Notes: Clostridium cylindrosporum (ex Barker and Beck 1942) nom. rev.

Andreesen, Jan R.; Zindel, U.; Dürre, P.

doi:10.1099/00207713-35-2-206

Cited by 27 publications

(13 citation statements)

References 6 publications

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“…A similarly confusing effect of W and Mo metabolism has been observed in the purinolytic clostridia, which grow by the fermentation of purines as their sole carbon and energy sources [166,[169][170][171][172]. For example, it was initially reported that C. cylindrosporum and C. acidiurici could be differentiated by their W and Mo requirements [165].…”

Section: Clostridiummentioning

confidence: 88%

Tungsten in biological systems

Kletzin

Adams

1996

FEMS Microbiology Reviews

134

144

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Tungsten (atomic number 74) and the chemically analogous and very similar metal molybdenum (atomic number 42) are minor yet equally abundant elements on this planet. The essential role of molybdenum in biology has been known for decades and molybdoenzymes are ubiquitous. Yet, it is only recently that a biological role for tungsten has been established in prokaryotes, although not as yet in eukaryotes. The best characterized organisms with regard to their metabolism of tungsten are certain species of hyperthermophilic archaea (Pyrococcus furiosus and Thermococcus litoralis), methanogens (Methanobacterium thermoautotrophicum and Mb. wolfei), Gram-positive bacteria (Clostridium thermoaceticum, C. formicoaceticum and Eubacterium acidaminophilum), Gram-negative anaerobes (Desulfovibrio gigas and Pelobacter acetylenicus) and Gram-negative aerobes (Methylobacterium sp. RXM). Of these, only the hyperthermophilic archaea appear to be obligately tungsten-dependent. Four different types of tungstoenzyme have been purified: formate dehydrogenase, formyl methanofuran dehydrogenase, acetylene hydratase, and a class of phylogenetically related oxidoreductases that catalyze the reversible oxidation of aldehydes. These are carboxylic reductase, and three ferredoxin-dependent oxidoreductases which oxidize various aldehydes, formaldehyde and glyceraldehyde 3-phosphate. All tungstoenzymes catalyze redox reactions of very low potential (< -420 mV) except one (acetylene hydratase) which catalyzes a hydration reaction. The tungsten in these enzymes is bound by a pterin moiety similar to that found in molybdoenzymes. The first crystal structure of a tungsten-or pterin-containing enzyme, that of aldehyde ferredoxin oxidoreductase from P. furiosus, has revealed a catalytic site with one W atom coordinated to two pterin molecules which are themselves bridged by a magnesium ion. The geochemical, ecological, biochemical and phylogenetic basis for W-vs. Mo-dependent organisms is discussed.

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Section: Clostridiummentioning

confidence: 88%

Tungsten in biological systems

Kletzin

Adams

1996

FEMS Microbiology Reviews

134

144

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“…C. cylindrosporum is an obligately purine-utilizing anaerobe (2, 13). Purine is degraded to glycine, which is also metabolized via the glycine decarboxylase-glycine reductase system if selenium is present (2,13 (44). The authors concluded that a transhydrogenase reaction couples the NADH-specific and NADPH-specific processes.…”

Section: Discussionmentioning

confidence: 99%

Purification and comparative studies of dihydrolipoamide dehydrogenases from the anaerobic, glycine-utilizing bacteria Peptostreptococcus glycinophilus, Clostridium cylindrosporum, and Clostridium sporogenes

Dietrichs

Andreesen

1990

J Bacteriol

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Three different dihydrolipoamide dehydrogenases were purified to homogenity from the anaerobic glycine-utilizing bacteria Clostridium cylindrosporum, Clostridium sporogenes, and Peptostreptococcus glycinophilus, and their basic properties were determined. The enzyme isolated from P. glycinophilus showed the properties typical of dihydrolipoamide dehydrogenases: it was a dimer with a subunit molecular mass of 53,000 and contained 1 mol of flavin adenine dinucleotide and 2 redox-active sulfhydryl groups per subunit. Only NADH was active as a coenzyme for reduction of lipoamide. Spectra of the oxidized enzyme exhibited maxima at 230, 270, 353, and 453 nm, with shoulders at 370, 425, and 485 nm. The dihydrolipoamide dehydrogenases of C. cylindrosporum and C. sporogenes were very similar in their structural properties to the enzyme of P. glycinophilus except for their coenzyme specificity. The enzyme of C. cylindrosporum used NAD(H) as well as NADP(H), whereas the enzyme of C. sporogenes reacted only with NADP(H), and no reaction could be detected with NAD(H). Antibodies raised against the dihydrolipoamide dehydrogenase of C. cylindrosporum reacted with extracts of Clostridium acidiurici, Clostridium purinolyticum, and Eubacterium angustum, whereas antibodies raised against the enzymes of P. glycinophilus and C. sporogenes showed no cross-reaction with extracts from 42 organisms tested.

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“…There has been so me doubt as to whether these are strains of the same species or of different species (Cato et al, 1986). Phenotypically they are very similar; however, 16S rRNA cataloging (Tanner et al, 1982) and DNA-DNA hybridization data (Schiefer-Ullrich et al, 1984;Andreesen et al , 1985) demonstrate clearly that C. acidiurici, C. cylindrosporum, and C. purinolyticum are different species.…”

Section: The Purinolytic Acetogenic Clostridiamentioning

confidence: 91%

“…Table I. iurici, C. cylindrosporum (Barker and Beck, 1942;Andreesen et al, 1985), and C. purinolyticum (Dürre et al, 1981). They are all mesophilic.…”

Section: Thermoaceticum (Thermaceticum) and C Thermoautotrophicumentioning

confidence: 98%