Catalyzing “Hot” Reactions: Enzymes from Hyperthermophilic Archaea
Identifieur interne : 003409 ( Main/Exploration ); précédent : 003408; suivant : 003410Catalyzing “Hot” Reactions: Enzymes from Hyperthermophilic Archaea
Auteurs : Tadayuki Imanaka [Japon] ; Haruyuki Atomi [Japon]Source :
- The Chemical Record [ 1527-8999 ] ; 2002-05.
English descriptors
- Teeft :
- Acidic residues, Active sites, Adac, Amino acids, Appl environ microbiol, Archaea, Associate professor, Atomi, Basic principles, Biochem, Biochem biophys, Biological chemistry, Calvin cycle, Catalyzing, Chemical record, Circular dichroism, Complete genome sequences, Deep vent, Dimerization surface, Elemental sulfur, Enzyme, Enzyme activity, Exonuclease, Exonuclease activity, Exonuclease domain, Febs lett, Forked point, Fruitful collaborations, Fujiwara, Genome, Glutamate dehydrogenase, Graduate school, Growth rate, Heat treatment, Hexameric form, High activity, High temperature, High temperatures, Hydrophobic interactions, Hydrophobic residues, Hyperthermophiles, Hyperthermophilic, Hyperthermophilic archaea, Imanaka, Ionic interactions, Japan chemical journal forum, Kod1, Kod1 cells, Kodakaraensis, Kodakaraensis kod1, Kyoto university, Ligase, Ligase activity, Ligation, Lower exonuclease activity, Mesophilic proteins, Methods enzymol, Moderate thermophiles, Molecular mass, Mutant, Mutant proteins, Mutation frequency, Native enzyme, Neutral protease, Nishioka, Osaka university, Phosphodiester bond formation, Phylogenetic tree, Polar residues, Polyclonal antibodies, Polymerase, Polymerase activity, Polymerase domain, Primary structure, Primary structures, Proc natl acad, Product substrate, Protein engineering, Protein product, Protein thermostability, Recombinant, Recombinant enzyme, Recombinant hexamers, Recombinant protein, Ribulose, Rubisco, Rubisco activity, Sasa, Secondary structure, Simplest forms, Strain kod1, Structural analyses, Structural comparison, Structural studies, Subunit, Synthetic chemistry, Tadayuki imanaka, Takagi, Template strand, Thermococcus, Thermococcus kodakaraensis kod1, Thermophiles, Thermostability, Thermostable, Thermostable enzymes, Thermostable proteins, Thumb domain, Undesirable elongation, Wiley periodicals.
Abstract
We reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1 and its enzymes. The strain can grow at temperatures up to the boiling point and also represents one of the simplest forms of life. As expected, all enzymes displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, we focus on a few enzymes that are useful in application, and whose three‐dimensional structures are characteristic of thermostable enzymes. © 2002 The Japan Chemical Journal Forum and Wiley Periodicals, Inc. Chem Rec 2: 149–163, 2002: Published online in Wiley InterScience (www.interscience.wiley.com) DOI 10.1002/tcr.10023
Url:
DOI: 10.1002/tcr.10023
Affiliations:
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record</term><term>Circular dichroism</term><term>Complete genome sequences</term><term>Deep vent</term><term>Dimerization surface</term><term>Elemental sulfur</term><term>Enzyme</term><term>Enzyme activity</term><term>Exonuclease</term><term>Exonuclease activity</term><term>Exonuclease domain</term><term>Febs lett</term><term>Forked point</term><term>Fruitful collaborations</term><term>Fujiwara</term><term>Genome</term><term>Glutamate dehydrogenase</term><term>Graduate school</term><term>Growth rate</term><term>Heat treatment</term><term>Hexameric form</term><term>High activity</term><term>High temperature</term><term>High temperatures</term><term>Hydrophobic interactions</term><term>Hydrophobic residues</term><term>Hyperthermophiles</term><term>Hyperthermophilic</term><term>Hyperthermophilic archaea</term><term>Imanaka</term><term>Ionic interactions</term><term>Japan chemical journal forum</term><term>Kod1</term><term>Kod1 cells</term><term>Kodakaraensis</term><term>Kodakaraensis 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The strain can grow at temperatures up to the boiling point and also represents one of the simplest forms of life. As expected, all enzymes displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, we focus on a few enzymes that are useful in application, and whose three‐dimensional structures are characteristic of thermostable enzymes. © 2002 The Japan Chemical Journal Forum and Wiley Periodicals, Inc. Chem Rec 2: 149–163, 2002: Published online in Wiley InterScience (www.interscience.wiley.com) DOI 10.1002/tcr.10023</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région du Kansai</li></region><settlement><li>Kyoto</li></settlement><orgName><li>Université de Kyoto</li></orgName></list><tree><country name="Japon"><region name="Région du Kansai"><name sortKey="Imanaka, Tadayuki" sort="Imanaka, Tadayuki" uniqKey="Imanaka T" first="Tadayuki" last="Imanaka">Tadayuki Imanaka</name></region><name sortKey="Atomi, Haruyuki" sort="Atomi, Haruyuki" uniqKey="Atomi H" first="Haruyuki" last="Atomi">Haruyuki Atomi</name><name sortKey="Imanaka, Tadayuki" sort="Imanaka, Tadayuki" uniqKey="Imanaka T" first="Tadayuki" last="Imanaka">Tadayuki Imanaka</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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