LMPD Database

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LMP012822

UniProt Annotations

Entry Information
Gene Namemalonyl-CoA decarboxylase
Protein EntryDCMC_RAT
UniProt IDQ920F5
SpeciesRat
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative initiation; Named isoforms=2; Comment=According to PubMed:10229677, a single transcription start site has been demonstrated.; Name=Mitochondrial; IsoId=Q920F5-1; Sequence=Displayed; Name=Cytoplasmic+peroxisomal; IsoId=Q920F5-2; Sequence=VSP_018818; Note=May be produced by alternative initiation at Met-39 of isoform mitochondrial. Alternatively, represents a proteolytic processed form of the mitochondrial form (PubMed:10947976). ;
Biophysicochemical PropertiesKinetic parameters: KM=0.36 mM for malonyl-CoA ;
Catalytic ActivityMalonyl-CoA = acetyl-CoA + CO(2). {ECO:0000269|PubMed:10229677, ECO:0000269|PubMed:12297032, ECO:0000269|PubMed:16298369}.
Enzyme RegulationMalonyl-CoA decarboxylase activity does not require any cofactors or divalent metal ions
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. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:10947976, ECO:0000269|PubMed:15105298, ECO:0000269|PubMed:16298369}.
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 (By similarity)
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
Subcellular LocationCytoplasm . Mitochondrion matrix . Peroxisome {ECO:0000250}. Peroxisome matrix . Note=Enzymatically active in all three subcellular compartments.
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)
Tissue SpecificityExpressed in liver, heart, skeletal muscles and adipose tissues (at protein level). Ubiquitous. Strongly expressed in liver, kidney, heart, skeletal muscle and adipose tissues. Weakly expressed in brain. {ECO:0000269|PubMed:10229677, ECO:0000269|PubMed:10455107, ECO:0000269|PubMed:10947976, ECO:0000269|PubMed:12297032}.