Disease relevance of Acidaminococcus

• The properties of the pOSEX expression vectors were tested by positioning a promoterless lacZ (encoding beta-galactosidase) gene from E. coli and the gcdA (encoding carboxytransferase) gene from the Gram+ bacterium Acidaminococcus fermentans under the control of the proU regulatory region [1].
• The equilibrium constants of the reactions catalysed by (S)-citramalate lyase and (R)-2-hydroxyglutarate dehydrogenase were determined using the purified enzymes from Clostridium tetanomorphum and Acidaminococcus fermentans, respectively [2].
• The determination of enzymatic activities in cell-free extracts of Acidaminococcus fermentans and Peptostreptococcus asaccharolyticus led to a refined scheme for the pathway of glutamate fermentation via (R)-2-hydroxyglutarate to acetate and butyrate [3].
• (R)-2-Hydroxyglutaryl-CoA dehydratase (HgdAB) from Acidaminococcus fermentans catalyses the reversible dehydration of its substrate to glutaconyl-CoA [4].

High impact information on Acidaminococcus

• Here we present the crystal structure of the decarboxylase subunit (Gcdalpha) from Acidaminococcus fermentans and its complex with glutaconyl-CoA [5].
• Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis [6].
• The exchange of oxygen atoms between acetate, glutaryl-CoA, and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans was analyzed using [(18)O(2)]acetate together with matrix-assisted laser desorption/ionization time of flight mass spectrometry of an appropriate undecapeptide [6].
• The sodium ion translocating glutaconyl-CoA decarboxylase from Acidaminococcus fermentans: cloning and function of the genes forming a second operon [7].
• Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A [8].

Chemical compound and disease context of Acidaminococcus

• This fact was used to determine the stereospecificity at C4 of NAD(P) for the NADP-dependent alcohol dehydrogenase from Methanogenium organophilum and for the NAD-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans [9].
• Emendation of the description of Acidaminococcus fermentans, a trans-aconitate- and citrate-oxidizing bacterium [10].
• A biotin-dependent sodium pump: glutaconyl-CoA decarboxylase from Acidaminococcus fermentans [11].
• In the course of glutamate fermentation by Acidaminococcus fermentans glutaconate coenzyme A-transferase catalyzes the transfer of CoAS- from acetyl-CoA to (R)-2-hydroxyglutarate, forming (R)-2-hydroxyglutaryl-CoA [12].
• Ability of Acidaminococcus fermentans to oxidize trans-aconitate and decrease the accumulation of tricarballylate, a toxic end product of ruminal fermentation [13].

Biological context of Acidaminococcus

• Glutaconyl-CoA decarboxylase from Acidaminococcus fermentans (clostridal cluster IX), a strict anaerobic inhabitant of animal intestines, uses the free energy of decarboxylation (delta G(o) approximately -30 kJ mol-1) in order to translocate Na+ from the inside through the cytoplasmic membrane [7].
• Ruminal fluid which was enriched with trans-aconitate yielded a gram-negative diplococcus (strain AO) which was identified by 16S ribosomal DNA sequence analysis as Acidaminococcus fermentans [10].

Anatomical context of Acidaminococcus

• Glutaconyl-CoA decarboxylase from Acidaminococcus fermentans is a biotin enzyme, which is integrated into membranes [14].

Gene context of Acidaminococcus

• ACI-1 from Acidaminococcus fermentans: characterization of the first beta-lactamase in Anaerobic cocci [15].
• We describe here the crystal structure of glutaconate CoA-transferase (GCT) from the strictly anaerobic bacterium Acidaminococcus fermentans [16].

References