EC Number   |
General Information |
Reference |
|---|
    1.3.8.1 | malfunction |
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 |
725641 |
| 1.3.8.1 | malfunction |
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 |
725613 |
| 1.3.8.1 | malfunction |
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 |
725105 |
| 1.3.8.1 | 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 |
725287 |
| 1.3.8.1 | metabolism |
mutations in the gene encodine acyl-CoA dehydrogenase, ACAD, cause alterations in SCAD activity, overview |
712126 |
| 1.3.8.1 | metabolism |
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 |
712123 |
| 1.3.8.1 | 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 |
725287 |
| 1.3.8.1 | more |
FAD inhibits PE-induced cardiomyocyte hypertrophy via activating the enzyme, phenotype, overview |
-, 762716 |
| 1.3.8.1 | more |
modeling of structures of the EtfAf-ferredoxin and EtfAf-BcdAf enzyme complexes |
-, 742866 |
| 1.3.8.1 | more |
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 |
712123 |
