Anti-MLYCD/MCD antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The MLYCD protein also known as malonyl-CoA decarboxylase (MCD) is an enzyme with a molecular mass of approximately 55 kDa. It is primarily located in the cytosol mitochondria and peroxisomes of cells. MLYCD functions by decarboxylating malonyl-CoA to acetyl-CoA and carbon dioxide playing an important role in the regulation of fatty acid metabolism and energy production.

Biological function summary

MLYCD converts malonyl-CoA an inhibitor of mitochondrial fatty acid oxidation into acetyl-CoA. This conversion permits fatty acids to enter mitochondria for beta-oxidation. It is not typically part of larger protein complexes but can interact with other molecules regulating lipid metabolism. Through these interactions it indirectly influences cellular energy balance and lipid biosynthesis.

Pathways

MLYCD is involved in the fatty acid metabolism pathway and energy homeostasis. Within these it serves as a regulatory point influencing the balance between fat utilization and storage. MLYCD maintains balance alongside proteins such as carnitine palmitoyltransferase 1A (CPT1A) which controls the entry of fatty acids into mitochondria for beta-oxidation linking these pathways.

Associated diseases and disorders

MLYCD connects to metabolic conditions like malonyl-CoA decarboxylase deficiency and Type 2 diabetes. In malonyl-CoA decarboxylase deficiency reduced activity of MLYCD leads to the accumulation of malonyl-CoA affecting the energy metabolism. In Type 2 diabetes dysregulation of MLYCD can influence insulin sensitivity and lipid metabolism. Its role makes it critical for understanding metabolic health and disease with connections to proteins such as CPT1A and ACC (acetyl-CoA carboxylase) in these contexts.