Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri

Shima, Seigo; Hérault, David A.; Berkessel, Albrecht; Thauer, Rudolf K.

doi:10.1007/s002030050669

Cited by 58 publications

(48 citation statements)

References 29 publications

(30 reference statements)

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“…The role of DIP in the thermostabilization of enzymes remains questionable, although it has been shown to have a positive effect on the stabilization of glyceraldehyde-3-phosphate dehydrogenase of P. woesei, but did not increase the stability of hydrogenase and pyruvate ferredoxin oxidoreductase of Thermotoga maritima (Scholz et al, 1992;Ramakrishnan et al, 1997). The stabilizing effect of cBPG was also recently demonstrated on two enzymes involved in methane formation in Methanopyrus kandleri (Shima et al, 1998).…”

Section: The Role Of Hypersolutes In Thermoprotection Of Enzymesmentioning

confidence: 74%

Compatible solutes of organisms that live in hot saline environments

Santos

Costa

2002

Environmental Microbiology

248

206

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SummaryThe accumulation of organic solutes is a prerequisite for osmotic adjustment of all microorganisms. Thermophilic and hyperthermophilic organisms generally accumulate very unusual compatible solutes namely, di-myo -inositol-phosphate, di-mannosyl-di-myoinositol-phosphate, di-glycerol-phosphate, mannosylglycerate and mannosylglyceramide, which have not been identified in bacteria or archaea that grow at low and moderate temperatures. There is also a growing awareness that some of these compatible solutes may have a role in the protection of cell components against thermal denaturation. Mannosylglycerate and di-glycerol-phosphate have been shown to protect enzymes and proteins from thermal denaturation in vitro as well, or better, than compatible solutes from mesophiles. The pathways leading to the synthesis of some of these compatible solutes from thermophiles and hyperthermophiles have been elucidated. However, large numbers of questions remain unanswered. Fundamental and applied interest in compatible solutes and osmotic adjustment in these organisms, drives research that, will, in the near future, allow us to understand the role of compatible solutes in osmotic protection and thermoprotection of some of the most fascinating organisms known on Earth.

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Section: The Role Of Hypersolutes In Thermoprotection Of Enzymesmentioning

confidence: 74%

Compatible solutes of organisms that live in hot saline environments

Santos

Costa

2002

Environmental Microbiology

248

206

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“…The last reaction in this synthesis is the only one exergonic enough to drive the synthesis up to cDPG rather than to its precursor 2,3-DPG. Also, at pH 7.0, cDPG is a trianion whereas 2,3-DPG is a penta-anion; thus cDPG has a smaller effect on the ionic strength than would 2,3-DPG (305).…”

Section: Extrinsic Parametersmentioning

confidence: 94%

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

Vieille¹,

Zeikus

2001

Microbiol Mol Biol Rev

1,847

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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“…Residues 174-175 are disordered. The coordinates were deposited in the RCSB Protein Data Bank 13 with accession number 2 3 7 M. The chemical identities of the two Zn 21 ions were established by an anomalous difference map. Data collection and refinement statistics are listed in Table I.…”

Section: Methodsmentioning

confidence: 99%