Glutaryl-CoA dehydrogenase, a multifunctional enzyme responsible for dehydrogenation and decarboxylation of glutaryl-CoA to crotonyl-CoA, has been purified 1,680-fold from porcine liver mitochondria. The purified porcine enzyme has a subunit molecular weight of 47,800 and a native molecular weight of 190,500. Porcine glutaryl-CoA dehydrogenase catalyzed the conversion of [1,5-14C]glutaryl-CoA t...

Rat liver mitochondria metabolize glutarate at a very slow rate as compared with glutaryl coenzyme A. The stimulatory effect of citric acid cycle intermediates, NAD, and coenzyme A on glutarate metabolism was interpreted as a manifestation of their involvement in the activation of glutarate by a thiol transferase with succinyl-Cob as the coenzyme A donor. Glutaryl-CoA dehydrogenase, which catal...

Patients with glutaric aciduria (GA) have greatly increased urinary excretion of glutarate. Their leukocyte and fibroblast sonicates have deficient ability to produce 14CO2 from [1,5-14C]glutaryl-CoA, an enzymatic process with two sequential reaction steps, dehydrogenation and decarboxylation. In normal individuals, it is not known whether these two reaction steps require one or two enzymes, an...

Glutaric aciduria type 1 (glutaryl-CoA dehydrogenase deficiency, glutaric acidemia 1) (OMIM 231670) is an autosomal recessive disease caused by mutations in the gene encoding enzyme glutaryl-CoA (GCDH). Glutaryl-CoA (GCDH) plays important role degradation metabolism of L-lysine, L-hydroxylysine and L-tryptophan. The insufficiency or absence leads to accumulation by-products such amino acids as ...

Glutaryl-coenzyme A (CoA) dehydrogenase and the electron transfer flavoprotein (ETF) of Paracoccus denitrificans were purified to homogeneity from cells grown with glutaric acid as the carbon source. Glutaryl-CoA dehydrogenase had a molecular weight of 180,000 and was made up of four identical subunits with molecular weights of about 43,000 each of which contained one flavin adenine dinucleotid...

In anaerobic bacteria using aromatic growth substrates, glutaryl-coenzyme A (CoA) dehydrogenases (GDHs) are involved in the catabolism of the central intermediate benzoyl-CoA to three acetyl-CoAs and CO(2). In this work, we studied GDHs from the strictly anaerobic, aromatic compound-degrading organisms Geobacter metallireducens (GDH(Geo)) (Fe[III] reducing) and Desulfococcus multivorans (GDH(De...

A C7 dicarboxylic (pimelic) acid derivative is postulated as an intermediate in anaerobic degradation of benzoate. Four strains of Gram-negative, nitrate-reducing bacteria capable of growth with both pimelate and benzoate as sole carbon and energy source were isolated. The metabolism of strain LP-1, which was enriched from activated sludge with pimelate as substrate, was studied in detail. This...