N 5,N 10-Methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri

Klein, Andreas R.; Breitung, J.; Linder, Dietmar; Stetter, Karl O.; Thauer, Rudolf K.

doi:10.1007/bf00248474

Cited by 37 publications

(26 citation statements)

References 34 publications

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“…Inorganic salts stabilize proteins in two ways: (i) through a specific effect, where a metal ion interacts with the protein in a conformational manner (see "Metal binding" above), and (ii) through a general salt effect, which mainly affects the water activity. Thauer and colleagues studied the effect of salts on the thermostability and the activity of five M. kandleri methanogenic enzymes (36,37,181,224,225). While the five enzymes are activated and kinetically stabilized by salts, the extent of the salt effect is enzyme dependent.…”

Section: Extrinsic Parametersmentioning

confidence: 99%

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Vieille¹,

Zeikus

2001

Microbiol Mol Biol Rev

1,822

1,476

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Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth temperatures of >80°C), also called hyperthermophilic enzymes, are typically thermostable (i.e., resistant to irreversible inactivation at high temperatures) and are optimally active at high temperatures. These enzymes share the same catalytic mechanisms with their mesophilic counterparts. When cloned and expressed in mesophilic hosts, hyperthermophilic enzymes usually retain their thermal properties, indicating that these properties are genetically encoded. Sequence alignments, amino acid content comparisons, crystal structure comparisons, and mutagenesis experiments indicate that hyperthermophilic enzymes are, indeed, very similar to their mesophilic homologues. No single mechanism is responsible for the remarkable stability of hyperthermophilic enzymes. Increased thermostability must be found, instead, in a small number of highly specific alterations that often do not obey any obvious traffic rules. After briefly discussing the diversity of hyperthermophilic organisms, this review concentrates on the remarkable thermostability of their enzymes. The biochemical and molecular properties of hyperthermophilic enzymes are described. Mechanisms responsible for protein inactivation are reviewed. The molecular mechanisms involved in protein thermostabilization are discussed, including ion pairs, hydrogen bonds, hydrophobic interactions, disulfide bridges, packing, decrease of the entropy of unfolding, and intersubunit interactions. Finally, current uses and potential applications of thermophilic and hyperthermophilic enzymes as research reagents and as catalysts for industrial processes are described

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Section: Extrinsic Parametersmentioning

confidence: 99%

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Vieille¹,

Zeikus

2001

Microbiol Mol Biol Rev

1,822

1,476

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“…F,,o is a 5' deazaflavin derivative found in relatively high concentrations in methanogenic archaea (Gorris & van der Drift, 1994). See also the legend to Heterodisulphide reductase (hdrA, hdrBC)++ Schmitz et al (1994) ; Bertram & ; Bertram et al (1994a, b) ; Wasserfallen (1994) ; Hochheimer et al (1995Hochheimer et al ( , 1996; Vorholt et al (1996Vorholt et al ( , 1997b Ermler et al (1997a) ; Kunow et al (1996) 1998) Shima et al (1995 ; Lehmacher Klein et al (1993a) ; Vaupel et al (1996, Klein et al (1993b ; Kunow et al (1993) ;…”

Section: Energy Metabolism Of Methanoarchaeamentioning

confidence: 99%

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

1998

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Historical overview In 1933, Stephenson & Stickland (1933a) published that they had isolated from river mud, by the single cell technique, a methanogenic organism capable of growth in an inorganic medium with formate as the sole carbon source. 4 H C 0 0-+ 4H' + CH, + 3 C 0 , + 2H,O AGO' =-144-5 kJ mol-' Methane formation from formate was shown to occur in a stepwise manner, by the preliminary decomposition of formic acid into CO, and H, followed by a reduction of CO, by H,, suggesting that formate was not an intermediate in the reduction of CO, to methane. HCOO-+ H+-+ H, + CO, 4H,+CO,-+ C H , + 2 H 2 0 AGO' =-3-5 kJ mol-' AGO' =-131 kJ mol-' Cell suspensions of the microorganism catalysed the reduction of methylene blue with H,, indicating that the methanogen contained an enzyme which activates molecular hydrogen. H,-+ 2e-+ 2H+ E; =-414mV This enzyme had been discovered by Stephenson & Stickland (1931a) 2 years before in a number of bacterial species and was named by them 'hydrogenase'. The paper by Stephenson & Stickland (1933a) is considered to mark the beginning of the modern era for study of methanogenesis (Wolfe, 1993). It is the first Except when otherwise noted, the free energy changes given for methanogenic reactions were calculated from the free energies of formation from the elements of the substrates and products with non-gaseous compounds at 1 M aqueous solution and gaseous compounds in the gaseous state at 1 atmosphere pressure (101 kPa). The free energy changes of formation were taken from Thauer eta/. (1977). 0002-2667 0 1998 SGM Glucose-+ 3C0, + 3CH, AGO' =-418.1 kJ mol-' This reaction is not catalysed by single microorganisms but by syntrophic associations of microorganisms. First the glucose is fermented to acetate, CO, and H, or to acetate, formate and H, : Glucose + 2H,O + 2CH3COO-+ 2H' + 2C0, + 4H2 AGO' =-215.7 kJ mol-' Glucose + 2H20-+ 2CH3COO-+ 2HC00-+ 4H' + 2H, AGO' =-208.7 kJ mol-1 These fermentations are brought about by strictly anaerobic bacteria and/or protozoa. In a second step, the products of glucose fermentation are then converted to methane, the rate of conversion being such that the concentrations of acetate (< 1 mM), formate (< 0.1 mM) and H, (< 1 pM) in the anaerobic sediments remain very low (Zinder, 1993). CH3COO-+Hf-+ C02+CH, AGO' =-36 kJ mol-' 4H, + CO,-+ CH, + 2H20 AGO' =-131 kJ mol-' 4HC00-+4H+ + CH,+3C02+2H,0 AGO' =-144.5 kJ mol-' H-S-CoM, coenzyme M ; H-S-COB, coenzyme B ; H,SPT, tetrahydrosarcinapterin, which is the modified tetrahydromethanopterin (for structures see Fig. 3) present in the Methanosarcinales (Gorris & van der Drift, 1994). Reaction" Enzyme (gene) Most recent literature Acetate + CoA + acetyl-CoA + H,O AGO' = + 35.7 k J rnol-lt

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confidence: 97%

“…Many of these solutes have only been identified in marine thermophiles and hyperthermophiles and may constitute an adaptive feature of these organisms to high temperatures (8; Santos and da Costa, submitted). This view is supported by the enlarged intracellular pools of organic solutes accumulating in response to growth at supraoptimal temperatures (14,20,24,26,36) and by the demonstration of the protecting effect of some of these solutes against heat inactivation of several enzymes in vitro (14,18,29,31,32).A few years ago we discovered and characterized the new compound DGP (the correct chemical designation is 1,1Ј-diglyceryl phosphate) as the major solute accumulating in the hyperthermophilic archaeon Archaeoglobus fulgidus primarily in response to a salt stress (26). When A. fulgidus was grown in medium containing 4.5% NaCl, the intracellular levels reached approximately 1.4 mol ⅐ mg of protein Ϫ1 (26), which corresponds to a concentration of 350 mM, providing that the value of 2.2 l ⅐ mg of dry weight Ϫ1 determined for the internal volume of Pyrococcus furiosus (24) is appropriate.…”

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confidence: 98%

Thermostabilization of Proteins by Diglycerol Phosphate, a New Compatible Solute from the Hyperthermophile Archaeoglobus fulgidus

Lamosa

Burke

Peist

et al. 2000

Appl Environ Microbiol

102

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Appl. Environ. Microbiol. 63:896-902, 1997). This solute was purified after extraction from the cell biomass. In addition, the optically active and the optically inactive (racemic) forms of the compound were synthesized, and the ability of the solute to act as a protecting agent against heating was tested on several proteins derived from mesophilic or hyperthermophilic sources. Diglycerol phosphate exerted a considerable stabilizing effect against heat inactivation of rabbit muscle lactate dehydrogenase, baker's yeast alcohol dehydrogenase, and Thermococcus litoralis glutamate dehydrogenase. Highly homologous and structurally well-characterized rubredoxins from Desulfovibrio gigas, Desulfovibrio desulfuricans (ATCC 27774), and Clostridium pasteurianum were also examined for their thermal stabilities in the presence or absence of diglycerol phosphate, glycerol, and inorganic phosphate. These proteins showed different intrinsic thermostabilities, with half-lives in the range of 30 to 100 min. Diglycerol phosphate exerted a strong protecting effect, with approximately a fourfold increase in the half-lives for the loss of the visible spectra of D. gigas and C. pasteurianum rubredoxins. In contrast, the stability of D. desulfuricans rubredoxin was not affected. These different behaviors are discussed in the light of the known structural features of rubredoxins. The data show that diglycerol phosphate is a potentially useful protein stabilizer in biotechnological applications.One of the most striking characteristics of extremophiles is their ability to thrive under environmental conditions that would be lethal to most organisms. In particular, hyperthermophiles, having optimal growth temperatures above 80°C (4), pose intriguing questions regarding the biochemical strategies used for the adaptation of their cellular structures to withstand such high temperatures. Maintaining protein performance at high temperature could be accomplished by a number of mechanisms: (i) intrinsic thermostability, (ii) increased turnover, (iii) improved action of molecular chaperones, and (iv) extrinsic stabilization by compatible solutes (13). Although most enzymes from thermophilic sources show an intrinsic thermostability higher than that of their mesophilic counterparts, several enzymes derived from hyperthermophilic sources show an unexpectedly low intrinsic stability in vitro (13,14). Therefore, extrinsic factors, such as compatible solutes, may play a role in the thermostabilization of these cellular components.Some compatible solutes, namely, glutamate, betaine, and trehalose, are widespread in mesophilic organisms, but compatible solutes unique to thermophiles and hyperthermophiles have also been identified in recent years (8; H. Santos and M. S. da Costa, submitted for publication). Newly discovered solutes from thermophilic and hyperthermophilic organisms include cyclic-2,3-bisphosphoglycerate (17), two isomers of dimyo-inositol phosphate (25, 31), mannosylglycerate and mannosylglyceramide (24, 28, 36), di-mannosyl-di-myo-inosito...

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N 5,N 10-Methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri

Cited by 37 publications

References 34 publications

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

Thermostabilization of Proteins by Diglycerol Phosphate, a New Compatible Solute from the Hyperthermophile Archaeoglobus fulgidus

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