Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability

Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability

Item
http://www.wikidata.org/entity/Q27621093
Structural Basis for Thermostability of -Glycosidase from the Thermophilic Eubacterium Thermus nonproteolyticus HG102Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogasterHyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostabilityStructural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase IICrystallization and preliminary X-ray diffraction analysis of the Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase I86A mutant.Molecular characterization of an NADPH-dependent acetoin reductase/2,3-butanediol dehydrogenase from Clostridium beijerinckii NCIMB 8052.Extreme makeover: Engineering the activity of a thermostable alcohol dehydrogenase (AdhD) from Pyrococcus furiosus.Determining the roles of the three alcohol dehydrogenases (AdhA, AdhB and AdhE) in Thermoanaerobacter ethanolicus during ethanol formation.Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution.Stability and fibril formation properties of human and fish transthyretin, and of the Escherichia coli transthyretin-related protein.Diversity in αβ and βα Loop Connections in TIM Barrel Proteins: Implications for Stability and Design of the Fold.In vitro biocatalytic pathway design: orthogonal network for the quantitative and stereospecific amination of alcohols.Methodology Development in Directed Evolution: Exploring Options when Applying Triple-Code Saturation Mutagenesis.A Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase mutant derivative highly active and stereoselective on phenylacetone and benzylacetone.Role of conformational dynamics in the evolution of novel enzyme function.
P2860

Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability

Item
http://www.wikidata.org/entity/Q27621093
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
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1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
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name
Crystal structure of a thermop ...... pecificity and thermostability
@ast
Crystal structure of a thermop ...... pecificity and thermostability
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Crystal structure of a thermop ...... pecificity and thermostability
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type
label
Crystal structure of a thermop ...... pecificity and thermostability
@ast
Crystal structure of a thermop ...... pecificity and thermostability
@en
Crystal structure of a thermop ...... pecificity and thermostability
@nl
prefLabel
Crystal structure of a thermop ...... pecificity and thermostability
@ast
Crystal structure of a thermop ...... pecificity and thermostability
@en
Crystal structure of a thermop ...... pecificity and thermostability
@nl
P1433
P1476
P2093
P2860
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P356
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P921
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P1433
P1476
Crystal structure of a thermop ...... pecificity and thermostability
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P2093
P2860
P304
P31
P356
10.1002/(SICI)1097-0134(19991201)37:4<619::AID-PROT12>3.0.CO;2-H
P407
P433
P478
P577
P698
P921