Malonyl-CoA Decarboxylase (丙二酰辅酶 A 脱羧酶)

Malonyl-CoA Decarboxylase (MCD) is responsible for catalyzing the decomposition of Malonyl-CoA into Acetyl-CoA and carbon dioxide, playing a regulatory role in the oxidation and synthesis of fatty acids. Malonyl-CoA is not only a precursor for fatty acid synthesis but also inhibits the entry of fatty acids into mitochondria for β-oxidation. Inhibiting MCD activity can increase the content of Malonyl-CoA in the myocardium, thereby reducing the rate of fatty acid oxidation and increasing pyruvate oxidation. This metabolic change helps enhance heart function and efficiency, especially under conditions of cardiac ischemia, demonstrating potential in research into ischemic heart diseases.
MCD activity is also related to obesity and metabolic disorders. Studies show that the enzyme SIRT4 can deacetylate MCD, reducing its activity, thereby regulating the concentration of Malonyl-CoA and balancing the synthesis and decomposition of fatty acids. Mice lacking SIRT4 exhibit increased exercise endurance and resistance to diet-induced obesity, highlighting the critical role of MCD in regulating energy metabolism and weight management.
Furthermore, in studies on pulmonary hypertension, mice lacking MCD do not exhibit pulmonary artery constriction in low-oxygen environments and do not develop pulmonary hypertension under chronic hypoxia. This suggests that inhibiting MCD may prevent vascular remodeling and apoptosis associated with pulmonary hypertension by altering the balance of fatty acid and sugar metabolism.
Regulating MCD activity provides a new direction for research into heart diseases, pulmonary hypertension, and metabolic disorders^[1][2][3].