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malonyl-CoA decarboxylase N-terminal domain-containing protein
This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidised. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK) [1]. [1]. 12065578. Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise. Park H, Kaushik VK, Constant S, Prentki M, Przybytkowski E, Ruderman NB, Saha AK;. J Biol Chem 2002;277:32571-32577. (from Pfam)
malonyl-CoA decarboxylase domain-containing protein
malonyl-CoA decarboxylase
malonyl-CoA decarboxylase (MCD) is a key intermediate in the biosynthesis of long-chain and very long-chain fatty acids, and also has a crucial role in the regulation of fatty acid oxidation through its potent inhibition of carnitine palmitoyltransferase I
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