Recombinant Human MLYCD/MCD protein is a Human Full Length protein, in the 1 to 493 aa range, expressed in Wheat germ and suitable for ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes 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.
MCD, MLYCD
Recombinant Human MLYCD/MCD protein is a Human Full Length protein, in the 1 to 493 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Catalyzes 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.
Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 by SIRT4 represses activity, leading to promote lipogenesis (By similarity).
This product was previously labelled as MLYCD.
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.
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.
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.
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.
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ab161633 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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