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anti-Human MLYCD Antibodies:
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Human Polyclonal MLYCD Primary Antibody for WB - ABIN525162
Kulkarni, Salehzadeh, Fritz, Zierath, Krook, Osler: Mitochondrial regulators of fatty acid metabolism reflect metabolic dysfunction in type 2 diabetes mellitus. in Metabolism: clinical and experimental 2012
To identify the active site of MCD, molecular docking and molecular dynamics simulations were performed to explore the interactions of human mitochondrial MCD (HmMCD) and CoA derivatives. The findings reveal that the active site of HmMCD indeed resides in the prominent groove which resembles that of curacin A.
Our result expands the phenotype of malonyl-CoA decarboxylase deficiency and suggests attentions should be paid to the mild form of disorders, for example, malonyl-CoA decarboxylase deficiency, which usually present a severe disease course.
The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily.
Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.
Our case emphasizes the need for ongoing cardiac disease screening in patients with MCD deficiency and the benefits and limitations of current dietary interventions.
This study of fatty acid oxidation and malonyl-CoA decarboxylase identifies a critical role for metabolism in both the normal pulmonary circulation (hypoxic pulmonary vasoconstriction) and pulmonary hypertension
Malonyl-CoA decarboxylase deficiency may result from MLYCD mutations that result in protein mistargeting.
The concentration of malonyl-CoA is diminished in muscle after physical training, most likely because of PGC-1alpha-mediated increases in MCD expression and activity.
analysis of nine novel MLYCD mutations in patients with malonyl-coenzyme A decarboxylase deficiency
MCD silencing suppresses lipid uptake and enhances glucose uptake in primary human myotubes.
Data suggest that increased expression of malonyl CoA decarboxylase, and the decreased expression of acetyl CoA carboxylase and 5'-AMP activated protein kinase are important regulators of the maturation of fatty acid oxidation in the newborn human heart.
Decreased fat oxidation in MCD(-/-) mice resulted in the accumulation of lipid intermediates in peripheral tissues, but this was not associated with a worsening of age-associated insulin resistance and, conversely, improved longevity.
MCD(-/-) mice consistently exhibited cardiac dysfunction and severe metabolic perturbations while on a high-fat, low carbohydrate diet of maternal milk and these gradually resolved post-weaning.
Data indicate that a full-dosage of p53 and an intact ribosomal protein-murine double minute 2 protein (Mdm2)-p53 pathway are required for the induction of malonyl coA decarboxylase (MCD), a critical regulator of fatty acid oxidation.
SIRT4 deacetylates and represses malonyl CoA decarboxylase, regulating malonyl coA levels.
In vivo and ex vivo cardiac function is similar in wild-type and mcd-deficient mice; however, deletion of MCD markedly increases glucose oxidation and improves functional recovery of the heart after ischemia.
Mcd deficiency is not detrimental to the heart in obesity in mice.
The product of this gene catalyzes the breakdown of malonyl-CoA to acetyl-CoA and carbon dioxide. Malonyl-CoA is an intermediate in fatty acid biosynthesis, and also inhibits the transport of fatty acyl CoAs into mitochondria. Consequently, the encoded protein acts to increase the rate of fatty acid oxidation. It is found in mitochondria, peroxisomes, and the cytoplasm. Mutations in this gene result in malonyl-CoA decarboyxlase deficiency.
MaLonyl CoA Decarboxylase family member (mlcd-1)
, malonyl coenzyme A decarboxylase
, malonyl-CoA decarboxylase, mitochondrial