Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate

  title={Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate},
  author={Ulrich H{\"a}rtel and Elke Eckel and J{\"u}rgen Koch and Georg Fuchs and Dietmar Linder and Wolfgang Buckel},
  journal={Archives of Microbiology},
Cell-free extracts of Pseudomonas sp. strains KB 740 and K 172 both contained high levels of glutaryl-CoA dehydrogenase when grown anaerobically on benzoate or other aromatic compounds and with nitrate as electron acceptor. [] Key Result These aromatic compounds have in common benzoyl-CoA as the central aromatic intermediate of anerobic metabolism. The enzymatic activity was almost absent in cells grown aerobically on benzoate regardless whether nitrate was present.
Decarboxylating and Nondecarboxylating Glutaryl-Coenzyme A Dehydrogenases in the Aromatic Metabolism of Obligately Anaerobic Bacteria
Highly conserved amino acid residues that were proposed to be specifically involved in the decarboxylation of the intermediate glutaconyl-CoA were identified inGDH(Geo) but are missing in GDH(Des), and the differential use of energy-yielding/energy-demanding enzymatic processes in anaerobic bacteria that degrade aromatic compounds is discussed.
Identification and analysis of a glutaryl-CoA dehydrogenase-encoding gene and its cognate transcriptional regulator from Azoarcus sp. CIB.
In this work, the gcdH gene from the denitrifying beta-proteobacterium Azoarcus sp. CIB was shown to encode a glutaryl-CoA dehydrogenase, which is essential for the anaerobic catabolism of many
Activation and degradation of benzoate, 3-phenylpropionate and crotonate bySyntrophus buswellii strain GA. Evidence for electron-transport phosphorylation during crotonate respiration
A strictly anaerobic, benzoate-degrading bacterium,Syntrophus buswellii strain GA, was able to degrade benzoate or 3-phenylpropionate to acetate, CO2 and H2 if the hydrogen partial pressure was
Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ3-Δ2-isomerase
The finding of this dehydratase means that all of the enzymes necessary for fermentation of succinate plus ethanol by C. kluyveri have now been demonstrated to exist in this organism and confirms the proposed pathway involving a reduction of succinated via 4-hydroxybutyrate to butyrate.
Hydroquinone degradation via reductive dehydroxylation of gentisyl-CoA by a strictly anaerobic fermenting bacterium
Anaerobic degradation of hydroquinone was studied with the fermenting bacterium strain HQGö1 and gentisyl-CoA was reduced to benzoyl- CoA with reduced methyl viologen as electron donor by simultaneous reductive elimination of both the ortho and meta hydroxyl group.
The pimFABCDE operon from Rhodopseudomonas palustris mediates dicarboxylic acid degradation and participates in anaerobic benzoate degradation.
The finding that the pim operon deletion mutant is still able to grow on dicarboxylic acids, albeit at a slower rate, indicates that R. palustris has additional genes that can also specify the degradation of these compounds.
Glutaryl‐coenzyme A dehydrogenase from Geobacter metallireducens – interaction with electron transferring flavoprotein and kinetic basis of unidirectional catalysis
The benzoate‐induced BamOP is identified, purified and characterized as the electron accepting ETF of GDH (BamM) from the Fe(III)‐respiring Geobacter metallireducens and provides a kinetic rational for the apparent inability of BamM to catalyze the reverse reductive crotonyl‐CoA carboxylation, even under thermodynamically favourable conditions.
Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae
The pathway of fermentative benzoate degradation by the syntrophically fermenting bacterium Syntrophus gentianae was studied by measurement of enzyme activities in cell-free extracts and can be balanced to yield one-third to two-thirds of an ATP unit per Benzoate degraded, in accordance with earlier measurements of whole-cell energetics.
Anaerobic degradation of aromatic amino acids by the hyperthermophilic archaeon Ferroglobus placidus.
The results suggested that the general strategies for anaerobic degradation of aromatic amino acids are highly conserved amongst bacteria and archaea living in both mesophilic and hyperthermophilic environments.
Biochemistry of glutaric aciduria type I: Activities of in vitro expressed wild-type and mutant cDNA encoding human glutaryl-CoA dehydrogenase
Glutaric aciduria type I (GA I; McKusick 231670) is caused by deficiency of glutaryl-CoA dehydrogenase activity (EC, a key enzyme in the catabolism of the amino acids lysine, hydroxylysine


Partial purification and characterization of glutaryl-coenzyme A dehydrogenase, electron transfer flavoprotein, and electron transfer flavoprotein-Q oxidoreductase from Paracoccus denitrificans.
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 to assay for the reduction of ubiquinone 1 by ETF-Q oxidoreductase.
Mammalian metabolism of glutaric acid.
Malate dehydrogenase in phototrophic purple bacteria: purification, molecular weight, and quaternary structure
The citric acid cycle enzyme malate dehydrogenase was purified to homogeneity from the nonsulfur purple bacteria Rhodobacter capsulatus, Rhodospirillum rubrum, Rhodomicrobium vannielii, and
Mechanism of action of glutaryl-CoA and butyryl-CoA dehydrogenases. Purification of glutaryl-CoA dehydrogenase.
It is proposed that these results support an oxidation mechanism for glutaryl-CoA dehydrogenase and butyryl- CoA dehydrogensase which is initiated by proton abstraction and involves intermediate allene formation.
Enzymatic reduction of benzoyl-CoA to alicyclic compounds, a key reaction in anaerobic aromatic metabolism.
The anaerobic metabolism of these compounds has been shown in this organism to proceed directly via benzoyl-CoA rather than via free benzoate, suggesting that the reduction reaction is more complex.
The biotin-dependent sodium ion pump glutaconyl-CoA decarboxylase from Fusobacterium nucleatum (subsp. nucleatum)
Membrane preparations of Fusobacterium nucleatum grown on glutamate contain glutaconyl-CoA decarboxylase at a high specific activity and was stimulated up to 3-fold by phospholipids, while the gram-positive bacteria Acidaminococcus fermentans and Clostridium symbiosum have a lower apparent Km for Na+ and were not stimulated by phosphorus.
An enzyme preparation obtained from Pseudomonas JEuoTescens was able to activate glutarate to glutaryl coenzyme A and to convert 1 mole of the latter to 1 Mole of carbon dioxide and 2 moles of acetyl coen enzyme A.
Uptake of benzoate by Rhodopseudomonas palustris grown anaerobically in light
The very effective uptake of external benzoate can be explained by its conversion to benzoyl CoA immediately after its passage across the cell membrane by simple or facilitated diffusion, which would serve to maintain a downhill concentration gradient between the cell cytoplasm and the cell surroundings, even at very low external Benzoate concentrations.
Anaerobic degradation of phenol by pure cultures of newly isolated denitrifying pseudomonads
Preliminary evidence is presented that the first reaction in anaerobic phenol oxidation is phenol carboxylation to 4-hydroxybenzoate.