LMPD Database

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LMP000544

UniProt Annotations

Entry Information
Gene Namemalonyl-CoA decarboxylase
Protein EntryDCMC_MOUSE
UniProt IDQ99J39
SpeciesMouse
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative initiation; Named isoforms=2; Comment=A single transcription start site has been demonstrated in Rat.; Name=Mitochondrial; IsoId=Q99J39-1; Sequence=Displayed; Name=Cytoplasmic+peroxisomal; IsoId=Q99J39-2; Sequence=VSP_018817; Note=May be produced by alternative initiation at Met-39 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form.;
Catalytic ActivityMalonyl-CoA = acetyl-CoA + CO(2). {ECO:0000269|PubMed:17030679}.
Disruption PhenotypeMice show an increased expression of genes regulating fatty acid utilization and likely contributes to the absence of changes in energy metabolism in the aerobic heart. Display a preference for glucose utilization after ischemia and improve functional recovery of the heart. {ECO:0000269|PubMed:17030679}.
Enzyme RegulationMalonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions. {ECO:0000250}.
FunctionCatalyzes 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. Plays a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:17030679, ECO:0000269|PubMed:23746352}.
PathwayMetabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1.
PtmAcetylation at Lys-471 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-471 by SIRT4 represses activity, leading to promote lipogenesis. {ECO:0000269|PubMed:23576753, ECO:0000269|PubMed:23746352}.
PtmInterchain disulfide bonds may form in peroxisomes (Potential). Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria. {ECO:0000305}.
Subcellular LocationCytoplasm {ECO:0000250}. Mitochondrion matrix {ECO:0000269|PubMed:23746352}. Peroxisome {ECO:0000250}. Peroxisome matrix {ECO:0000250}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250}.
SubunitHomotetramer. Dimer of dimers. The two subunits within a dimer display conformational differences suggesting that at any given moment, only one of the two subunits is competent for malonyl-CoA binding and catalytic activity. Under oxidizing conditions, can form disulfide-linked homotetramers (in vitro). Associates with the peroxisomal targeting signal receptor PEX5 (By similarity). {ECO:0000250}.