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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 135 (1983), S. 237-240 
    ISSN: 1432-072X
    Keywords: 5-Aminolevulinic acid ; Shemin pathway ; C-5 pathway ; 4,5-Dioxovaleric acid ; 5-Aminolevulinic acid synthase ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum ; Tetrapyrrole biosynthesis ; Methanobrevibacter smithii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The pathway of 5-aminolevulinic acid (ALA) synthesis in growing cells of Methanobacterium thermoautotrophicum was studied. Advantage was taken of the fact that this anaerobic archaebacterium excretes ALA into the medium when growing in the presence of levulinic acid, which specifically inhibits the biosynthesis of tetrapyrroles at the level of ALA dehydratase. It was found that [1,4-14C]-succinate rather than [2-14C]glycine is incorporated into ALA. Evidence is provided that succinate incorporation into ALA probably proceeds via 2-oxoglutarate, which in M. thermoautotrophicum is synthesized from succinyl-CoA by reductive carboxylation. The data are consistent with the operation of the C-5 pathway for ALA synthesis and exclude the Shemin pathway in this methanogenic bacterium. The presence of l-alanine: 4,5-dioxovaleric acid aminotransferase activity and the apparent absence of ALA synthase in cell extracts support this conclusion.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 136 (1983), S. 106-110 
    ISSN: 1432-072X
    Keywords: Propionate assimilation ; Isoleucine biosynthesis ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum ; Methanobrevibacter arboriphilus ; Methanosarcina barkeri ; 2-Methylbutyrate assimilation ; Regulation of isoleucine biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanobacterium thermoautotrophicum, Methanobrevibacter arboriphilus, and Methanosarcina barkeri were found to assimilate propionate when growing on media supplemented with this volatile fatty acid. [1-14C]propionate was almost exclusively incorporated into isoleucine, only C-2 of which became labelled. Assimilation of propionate by M. thermoautotrophicum was specifically inhibited by isoleucine, by 2-methylbutyrate, and by 2-oxobutyrate, whereas there was little or no effect by leucine, valine, butyrate, and acetate. This finding indicates that propionate assimilation is under regulatory control by intermediates and/or the product of isoleucine biosynthesis.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 136 (1983), S. 111-113 
    ISSN: 1432-072X
    Keywords: Isoleucine biosynthesis ; Citramalate ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum ; Threonine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanobacterium thermoautotrophicum was grown on H2 and CO2 in a medium supplemented with [U-14C]threonine. Surprisingly, only threonine and not isoleucine in the cell protein became labelled indicating that the usual pathway of isoleucine biosynthesis via threonine is not operative in this anaerobic archaebacterium. Labelling studies with [1-14C]pyruvate, [2-14C]pyruvate and [1,4-14C]-succinate succinate revealed that isoleucine is probably synthesized from pyruvate and acetyl-CoA via citramalate as an intermediate.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Methanogenic bacteria ; Methanofuran ; Coenzyme M ; Tetrahydromethanopterin ; Coenzyme F420 ; Disulfide reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase were tested in cell extracts of 10 different methanogenic bacteria grown on H2/CO2 or on other methanogenic substrates. The four activities were found in all the organisms investigated: Methanobacterium thermoautotrophicum,M. wolfei, Methanobrevibacter arboriphilus, Methanosphaera stadtmanae, Methanosarcina barkeri (strains Fusaro and MS), Methanothrix soehngenii, Methanospirillum hungatei, Methanogenium organophilum, and Methanococcus voltae. Cell extracts of H2/CO2 grown M. barkeri and of methanol grown M. barkeri showed the same specific activities suggesting that the four enzymes are of equal importance in CO2 reduction to methane and in methanol disproportionation to CO2 and CH4. In contrast, cell extracts of acetate grown M. barkeri exhibited much lower activities of formylmethanofuran dehydrogenase and methylenetetrahydromethanopterin dehydrogenase suggesting that these two enzymes are not involved in methanogenesis from acetate. In M. stadtmanae, which grows on H2 and methanol, only heterodisulfide reductase was detected in activities sufficient to account for the in vivo methane formation rate. This finding is consistent with the view that the three other oxidoreductases are not required for methanol reduction to methane with H2.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 137 (1984), S. 362-365 
    ISSN: 1432-072X
    Keywords: Coenzyme F420 ; Flavin biosynthesis ; Deazaflavins ; Guanine assimilation ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Coenzyme F420 is a 8-hydroxy-5-deazaflavin present in methanogenic bacteria. We have investigated whether the pyrimidine ring of the deazaflavin originates from guanine as in flavin biosynthesis, in which the pyrimidine ring of guanine is conserved. For this purpose the incorporation of [2-14C]guanine and of [8-14C]guanine into F420 by growing cultures of Methanobacterium thermoautotrophicum was studied. Only in the case of [2-14C]guanine did F420 become labeled. The specific radioactivity of the deazaflavin and of guanine isolated from nucleic acids of [2-14C]guanine grown cells were identical. This finding suggests that the pyrimidine ring of the deazaflavin and of flavins are synthesized by the same pathway. F420 did not become labeled when M. thermoautotrophicum was grown in the presence of methyl-[14C] methionine, [U-14C]phenylalanine or [U-14C]tyrosine. This excludes that C-5 of the deazaflavin is derived from the methyl group of methionine and that the benzene ring comes from phenylalanine or tyrosine.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-072X
    Keywords: Factor F430 ; Coenzyme F430 ; Nickel porphinoid ; Tetrapyrroles ; Methyl-CoM reductase ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Factor F430 is a nickel porphinoid present in all methanogenic bacteria. It is a component of methyl-CoM reductase to which it is tightly but not covalently bound. Evidence is presented that in Methanobacterium thermoautotrophicum grown on nickel sufficient medium only approximately 30% of total F430 is associated with methyl-CoM reductase and that 70% is present in a non-bound, free form. When such cells were transferred to a nickel deficient medium the bacteria continued to grow although synthesis of total F430 stopped. During growth in the absence of nickel the amount of total F430 per 1 culture remained constant and that per g cells decreased. The ratio of free F430 to bound F430, however, changed. Free F430 was converted into the protein-bound form until almost all of the free F430 had disappeared. The kinetics of labelling with 63Ni of free and bound F430 agreed rather well with that calculated for a precursor-product relationship between free and bound F430.
    Type of Medium: Electronic Resource
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