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How enzymes adapt: lessons from directed evolution
scientific article (publication date: February 2001)
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scholarly article
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review article
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Europe PubMed Central
title
How enzymes adapt: lessons from directed evolution
(English)
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main subject
directed evolution
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author
Anne Gershenson
object named as
A Gershenson
series ordinal
4
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author name string
F H Arnold
series ordinal
1
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P L Wintrode
series ordinal
2
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K Miyazaki
series ordinal
3
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language of work or name
English
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publication date
February 2001
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published in
Trends in Biochemical Sciences
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volume
26
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issue
2
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page(s)
100-6
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cites work
The stability of proteins in extreme environments
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Crossref
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The crystal structure of citrate synthase from the hyperthermophilic archaeon pyrococcus furiosus at 1.9 A resolution,
1 reference
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Crossref
reference URL
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Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
1 reference
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Finding and using hyperthermophilic enzymes.
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reference URL
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Rigidity of Thermophilic Enzymes
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Rapid evolution of a protein in vitro by DNA shuffling
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reference URL
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Molecular evolution by staggered extension process (StEP) in vitro recombination
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Crossref
reference URL
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Directed evolution study of temperature adaptation in a psychrophilic enzyme
1 reference
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reference URL
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Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function
1 reference
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Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
1 reference
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Improving the catalytic activity of a thermophilic enzyme at low temperatures
1 reference
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reference URL
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Directed evolution of a thermostable esterase.
1 reference
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Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases
1 reference
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Directed evolution converts subtilisin E into a functional equivalent of thermitase
1 reference
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Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution
1 reference
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A cold-adapted protease engineered by experimental evolution system
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Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution
1 reference
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A structural view of evolutionary divergence
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Stability and Activity of Mesophilic Subtilisin E and Its Thermophilic Homolog: Insights from Molecular Dynamics Simulations
1 reference
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Enzymes under extremes of physical conditions
1 reference
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reference URL
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Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
1 reference
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Crossref
reference URL
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7 January 2021
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inferred from DOI database lookup
Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
1 reference
stated in
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reference URL
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Amino acid substitutions enhancing thermostability of Bacillus polymyxa beta-glucosidase A
1 reference
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Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis
1 reference
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Crossref
reference URL
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Engineering an enzyme to resist boiling
1 reference
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reference URL
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Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
1 reference
stated in
Crossref
reference URL
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The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges.
1 reference
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Crossref
reference URL
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7 January 2021
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Identifiers
DOI
10.1016/S0968-0004(00)01755-2
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2861216
OpenCitations bibliographic resource ID
2861216
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2861216
PubMed publication ID
11166567
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2861216
ResearchGate publication ID
12162795
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