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malfunction
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expression of the R107C mutant variant SCAD protein gives rise to inactive misfolded protein species, eliciting a mild toxic response manifested though a decreased proliferation rate and oxidative stress, as shown by an increased demand for the mitochondrial antioxidant SOD2, occurance of increased markers of apoptotic activity in the mutant protein expressing cells. Development of a cell model system, stably expressing either the SCAD wild-type protein or the misfolding SCAD variant protein, R107C, genotype C319T. The model system is used for investigation of SCAD with respect to expression, degree of misfolding, and enzymatic SCAD activity, overview
malfunction
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patients with mutated beta-oxidation enzyme short-chain 3-hydroxyacyl-CoA dehydrogenase show hyperinsulinemia associated with non-ketotic hypoglycemia, analysis of the mechanism underlying HADHSC-mediated regulation of insulin secretion, overview. Enhanced glucose-stimulated insulin secretion induced by HADHSC knockdown is independent of changes in cytosolic Ca2+ and also occurs in the presence of fatty acids. The pan transaminase inhibitor amino-oxyacetate reverses HADHSC knockdown-mediated increases in glucose-stimulated insulin secretion. Oxidation of palmitate and octanoate is not reduced in HADHSC knockdown cells. L-3-Hydroxybutyryl-carnitine and L-3-hydroxyglutarate, which accumulate in blood and urine, respectively, of HADHSC-deficient patients, do not change insulin secretion. Transamination reaction(s) and the formation of short-chain acylcarnitines and CoAs may be implicated in the mechanism whereby HADHSC deficiency results in enhanced insulin secretion and hyperinsulinemia
malfunction
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SCAD deficiency causes a defect in the beta-oxidation of short-chain fatty acids of four to eight carbons in length. The majority of individuals with short-chain acyl-CoA dehydrogenase deficiency have normal growth and development. Two variants in the ACADS gene, 625G-A and 511C-T, are commonly found in the general population, that are associated with ethylmalonic aciduria and some decreased enzyme activity
metabolism
mutations in the gene encodine acyl-CoA dehydrogenase, ACAD, cause alterations in SCAD activity, overview
metabolism
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SCAD functions in mitochondria and is involved in the beta-oxidation of fatty acyl-CoA compounds in chains of 4-6 carbons.The mitochondrial pathway of fatty acid beta-oxidation is an alternative source of energy, especially during stress or fasting
metabolism
butyryl-CoA dehydrogenase from Clostridium difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NADH with the endergonic reduction of ferredoxin by NADH
metabolism
the genes necessary for butyrate formation from the genome of Clostridium difficile are expressed in Escherichia coli. The individual genes are assembled in a single plasmid vector into an artificial operon , which allows functional coexpression of the required genes and confers butyrate-forming capability to the host
physiological function
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Clostridium homopropionicum using the acryloyl-CoA pathway with low growth yield obtains its specific competitive advantage compared to Propionibacterium freudenreichii not through higher substrate affinity or metabolic shift toward enhanced acetate-plus-hydrogen formation but through faster specific substrate turnover
physiological function
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SCAD catalyzes the dehydrogenation of butyryl-CoA during the first step of the short-chain fatty acid beta-oxidation spiral
physiological function
SCAD is a mitochondrial enzyme involved in the beta-oxidation of fatty acids and mediates the metabolic transition from acyl-CoA with four or six carbon chains to 2-enoyl-CoA in the first step of the beta-oxidation spiral. Genetic defect of SCAD cause clinical symptoms such as progressive psychomotor retardation, muscle hypotonia, and myopathy
physiological function
the bifurcating electron transferring flavoprotein (EtfAf) and butyryl-CoA dehydrogenase (BcdAf) of Acidaminococcus fermentans couples the exergonic reduction of crotonyl-CoA to butyryl-CoA to the endergonic reduction of ferredoxin both with NADH. NADH reduces beta-FAD of Etf, which bifurcates one electron reduces the Dh-FAD (dehydrogenase FAD) of butyryl-CoA dehydrogenase, and the other goes to ferredoxin characterized by a low redox potential. Repetition of this process leads to a second reduced ferredoxin and butyryl-CoA upon hydride transfer from FADH- of butyryl-CoA dehydrogenase to crotonyl-CoA
physiological function
short-chain acyl-CoA dehydrogenase (SCAD) is the rate-limiting enzyme in fatty acid beta-oxidation. It has a negative regulatory effect on pathological cardiac hypertrophy and fibrosis
physiological function
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short-chain acyl-CoA dehydrogenase (SCAD) is the rate-limiting enzyme in fatty acid beta-oxidation. It has a negative regulatory effect on pathological cardiac hypertrophy and fibrosis
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physiological function
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the bifurcating electron transferring flavoprotein (EtfAf) and butyryl-CoA dehydrogenase (BcdAf) of Acidaminococcus fermentans couples the exergonic reduction of crotonyl-CoA to butyryl-CoA to the endergonic reduction of ferredoxin both with NADH. NADH reduces beta-FAD of Etf, which bifurcates one electron reduces the Dh-FAD (dehydrogenase FAD) of butyryl-CoA dehydrogenase, and the other goes to ferredoxin characterized by a low redox potential. Repetition of this process leads to a second reduced ferredoxin and butyryl-CoA upon hydride transfer from FADH- of butyryl-CoA dehydrogenase to crotonyl-CoA
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additional information
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patients with short-chain acyl-CoA dehydrogenase deficiency, a rare disorder of fatty acid oxidation, may show an increased risk of thyroid and other autoimmune diseases. The pathologic phenotype can include pernicious anaemia, vitiligo, autoimmune thyroiditis and lichen scleroatrophicus, overview
additional information
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SCAD misfolding leads to production of reactive oxygen species, which in turn leads to fission and a grain-like structure of the mitochondrial reticulum, indicating a toxic response elicited by misfolded R83C SCAD proteins, detailed overview
additional information
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short-chain acyl-CoA dehydrogenase deficiency, SCADD, is an autosomal recessive inborn error of mitochondrial fatty acid oxidation due to mutations in the SCAD protein. SCADD is biochemically characterized by increased C4-carnitine in plasma and ethylmalonic acid in urine, phenotype, overview
additional information
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short-chain acyl-CoA dehydrogenase-deficient mice, SCAD-/- mice, have increased brown adipose tissue mass as well as modest cardiac hypertrophy. Uncoupling protein-1 is reduced by 70% in brown adipose tissue, not due to a change in mitochondrial number, nor to decreased signal transduction through protein kinase A, which is known to be a major regulator of uncoupling protein-1 expression, phenotype, overview. Reduced brown adipose tissue function is not the major factor causing cold sensitivity in acyl-CoA dehydrogenase knockout strains, but other mechanisms such as shivering capacity, cardiac function, and reduced hepatic glycogen stores are involved
additional information
modeling of structures of the EtfAf-ferredoxin and EtfAf-BcdAf enzyme complexes
additional information
modeling of structures of the EtfAf-ferredoxin and EtfAf-BcdAf enzyme complexes
additional information
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modeling of structures of the EtfAf-ferredoxin and EtfAf-BcdAf enzyme complexes
additional information
FAD inhibits PE-induced cardiomyocyte hypertrophy via activating the enzyme, phenotype, overview
additional information
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FAD inhibits PE-induced cardiomyocyte hypertrophy via activating the enzyme, phenotype, overview
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additional information
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modeling of structures of the EtfAf-ferredoxin and EtfAf-BcdAf enzyme complexes
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