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At least 847 records · Page 47Linked to original sources
PubMed1994

Metabolism of homocetogens.

Homoacetogenic bacteria are strictly anaerobic microorganisms that catalyze the formation of acetate from C1 units in their energy metabolism. Most of these organisms are able to grow at the expense of hydrogen plus CO2 as the sole energy source. Hydrogen then serves as the electron donor for CO2 reduction to acetate. The methyl group of acetate is formed from CO2 via formate and reduced C1 intermediates bound to tetrahydrofolate. The carboxyl group is derived from carbon monoxide, which is synthesized from CO2 by carbon monoxide dehydrogenase. The latter enzyme also catalyzes the formation of acetyl-CoA from the methyl group plus CO. Acetyl-CoA is then converted either to acetate in the catabolism or to cell carbon in the anabolism of the bacteria. The homoacetogens are very versatile anaerobes, which convert a variety of different substrates to acetate as the major end product.

Acetates↗
PubMedDate not supplied

[Endotoxins: a neglected environmental factor].

The effects of bacterial endotoxins are well known form an experimental and clinical point of view. Their presence in the environment in general and their possible role for the development of clinical symptoms at low exposure levels has been less studied. Experimental and epidemiological evidence for such effects are reviewed with reference to particular environments where this exposure might be present.

Acetobacter↗
PubMed1990

Biooxidation of a synthetic waste by a microbial film grown on the liquid surface in a shallow flow reactor.

A new process of biological waste treatment was developed by use of microbial films grown on the liquid surface in a shallow flow reactor. The performance of this process was tested using a synthetic waste that contained acetic acid as a model organic pollutant. About 90% of acetic acid (10,000 mg/L-1) in the synthetic waste was removed by setting alpha tau: (alpha specific liquid surface area, cm-1, and tau: hydraulic liquid detention time, h) higher than 15 cm-1/h. It was necessary to maintain alpha large enough (more than 10 cm-1 in most cases) to satisfy oxygen demand for the biooxidation. The oxygen balance and TOC determinations showed that the acetic acid removed was completely oxidized with oxygen transferred through the liquid surface. This process would contribute to energy savings, since it requires no forced aeration for oxygen supply.

Acetates↗
PubMed2001

Isolation and characterization of a veratrol:corrinoid protein methyl transferase from Acetobacterium dehalogenans.

From 3-methoxyphenol-grown cells of Acetobacterium dehalogenans, an inducible enzyme was purified that mediated the transfer of the methyl groups of veratrol (1,2-dimethoxybenzene) to a corrinoid protein enriched from the same cells. In this reaction, veratrol was converted via 2-methoxyphenol to 1,2-dihydroxybenzene. The veratrol:corrinoid protein methyl transferase, designated MTIver, had an apparent molecular mass of about 32 kDa. With respect to the N-terminal amino acid sequence and other characteristics, MTIver is different from the vanillate:corrinoid protein methyl transferase (MTIvan) isolated earlier from the same bacterium. For the methyl transfer from veratrol to tetrahydrofolate, two additional protein fractions were required, one of which contained a corrinoid protein. This protein was not identical with the corrinoid protein of the vanillate O-demethylase system. However, the latter corrinoid protein could also serve as methyl acceptor for the veratrol:corrinoid protein methyl transferase. MTIver catalyzed the demethylation of veratrol, 3,4-dimethoxybenzoate, 2-methoxyphenol, and 3-methoxyphenol. Vanillate (3-methoxy-4-hydroxybenzoate), 2-methoxybenzoate, or 4-methoxybenzoate could not serve as substrates.

Acetobacter↗
PubMed2004

D-hexosaminate production by oxidative fermentation.

Microbial production of D-hexosaminate was examined by means of oxidative fermentation with acetic acid bacteria. In most strains of acetic acid bacteria, membrane-bound D-glucosamine dehydrogenase (synonymous with an alternative D-glucose dehydrogenase distinct from quinoprotein D-glucose dehydrogenase) oxidized D-hexosamines to the corresponding D-hexosaminates in a stoichiometric manner. Conversion of D-hexosamines to the corresponding D-hexosaminates was observed with growing cells of acetic acid bacteria, and D-hexosaminate was stably accumulated in the culture medium even though D-hexosamine was exhausted. Since the enzyme responsible is located on the outer surface of the cytoplasmic membrane, and the enzyme activity is linked to the respiratory chain of the organisms, resting cells, dried cells, and immobilized cells of acetic acid bacteria were effective catalysts for D-hexosaminate production. D-Mannosaminate and D-galactosaminate were also prepared for the first time by means of oxidative fermentation, and three different D-hexosaminates were isolated from unreacted substrate by a chromatographic separation. In this paper, D-hexosaminate production by oxidative fermentation carried out mainly with Gluconobacter frateurii IFO 3264 is exemplified as a typical example.

Acetobacter↗
PubMed1995

The Na(+)-translocating ATPase of Acetobacterium woodii is a F1F0-type enzyme as deduced from the primary structure of its beta, gamma and epsilon subunits.

A 4.5 kbp EcoRI fragment hybridizing to a fragment of uncD (coding for subunit beta of F1F0-ATPases) was cloned from chromosomal DNA of Acetobacterium woodii. The nucleotide sequence was determined and revealed five open reading frames (ORF), four of which were identified to code for subunits of the Na(+)-ATPase. The deduced amino acid sequences of these ORF's are homologous to subunit alpha (partial coding sequence, C-terminal end), gamma, beta and epsilon of F1F0-ATPases from various organisms; furthermore, the organization of the genes in the order uncA (alpha), uncG (gamma), uncD (beta), uncC (epsilon) is identical to the structure of unc operon as present in most bacteria. Downstream of uncC is an ORF whose deduced amino acid sequence has 53% sequence homology to AlgD from Pseudomonas aeruginosa. The structure and organization of the unc genes are the final proof that the Na(+)-ATPase from A. woodii is a member of the family of F1F0-ATPases.

Acetobacter↗
PubMed1983

GTP-insensitive ornithine decarboxylase in acetobacteria able to synthesize spermine.

Several Acetobacteria contained large amounts of spermine in addition to the putrescine and spermidine, which are the polyamines normally found in prokaryotes. A spermine synthase present in cell extracts of these Acetobacteria is the first example of this enzyme in prokaryotes. Dicyclohexylammonium sulphate inhibited both spermidine synthase and spermine synthase activities in Acetobacteria. Their ornithine decarboxylase was not stimulated by GTP nor inhibited by ppGpp and pppGpp (magic spots I and II) in contrast to ornithine decarboxylase of nearly all bacteria studied so far. However, their S-adenosyl-L-methionine decarboxylase resembled other prokaryotic adenosylmethionine decarboxylases in requiring Mg2+ ions in vitro for full activity.

Acetobacter↗