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Volumn 3, Issue 1, 1999, Pages 39-46

Extremozymes

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME;

EID: 0033055662     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)80008-8     Document Type: Article
Times cited : (226)

References (64)
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    • Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
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    • This paper describes the crystal structure of a formyltransferase from a methanogenic Archaeon that grows optimally at 98°C and has an internal salt concentration of 1.5 M phosphate. The structure is therefore analysed in terms of the enzyme's combined thermophilic and halophilic nature.
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    • Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • One of the most lucid accounts of analysing the changes in kinetics and thermodynamics of protein thermostability after site-directed mutagenesis.
    • Pappenberger G, Schurig H, Jaenicke R Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. J Mol Biol. 274:1997;676-683. One of the most lucid accounts of analysing the changes in kinetics and thermodynamics of protein thermostability after site-directed mutagenesis.
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    • Adjustment of conformational flexibility is a key event in the thermal adaption of proteins
    • Isopropylmalate dehydrogenase from Thermus thermophilus has optimum activity at 22-25°C above the E. coli enzyme and a 17°C higher melting temperature. H-D exchange showed that the Thermus enzyme is significantly more rigid at room temperature, whereas both enzymes have similar flexibility at their respective optimum temperatures.
    • Zavodsky P, Kardos J, Svingor A, Petsko G Adjustment of conformational flexibility is a key event in the thermal adaption of proteins. Proc Nat Acad Sci USA. 95:1998;7406-7411. Isopropylmalate dehydrogenase from Thermus thermophilus has optimum activity at 22-25°C above the E. coli enzyme and a 17°C higher melting temperature. H-D exchange showed that the Thermus enzyme is significantly more rigid at room temperature, whereas both enzymes have similar flexibility at their respective optimum temperatures.
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    • Directed evolution of a thermostable esterase
    • Directed evolution of p-nitrobenzyl esterase from Bacillus subtilis produced a mutant with a 14°C increase in melting temperature with no reduction in catalytic activity at lower temperatures. This suggests that these properties are not necessarily inversely correlated, although mutations that increased stability without compromising activity were rare.
    • Giver L, Gershenson A, Freskgard P-O, Arnold FH Directed evolution of a thermostable esterase. Proc Natl Acad Sci USA. 95:1998;12809-12813. Directed evolution of p-nitrobenzyl esterase from Bacillus subtilis produced a mutant with a 14°C increase in melting temperature with no reduction in catalytic activity at lower temperatures. This suggests that these properties are not necessarily inversely correlated, although mutations that increased stability without compromising activity were rare.
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    • Engineering an enzyme to resist boiling
    • One of the most impressive examples of enzyme engineering that combines rationally designed mutations with changes based on sequence comparisons with thermostable homologues. A protease is produced that is able to function at 100°C but which retains wild type activity at 37°C.
    • Van den Burg B, Vriend G, Veltman OR, Venema G, Eijsink VGH Engineering an enzyme to resist boiling. Proc Natl Acad Sci USA. 95:1998;2056-2060. One of the most impressive examples of enzyme engineering that combines rationally designed mutations with changes based on sequence comparisons with thermostable homologues. A protease is produced that is able to function at 100°C but which retains wild type activity at 37°C.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2056-2060
    • Van Den Burg, B.1    Vriend, G.2    Veltman, O.R.3    Venema, G.4    Eijsink, V.G.H.5
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    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • An excellent example of in vivo evolutionary engineering to increase the thermostability of an enzyme while at the same time improving the catalytic activity.
    • Akanuma S, Yamagishi A, Tanaka N, Oshima T Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci. 7:1998;698-705. An excellent example of in vivo evolutionary engineering to increase the thermostability of an enzyme while at the same time improving the catalytic activity.
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    • An autonomously replicating transforming vector for Sulfolobus solfataricus
    • A plasmid shuttle vector able to transform and to be stably maintained both in S. solfataricus and in E. coli was constructed. The vector suffered no rearrangement and/or chromosome integration, and its copy number in Sulfolobus was increased by exposure of the cells to mitomycin C.
    • Cannio R, Contursi P, Rossi M, Bartolucci S An autonomously replicating transforming vector for Sulfolobus solfataricus. J Bacteriol. 180:1998;3237-3240. A plasmid shuttle vector able to transform and to be stably maintained both in S. solfataricus and in E. coli was constructed. The vector suffered no rearrangement and/or chromosome integration, and its copy number in Sulfolobus was increased by exposure of the cells to mitomycin C.
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    • Directed evolution of enzyme catalysts
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    • Kuchner O, Arnold FH Directed evolution of enzyme catalysts. Trends Biotechnol. 15:1997;523-530. Reviews the directed evolution approach to engineering biocatalysts, including techniques for creating and screening combinatorial enzyme libraries. Examples include the evolution of thermostability, resistance to organic solvents, substrate specificity and enantioselectivity.
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    • Cold adaptation of a mesophilic serine protease, subtilisin, by in vitro random mutagenesis
    • Random mutagenesis of subtilisin BPN′ resulted in the isolation of a mutant with increased activity at low temperature (1-10°C). The thermostability of the mutant was similar to the wild type enzyme.
    • Kano H, Taguchi S, Momose H Cold adaptation of a mesophilic serine protease, subtilisin, by in vitro random mutagenesis. Appl Microbiol Biotechnol. 47:1997;46-51. Random mutagenesis of subtilisin BPN′ resulted in the isolation of a mutant with increased activity at low temperature (1-10°C). The thermostability of the mutant was similar to the wild type enzyme.
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