| competition for l-glutamate between specialised and versatile clostridium species. | clostridium cochlearium could be reproducibly enriched in an l-aspartate- and l-glutamate-limited, anaerobic chemostat inoculated with anaerobic sludge. l-glutamate, l-glutamine and l-histidine were the only fermentable substrates. less specialised clostridia of the c. tetanomorphum type could only be isolated from batch enrichments with l-glutamate and l-aspartate as energy sources. competition experiments with c. cochlearium and c. tetanomorphum in a l-glutamate-limited chemostat resulted in t ... | 1979 | 426599 |
| utilization of hydrogen and formate by campylobacter spec. under aerobic and anaerobic conditions. | a free-living aspartate-fermenting campylobacter spec. was shown to utilize hydrogen produced in mixed culture by clostridium cochlearium from glutamate. resting cells of campylobacter were shown to reduce aspartate, fumarate and malate as well as nitrate, nitrite, hydroxylamine, sulphite, thiosulphate and elemental sulphur with molecular hydrogen. growth of campylobacter spec. was demonstrated with formate as electron donor and nitrate, thiosulphate, elemental sulphur or oxygen as electron acce ... | 1978 | 718373 |
| glutamate mutase from clostridium cochlearium. purification, cobamide content and stereospecific inhibitors. | both components, e and s, of the adenosylcobalamin-(coenzyme b12)-dependent glutamate mutase from clostridium cochlearium were purified. component s (16 kda) must be added to component e to obtain activity, although the latter contains substoichiometric amounts of component s besides the major 50-kda subunit. the enzyme proved to be very similar to that of c. tetanomorphum as described by barker et al. [barker, h. a., rooze, v., suzuki, f. & iodice, a. a. (1964) j. biol. chem. 239, 3260-3266] bu ... | 1992 | 1315276 |
| identification of a paramagnetic species as an early intermediate in the coenzyme b12-dependent glutamate mutase reaction. a cob(ii)amide? | highly active and cobamide-free glutamate mutase was obtained from clostridium cochlearium by a modification of the original purification procedure. after incubation of the enzyme with dithiothreitol, adenosylcobalamin (coenzyme b12) and the substrate (s)-glutamate, a paramagnetic species was observed by epr-spectroscopy. the signal was maximal within 15 ms after mixing with glutamate. different signals were detected after incubating the system with the competitive inhibitors (2s,4s)-4-fluoroglu ... | 1992 | 1322827 |
| spore fine structure in clostridium cochlearium. | the fine structure of clostridium cochlearium was examined by use of thin sections, negative stains, and carbon replicas. particular attention was given to details of the sporulation process and to fine structure of the spores. spore coat formation was well advanced before the first evidence of cortex formation was noted. three distinct spore coats were detected, the outermost of which was composed of seven layers. in addition, the spores possessed tubular appendages of variable length attached ... | 1969 | 5354956 |
| crystalline inclusions of clostridium cochlearium. | | 1968 | 5726313 |
| crystalline inclusions in bacillus thuringiensis. | crystalline inclusion bodies resembling those seen in clostridium cochlearium were detected in cultures of bacillus thuringiensis infected with bacteriophage. | 1969 | 5784229 |
| involvement of mercury methylation in microbial mercury detoxication. | a vitamin b12 requiring strain was isolated from clostridium cochlearium t-2c which is known to synthesize various types of vitamin b12 including methylcobalamin and has an ability to methylate inorganic mercury. the vitamin b12 auxotroph lacking the mercury-methylating activity showed higher sensitivity to inorganic mercury than its original strain, while the sensitivity of both strains to methylmercury was relative low and essentially the same. these data seem to present affirmative evidence t ... | 1982 | 6462125 |
| characterization of organomercury-decomposing activity in cell extract of mercury-resistant clostridium cochlearium t-2p. | | 1982 | 7067654 |
| physiological role of mercury-methylation in clostridium cochlearium t-2c. | | 1982 | 7126920 |
| role of hydrogen sulfide in mercury resistance determined by plasmid of clostridium cochlearium t-2. | mercury resistance of clostridium cochlearium t-2p was found to be controlled by a different mechanism from those reported so far since no mercury-reducing activity was detected in this strain. the h2s generating ability as well as the demethylating activity in this bacterium was eliminated by the treatment of the cured acridine dye and recovered by the conjugation of the cured strain with the parent strain. in addition, the strain which lost their abilities to generate h2s and to decompose meth ... | 1981 | 7224780 |
| plasmid-controlled mercury biotransformation by clostridium cochlearium t-2. | a strain of clostridium cochlearium having methylmercury-decomposing ability was isolated. the ability was cured by the treatment with acridine dye and recovered by the conjugation of the cured strain with the parent strain. the cured strain then showed the activity to methylate mercuric ion as previously reported (m. yamada and k. tonomura, j. ferment. technol. 50:159-166, 1971). these results and the agarose gel electrophoretic pattern of the deoxyribonucleic acids from the lysates indicate a ... | 1980 | 7458307 |
| coordination of a histidine residue of the protein-component s to the cobalt atom in coenzyme b12-dependent glutamate mutase from clostridium cochlearium. | electron paramagnetic resonance (epr) spectroscopy of glutamate mutase from clostridium cochlearium was performed in order to test the idea, that a histidine residue of component s replaces the dimethylbenzimidazole ligand of the co-atom during binding of coenzyme b12 to the enzyme. the shapes and the superhyperfine splitting of the gz-lines of the co(ii) epr spectra were used as indicators of the interaction of the axial base nitrogen with the co-atom. a mixture of completely 15n-labelled compo ... | 1995 | 7649266 |
| characterization of the coenzyme-b12-dependent glutamate mutase from clostridium cochlearium produced in escherichia coli. | the glutamate mutase dependent on adenosylcobalamin (coenzyme b12) catalyzes the carbon skeleton rearrangement of (s)-glutamate to (2s,3s)-3-methylaspartate, the first step of the glutamate fermentation pathway of the anaerobic bacterium clostridium cochlearium. the enzyme consists of two protein components, e, a dimer epsilon 2 (epsilon, 53.5 kda) and s, a monomer (sigma, 14.8 kda). the corresponding genes (glme and glms) were cloned, sequenced and over-expressed in escherichia coli. the genes ... | 1994 | 7880251 |
| cloning, sequencing and expression in escherichia coli of the gene encoding component s of the coenzyme b12-dependent glutamate mutase from clostridium cochlearium. | adenosylcobalamin (coenzyme b12) dependent glutamate mutase catalyzes the carbon skeleton rearrangement of (s)-glutamate to (2s,3s)-methylaspartate. this is the first step of the fermentation of glutamate by the strict anaerobic bacterium clostridium cochlearium. the enzyme consists of the two protein components e and s. the gene encoding component s (glms) was cloned in escherichia coli and its nucleotide sequence was determined. the nucleotide sequence and the deduced amino acid sequence showe ... | 1994 | 8013871 |
| clostridium pascui sp. nov., a new glutamate-fermenting sporeformer from a pasture in pakistan. | four strains of an obligately anaerobic spore-forming bacterium were isolated from soil samples from a donkey pasture in pakistan. comparative 16s rrna sequence analysis demonstrated that the strains are members of phylogenetic cluster i of the genus clostridium (collins et al. 1994). the strains are mesophilic, nonsaccharolytic, and nonproteolytic, utilize glutamate and histidine, and produce indole. acetate, butyrate, ethanol, hydrogen, and carbon dioxide are the products of fermentation. alth ... | 1997 | 8995820 |
| identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme b12-dependent glutamate mutase from clostridium cochlearium. | a series of 2h- and 13c-labeled glutamates were used as substrates for coenzyme b12-dependent glutamate mutase, which equilibrates (s)-glutamate with (2s,3s)-3-methylaspartate. these compounds contained the isotopes at c-2, c-3, or c-4 of the carbon chain: [2-2h], [3,3-2h2], [4,4-2h2], [2,3,3,4,4-2h5], [2-13c], [3-13c], and [4-13c]glutamate. each reaction was monitored by electron paramagnetic resonance (epr) spectroscopy and revealed a similar signal characterized by g'xy = 2.1, g'z = 1.985, an ... | 1998 | 9521732 |
| crystallization and preliminary x-ray analysis of recombinant glutamate mutase and of the isolated component s from clostridium cochlearium. | glutamate mutase [varepsilon2sigma2(b12)1] was reconstituted by incubating purified components e (varepsilon2) and s (sigma2) from clostridium cochlearium, both produced in escherichia coli, with either aquo- or cyanocobalamin. the inactive glutamate mutase obtained was crystallized with polyethyleneglycol 4000 as precipitant. crystals are monoclinic with space group p21 and have cell dimensions a = 64.6, b = 113.2, c = 108.4 a and beta = 96.0 degrees for the glutamate mutase reconstituted with ... | 1998 | 9757132 |
| cloning, nucleotide sequencing, and expression of the 3-methylaspartate ammonia-lyase gene from citrobacter amalonaticus strain yg-1002. | the gene coding for 3-methylaspartate ammonia-lyase (3-methylaspartase, mal, ec 4.3.1.2) from citrobacter amalonaticus strain yg-1002 (tpu 6323) was cloned onto plasmid pbluescript ii ks(+), and the nucleotide sequence of the 1239-bp open reading frame (orf), consisting of 413 codons, was identified as the mal gene coding for mal. the predicted polypeptide has 62.5% identity with mal from the obligate anaerobe, clostridium tetanomorphum ncimb 11547. orf1, which showed 58.6% and 58.8% identities ... | 1998 | 9830098 |
| structure and dynamics of the b12-binding subunit of glutamate mutase from clostridium cochlearium. | glutamate mutase (glm) is an adenosylcobamide-dependent enzyme that catalyzes the reversible rearrangement of (2s)-glutamate to (2s, 3s)-3-methylaspartate. the active enzyme from clostridium cochlearium consists of two subunits (of 53.6 and 14.8 kda) as an alpha2beta2 tetramer, whose assembly is mediated by coenzyme b12. the smaller of the protein components, glms, has been suggested to be the b12-binding subunit. here we report the solution structure of glms, determined from a heteronuclear nmr ... | 1999 | 10429202 |
| glutamate mutase from clostridium cochlearium: the structure of a coenzyme b12-dependent enzyme provides new mechanistic insights. | glutamate mutase (glm) equilibrates (s)-glutamate with (2s,3s)-3-methylaspartate. catalysis proceeds with the homolytic cleavage of the organometallic bond of the cofactor to yield a 5'-desoxyadenosyl radical. this radical then abstracts a hydrogen atom from the protein-bound substrate to initiate the rearrangement reaction. glm from clostridium cochlearium is a heterotetrameric molecule consisting of two sigma and two epsilon polypeptide chains. | 1999 | 10467146 |
| native corrinoids from clostridium cochlearium are adeninylcobamides: spectroscopic analysis and identification of pseudovitamin b(12) and factor a. | the corrinoids from the obligate anaerobe clostridium cochlearium were extracted as a mixture of co(beta)-cyano derivatives. from 50 g of frozen cells, approximately 2 mg (1.5 micromol) of b(12) derivatives was obtained as a crystalline sample. analysis of the corrinoid sample of c. cochlearium by a combination of high-pressure liquid chromatography and uv-vis absorbance spectroscopy revealed the presence of three cyano corrinoids in a ratio of about 3:1:1. the spectroscopic data acquired for th ... | 2000 | 10940017 |
| a protein pre-organized to trap the nucleotide moiety of coenzyme b(12): refined solution structure of the b(12)-binding subunit of glutamate mutase from clostridium tetanomorphum. | uniformly (13)c,(15)n-labeled muts, the coenzyme b(12)-binding subunit of glutamate mutase from clostridium tetanomorphum, was prepared by overexpression from an escherichia coli strain. multidimensional heteronuclear nmr spectroscopic experiments with aqueous solutions of (13)c,(15)n-labeled muts provided signal assignments for roughly 90% of the 1025 hydrogen, 651 carbon, and 173 nitrogen atoms and resulted in about 1800 experimental restraints. based on the information from the nmr experiment ... | 2001 | 11828501 |
| structure and function of sanv: a gene involved in nikkomycin biosynthesis of streptomyces ansochromogenes. | a 6.3-kb bamhi- bglii dna fragment was cloned from cos20 by using chromosome walking strategy. it was partially sequenced with the result that there is a possible orf of 1272 nucleotides. the orf designated sanv was deposited in genbank under accession no. af469955. database search indicated that the deduced protein of sanv shows 28% identity and 44% similarity over 405 amino acid residues to the large component (e) of glutamate mutases from clostridium cochlearium. gene disruption was performed ... | 2003 | 12732945 |
| searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (r)-3-methylitaconate catalyzed by coenzyme b12-dependent 2-methyleneglutarate mutase from eubacterium barkeri. | coenzyme b(12)-dependent 2-methyleneglutarate mutase from the strict anaerobe eubacterium barkeri catalyzes the equilibration of 2-methyleneglutarate with (r)-3-methylitaconate. proteins with mutations in the highly conserved coenzyme binding-motif dxh(x)(2)g(x)(41)gg (d483n and h485q) exhibited decreased substrate turnover by 2000-fold and >4000-fold, respectively. these findings are consistent with the notion of h485 hydrogen-bonded to d483 being the lower axial ligand of adenosylcobalamin in ... | 2005 | 16060663 |
| a taxonomic study of "clostridium putrificum" and its establishment as a definite entity-clostridium lentoputrescens, nov. spec. | | 1934 | 16559715 |
| degradation of 2-nitrodiphenylamine, a component of otto fuel ii, by clostridium spp. | otto fuel ii, a propellant in torpedoes, is composed of 76% 1,2 propanediol dinitrate (pgdn), 22.5% di-n-butyl sebacate, and 1.5% 2-nitrodiphenylamine (ndpa), and is largely recalcitrant to aerobic microbial degradation. anaerobic microbial degradation of otto fuel ii was tested by inoculating anaerobic enrichment media, containing either 2% (vol:vol) complete otto fuel ii or 2% of a 0.02% solution of otto fuel ii in methanol, with soil and water from sites contaminated with munitions or with la ... | 1998 | 16887628 |
| characterization of clostridium spp. isolated from spoiled processed cheese products. | of 42 spoiled cheese spread products, 35 were found to harbor clostridium spp. typical signs of spoilage were gas production and off-odor. the identity was determined for about half of the isolates (n = 124) by analytab products (api), biolog, the riboprinter system, 16s rdna sequencing, cellular fatty acid analysis, or some combination of these. the majority of isolates were identified as clostridium sporogenes (in 33% of products), but clostridium cochlearium (in 12% of products) and clostridi ... | 2006 | 16924914 |
| influence of long-chain polyphosphate and heat treatment on clostridium cochlearium and clostridium sporogenes isolated from processed cheese spread. | the outgrowth of clostridium spp. spores causes spoilage in processed cheese products due to gas and off-odor formation. the present study focuses on the response of spores of clostridium sporogenes and clostridium cochlearium at 25 degrees c to polyphosphate, both alone and in combination with heat treatment. the two strains used were isolated from spoiled cheese spread. the addition of 1.5% polyphosphate but not 0.75% polyphosphate totally inhibited the growth of c. sporogenes sik4.3; in contr ... | 2007 | 17388069 |
| the reaction mechanism of the enzyme glutamate mutase studied by qm/mm simulations. | the radical mechanism of the conversion of glutamate to methylaspartate catalyzed by glutamate mutase is studied with qm/mm simulations based on density functional theory (dft/mm). the hydrogen transfer between the substrate and the cofactor is found to be rate limiting with a barrier of 101.1 kj mol<sup>-1</sup>. a careful comparison to the uncatalyzed reaction in water is performed. the protein influences the reaction predominantly electrostatically and to a lesser degree sterically. our calcu ... | 2011 | 21612278 |
| reactivation of latent hiv-1 by a wide variety of butyric acid-producing bacteria. | latently infected cells harbor human immunodeficiency virus type 1 (hiv-1) proviral dna copies integrated in heterochromatin, allowing persistence of transcriptionally silent proviruses. it is widely accepted that hypoacetylation of histone proteins by histone deacetylases (hdacs) is involved in maintaining the hiv-1 latency by repressing viral transcription. hiv-1 replication can be induced from latently infected cells by environmental factors, such as inflammation and co-infection with other m ... | 2012 | 22322557 |
| characterization of microbial community in the leachate associated with the decomposition of entombed pigs. | foot and mouth disease (fmd) is one of the acute infectious diseases in hoofed and even-toed mammals, including pigs, and it occurs via acute infection by aphthovirus. when fmd is suspected, animals around the location of origin are typically slaughtered and buried. other methods such as rendering, composting, and incineration have not been verified in practice in korea. after the fmd incident, the regular monitoring of the microbial community is required, as microorganisms greatly modify the ch ... | 2012 | 23075782 |
| isolation of acetic, propionic and butyric acid-forming bacteria from biogas plants. | in this study, acetic, propionic and butyric acid-forming bacteria were isolated from thermophilic and mesophilic biogas plants (bgp) located in germany. the fermenters were fed with maize silage and cattle or swine manure. furthermore, pressurized laboratory fermenters digesting maize silage were sampled. enrichment cultures for the isolation of acid-forming bacteria were grown in minimal medium supplemented with one of the following carbon sources: na(+)-dl-lactate, succinate, ethanol, glycero ... | 2016 | 26779817 |