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Methanococcus

Jones JB, TC Stadtman (1981) Selenium-dependent and selenium-independent formate dehydrogenase of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form. J Biol Chem 256 656-663. [Pg.273]

Graham DE, H Xu, RH White (2002) Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem 211 23500-23507. [Pg.327]

Lu ZJ, GD Markham (2004) Catalytic properties of the archaeal 5-adenosylmethionine decarboxylase from Methanococcus jannaschii. J Biol Chem 279 265-273. [Pg.330]

DeMoll E, T Auffenberg (1993) Purine metabolism in Methanococcus vannielii J Bacterial 175 5754-5761. [Pg.548]

Niess UM, A Klein (2004) Dimethylselenide demethylation is an adaptaive response to selenium deprivation in the urchaeon Methanococcus voltae. J Bacterial 186 3640-3648. [Pg.594]

Lowe J. Crystal structure determination of FtsZ from Methanococcus jannaschii. J Struct Biol 1998 124 235-243. [Pg.275]

Jones, J.B. and T.C. Stadtman. 1977. Methanococcus vanniellii culture and effects of selenium and tungsten on growth. Jour. Bacteriol. 130 1404-1406. [Pg.1628]

Figure 10.9 Active site of Methanococcus phosphoserine phosphatase with Mg2+ and phosphoserine in the active site (a) and of human phosphoserine phosphatase with Ca2+ bound and the modelled substrate in the active site (b). (From Peeraer et al., 2004. Reproduced with permission of Blackwell Publishing Ltd.)... Figure 10.9 Active site of Methanococcus phosphoserine phosphatase with Mg2+ and phosphoserine in the active site (a) and of human phosphoserine phosphatase with Ca2+ bound and the modelled substrate in the active site (b). (From Peeraer et al., 2004. Reproduced with permission of Blackwell Publishing Ltd.)...
Fig. 6. Multiple alignment of a putative zinc finger in pushover/calossin and two archaeal proteins. Conserved cysteines predicted to bind Zn2+ are shown as white-on-black. Annotation of this alignment is as Fig. 4. Species abbreviations as Figs. 4 and 5, except ARCFU, Archaeoglobus fulgidus METJA, Methanococcus jannaschii. Fig. 6. Multiple alignment of a putative zinc finger in pushover/calossin and two archaeal proteins. Conserved cysteines predicted to bind Zn2+ are shown as white-on-black. Annotation of this alignment is as Fig. 4. Species abbreviations as Figs. 4 and 5, except ARCFU, Archaeoglobus fulgidus METJA, Methanococcus jannaschii.
Fig. 6. Distribution of the most common folds in selected bacterial, archaeal, and eukaryotic proteomes. The vertical axis shows the fraction of all predicted folds in the respective proteome. Fold name abbreviations FAD/NAD, FAD/NAD(P)-binding Rossman-like domains TIM, TIM-barrel domains SAM-MTR, S-adenosylmethionine-dependent methyltransferases PK, serine-threonine protein kinases PP-Loop, ATP pyrophosphatases. mge, Mycoplasma genitalium rpr, Rickettsiaprowazekii hh x, Borrelia burgdorferi ctr, Chlamydia trachomatis hpy, Helicobacter pylori tma, Thermotoga maritima ssp, Synechocystis sp. mtu, Mycobacterium tuberculosis eco, Escherichia coli mja, Methanococcus jannaschii pho, Pyrococcus horikoshii see, Saccharomyces cerevisiae, cel, Caenorhabditis elegans. Fig. 6. Distribution of the most common folds in selected bacterial, archaeal, and eukaryotic proteomes. The vertical axis shows the fraction of all predicted folds in the respective proteome. Fold name abbreviations FAD/NAD, FAD/NAD(P)-binding Rossman-like domains TIM, TIM-barrel domains SAM-MTR, S-adenosylmethionine-dependent methyltransferases PK, serine-threonine protein kinases PP-Loop, ATP pyrophosphatases. mge, Mycoplasma genitalium rpr, Rickettsiaprowazekii hh x, Borrelia burgdorferi ctr, Chlamydia trachomatis hpy, Helicobacter pylori tma, Thermotoga maritima ssp, Synechocystis sp. mtu, Mycobacterium tuberculosis eco, Escherichia coli mja, Methanococcus jannaschii pho, Pyrococcus horikoshii see, Saccharomyces cerevisiae, cel, Caenorhabditis elegans.
The importance of H2 metabolism to some organisms is highlighted by their possession of more than one hydrogenase system. Four hydrogenase systems are known in Escherichia coli and Methanococcus voltae, three in Desufovibrio vulgaris and... [Pg.31]

Methanococcus mazeii 2[NiFe] hydrogenases Membrane-bound cytochrome b reducing (Vht) Membrane-bound cytochrome b reducing (Vho) Methanogenesis Methanogenesis H2/CO2, methanol, acetate Constitutive 10... [Pg.53]

Berghofer, Y., Agha-Amiri, K. and Klein, A. (1994) Selenium is involved in the negative regulation of the expression of selenium-free [NiFe] hydrogenases in Methanococcus voltae. Mol. Gen. Genet., 242, 369-73. [Pg.258]

Halboth, S. (1991) Molekulargenetische Untersuchung der Hydrogenasen aus Methanococcus voltae. Ph.D., University of Marburg. [Pg.264]


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Methanococcus jannaschii

Methanococcus vannielii

Methanococcus vannielli

Methanococcus voltae

Methanococcus voltae cation transport

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