyl-CoA decarboxylase; MCD; MGC59795; mitochondrial; Mlycd

Target Background

The product of this gene catalyzes the breakdown of malonyl-CoA to acetyl-CoA and carbon dioxide. Malonyl-CoA is an intermediate in fatty acid biosynthesis, and also inhibits the transport of fatty acyl CoAs into mitochondria. Consequently, the encoded protein acts to increase the rate of fatty acid oxidation. It is found in mitochondria, peroxisomes, and the cytoplasm. Mutations in this gene result in malonyl-CoA decarboyxlase deficiency.