Enzymes, Extremely Thermostable

Hicks, Paula M; Adams, Michael W. W.; Kelly, Robert M.

doi:10.1002/0471250589.ebt081

Cited by 2 publications

(1 citation statement)

References 200 publications

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“…In nature there are many examples of organisms adapted to high temperatures. They can be classified as thermophiles with optimal growth temperatures between 333 K and 353 K, and hyperthermophiles with optimal growth temperatures between 353 K and 383 K, as opposed to the non-adapted mesophiles with optimal growth temperatures between 298 K and 323 K. Generally, enzymes belonging to these adapted organisms are also thermostable enzymes with T m , the temperature at which 50% of the proteins are folded, close to the organism's optimal growth temperature [1]. The most studied thermostable protein is rubredoxin, from Pyrococcus furiosus, which presents an optimal growth temperature of 373 K [2].…”

Section: Introductionmentioning

confidence: 99%

Molecular basis of thermal stability in truncated (2/2) hemoglobins

Bustamante

Bonamore

Nadra

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Section: Introductionmentioning

confidence: 99%

Molecular basis of thermal stability in truncated (2/2) hemoglobins

Bustamante

Bonamore

Nadra

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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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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Enzymes, Extremely Thermostable

Cited by 2 publications

References 200 publications

Molecular basis of thermal stability in truncated (2/2) hemoglobins

Molecular basis of thermal stability in truncated (2/2) hemoglobins

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

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