malonyl-CoA decarboxylase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: malonyl-CoA = acetyl-CoA + CO2. [EC:4.1.1.9, MetaCyc:MALONYL-COA-DECARBOXYLASE-RXN]

Malonyl-CoA decarboxylase (MCD) activity is a crucial enzymatic process involved in the metabolism of fatty acids. This activity is catalyzed by the enzyme malonyl-CoA decarboxylase, which specifically removes a carboxyl group from malonyl-CoA, a key intermediate in fatty acid biosynthesis. The reaction involves the conversion of malonyl-CoA to acetyl-CoA and carbon dioxide. This decarboxylation reaction plays a pivotal role in regulating fatty acid synthesis by controlling the availability of malonyl-CoA, a potent inhibitor of carnitine palmitoyltransferase 1 (CPT1). CPT1 is a key enzyme involved in the transport of long-chain fatty acids into mitochondria for beta-oxidation, the process of fatty acid breakdown. Therefore, by reducing malonyl-CoA levels, MCD activity indirectly promotes fatty acid oxidation. Furthermore, MCD activity is essential for the biosynthesis of certain specialized fatty acids, such as those found in the myelin sheath that insulates nerve cells. In summary, malonyl-CoA decarboxylase activity is a critical enzymatic step that regulates fatty acid metabolism and plays a role in various cellular processes.'
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Proteins (2)

Compounds (1)