Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.3.1.8 (acyl-CoA dehydrogenase)
 785 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Weanling rats were fed a riboflavin-deficient diet. The mitochondrial fatty acid oxidation in liver was depressed in riboflavin deficiency but restored after supplementation of riboflavin. Among the enzymes involved in this system, only the acyl-CoA dehydrogenase (EC 1.3.99.2 and 1.3.99.3) activities varied with the change in fatty acid oxidation. An accumulation of the apoforms of acyl-CoA dehydrogenases was found in riboflavin deficiency. The levels of electron transfer flavoprotein and other enzymes involved in the beta-oxidation system remained unchanged. The peroxisomal fatty acid oxidation and levels of individual enzymes of this system remained constant. No accumulation of the apoform of acyl-CoA oxidase was observed under simple, riboflavin-deficient conditions. However, accumulation of a large amount of apo-acyl-CoA oxidase was observed when the peroxisomal system was induced by administration of a peroxisome proliferator, di(2-ethylhexyl)phthalate, under riboflavin-deficient conditions.
 ...
PMID:Riboflavin deficiency and beta-oxidation systems in rat liver. 714 48

Three acyl-CoA dehydrogenases and electron transfer flavoprotein, which catalyze the initial step of mitochondrial fatty acid beta-oxidation, were purified from livers of rats fed a diet containing di(2-ethylhexyl)phthalate. Three acyl-CoA dehydrogenases, classified into short chain, general, and long chain acyl-CoA dehydrogenases on the basis of their substrate specificities, each consisted of four subunits of identical size: the molecular weights of the native enzymes were 169,000 for short chain acyl-CoA dehydrogenase, 182,000 for general acyl-CoA dehydrogenase, and 168,000 for long chain acyl-CoA dehydrogenase. Electron transfer flavoprotein with a molecular weight of 57,000 consisted of heterogeneous subunits with molecular weight of 33,500 and 25,100. The catalytic properties and molecular structures of rat liver acyl-CoA dehydrogenases were similar to those of the enzymes purified from other mammalian tissues such as pig heart, pig liver, and beef kidney. We could not obtain purified preparations of the three acyl-CoA dehydrogenases from livers of the control rats although the three dehydrogenases were completely separated from each other. The enzymes from the control and the di(2-ethylhexyl)phthalate-treated rats were compared and no differences were found in molecular sizes of the native enzymes and of their subunits, substrate specificities and immunochemical reactivities.
 ...
PMID:Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein. 733 8