Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes

Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes

Item
http://www.wikidata.org/entity/Q27759625
Three-dimensional structures of the three human class I alcohol dehydrogenasesEnzymes: An integrated view of structure, dynamics and functionAtomic-Resolution Structures of Horse Liver Alcohol Dehydrogenase with NAD + and Fluoroalcohols Define Strained Michaelis ComplexesEffects of Cavities at the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase on Structure, Dynamics and CatalysisAldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate specificity, and clinical applicationEffects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reactionConformational changes and catalysis by alcohol dehydrogenase.Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactionsActive site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures.Ocular aldehyde dehydrogenases: protection against ultraviolet damage and maintenance of transparency for vision.Protein motions and the activation of the CH bond catalyzed by dihydrofolate reductase.The ternary complex of Pseudomonas aeruginosa alcohol dehydrogenase with NADH and ethylene glycolThe effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.Molecular dynamics simulations of NAD+-induced domain closure in horse liver alcohol dehydrogenase.Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase. Implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes.Contribution of Buried Distal Amino Acid Residues in Horse Liver Alcohol Dehydrogenase to Structure and Catalysis.NMR investigation of Tyr105 mutants in TEM-1 beta-lactamase: dynamics are correlated with function.
P2860

Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes

Item
http://www.wikidata.org/entity/Q27759625
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
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1998年論文
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1998年論文
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1998年論文
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1998年論文
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1998年論文
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1998年论文
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name
Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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Active site modifications in a ...... of two enzyme-ligand complexes
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P2093
P304
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P356
P407
P433
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P577
P698