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  • 1
    Electronic Resource
    Electronic Resource
    Glucose catabolism of the hyperthermophilic archaeum Thermoproteus tenax (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 111 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Pulse labelling experiments and enzyme studies show that Thermoproteus tenax is able to degrade glucose via the Embden-Meyerhof-Parnas (EMP) pathway. T. tenax is the first archeum for which the glycolytic EMP pathway could be established. One of the key enzymes, 6-phosphofructokinase of T. tenax depends on (pyrophosphate-fructose-6-phosphate-1-phosphotransferase) instead of ATP as found in some bacterial and eucaryal species. In addition to the intermediates of the EMP pathway the intermediary products of the non-phosphorylated Entner-Doudoroff pathway were also detected by pulse labelling experiments indicating that under chemoorganotrophic conditions at least 2 glycolytic pathways are operative in T. tenax.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06353.x
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  • 2
    Electronic Resource
    Electronic Resource
    The biosynthesis pathway of di-myo-inositol-1,1′-phosphate in Pyrococcus woesei (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 168 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: From in vitro experiments with dialyzed cell-free extracts of the hyperthermophilic Archaeum Pyrococcus woesei, the biosynthetic pathway of di-myo-inositol-1,1′-phosphate was deduced. Starting from glucose 6-phosphate, the synthesis proceeds in two steps with l-myo-inositol 1-phosphate as intermediate. (1) Interconversion of glucose 6-phosphate to inositol 1-phosphate was observed without adding cofactors, such as nucleoside triphosphates or pyridine dinucleotides suggesting that the first enzyme reaction corresponds to the NAD+-dependent inositol 1-phosphate synthase reaction as already described for eukaryal systems, but differing from the latter by a stronger pyridine dinucleotide binding rendering the enzyme virtually independent from external NAD+. (2) In a second step, two l-myo-inositol 1-phosphates are coupled under the expense of NTP to yield di-myo-inositol-1,1′-phosphate. The coupling of two l-myo-inositol 1-phosphates without preceding dephosphorylation of one of both by a phosphorylase as proposed for the di-myo-inositol-1,1′-phosphate synthesis in Methanococcus igneus (Chen, L. and Roberts, M. (1998) Appl. Environ. Microbiol. 64, 2609–2615) is supported by labeling experiments which resulted only in a labeled product with l-myo [U-14C]inositol 1-phosphate, but not with radiolabeled l-myo-[U-14C]inositol and non-labeled l-myo-inositol 1-phosphate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13252.x
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  • 3
    Electronic Resource
    Electronic Resource
    Thermoadaptation of methanogenic bacteria by intracellular ion concentration (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract An inter- and intra-species correlation was found between the intracellular potassium concentration and growth temperature within the Methanobacteriales, comprising mesophiles as well as moderate (Methanobacterium thermoautotrophicum) and extreme thermophiles (Methanothermus fervidus, Mt. sociabilis). Potassium concentrations in different species were determined at optimal growth temperatures and for the same species cultured at different temperatures. The main anionic component was found to be the unusual trianionic cyclic 2,3-diphosphiglycerate. In vitro experiments with the thermolabile enzymes glyceraldehyde-3-phosphate dehydrogenase and malate dehydrogenase from Mt. fervidus indicated that the potassium salt of the cyclic diphosphoglycerate acts as potent thermostabilizer. Thus it appears that, for the methanogens, changes in the intracellular ion concentration are the basis of thermoadaptation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02685.x
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction analysis of the NAD-dependent non-phosphorylating GAPDH of the hyperthermophilic archaeon Thermoproteus tenax (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 89-91 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Recombinant non-phosphorylating NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPN) of the hyperthermophilic crenarchaeote Thermoproteus tenax has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion technique. Crystals of different habits were obtained from several precipitant solutions (salts and polyethylene glycols). Preliminary X-ray analysis was performed with crystals grown in ammonium formate, which belonged to the primitive hexagonal space group P622, and had unit-cell parameters a = b = 184.8, c = 133.0 Å, γ = 120°. Assuming a molecular weight of 55 kDa, a Matthews parameter of 3.3 Å3 Da−1 is calculated assuming two molecules per asymmetric unit. The diffraction limit of these crystals is 2.5 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999014134
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  • 5
    Electronic Resource
    Electronic Resource
    Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 1419-1421 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Recombinant triosephosphate isomerase (TIM) from a hyperthermophilic Archaeon, Pyrococcus woesei, has been crystallized. Three crystal forms have been obtained: monoclinic, orthorhombic and hexagonal. The monoclinic crystals belong to space group P21 with cell dimensions a = 79.1, b = 89.2, c = 145.4 Å and β = 92.8°, and diffract to at least 2.6 Å. The orthorhombic crystals belong to space group P21212 with a = 89.4, b = 155.9, c = 79.5 Å, and diffract to 2.9 Å. Diffraction from the hexagonal form showed extensive disorder. The monoclinic form contains two tetramers in the asymmetric unit, which are in the same orientation but related by a pseudo-centring. The orthorhombic form contains one tetramer in the asymmetric unit which is in approximately the same orientation as in the monoclinic form. Knowledge of the structure of this hyperthermostable TIM, which is tetrameric in contrast to dimeric forms previously observed, will add to the understanding of protein thermostability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998004910
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  • 6
    Electronic Resource
    Electronic Resource
    Carbohydrate metabolism in Thermoproteus tenax: in vivo utilization of the non-phosphorylative Entner-Doudoroff pathway and characterization of its first enzyme, glucose dehydrogenase (1997)
    Springer
    Archives of microbiology 168 (1997), S. 120-127 
    Details
    ISSN: 1432-072X
    Keywords: Key words Archaeum ; Carbohydrate metabolism ; Embden-Meyerhof-Parnas pathway ; Modified ; (nonphosphorylative) Entner-Doudoroff pathway ; Glucose dehydrogenase ; Dual cosubstrate specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thermoproteus tenax is a hyperthermophilic, facultative heterotrophic archaeum. In this organism the utilization of the two catabolic pathways, a variant of the Embden-Meyerhof-Parnas (EMP) pathway and the modified (nonphosphorylative) Entner-Doudoroff (ED) pathway, was investigated and the first enzyme of the ED pathway, glucose dehydrogenase, was characterized. The distribution of the 13C label in alanine synthesized by cells grown with [1-13C]glucose indicated that in vivo the EMP pathway and the modified ED pathway operate parallel, with glucose metabolization via the EMP pathway being prominent. To initiate studies on the regulatory mechanisms governing carbon flux via these pathways, the first enzyme of the ED pathway, glucose dehydrogenase, was purified to homogeneity and its phenotypic properties were characterized. The pyridine-nucleotide-dependent enzyme used both NAD+ and NADP+ as cosubstrates, showing a 100-fold higher affinity for NADP+. Besides glucose, xylose was used as substrate, but with significantly lower affinity. These data suggest that the physiological function of the enzyme is the oxidation of glucose by NADP+. A striking feature was the influence of NADP+ and NAD+ on the quaternary structure and activity state of the enzyme. Without cosubstrate, the enzyme was highly aggregated (mol. mass 〉 600 kDa) but inactive, whereas in the presence of the cosubstrate the aggregates dissociated into enzymatically active, homomeric dimers with a mol. mass of 84 kDa (mol. mass of subunits: 41 kDa). The N-terminal amino acid sequence showed striking similarity to the respective partial sequences of alcohol dehydrogenases and sorbitol dehydrogenases, but no resemblance to the known pyridine-nucleotide-dependent archaeal and bacterial glucose dehydrogenases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050477
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  • 7
    Electronic Resource
    Electronic Resource
    Cloning, sequencing and expression of the gene encoding 2-phosphoglycerate kinase from Methanothermus fervidus (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 163-168 
    Details
    ISSN: 1617-4623
    Keywords: Cyclic 2,3-diphosphoglycerate ; 2-phosphoglycerate kinase ; Methanogen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene encoding 2-phosphoglycerate kinase (2PGK), which catalyses the first step in the biosynthesis of cyclic 2,3-diphosphoglycerate in methanogens, was cloned and sequenced from the hyperthermophilic Methanothermus fervidus. The 2pgk gene codes for 304 amino acids, corresponding to a relative molecular mass of 35040. The 2pgk mRNA was estimated to be 1600 nucleotides in size. Putative transcription signals and the ribosome-binding site of 2pgk are discussed. Production of 2PGK from M. fervidus in Es-cherichia coli reveals the same apparent molecular weights for the native enzyme and its denatured subunit as those shown by the 2PGK purified from M. fervidus. Also the kinetic parameters of 2PKG produced in E. coli correspond well with those from the enzyme isolated from the natural host M. fervidus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391009
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