Abstract
The enzymatic activity of the protease subtilisin in anhydrous organic solvents can be dramatically increased by pretreating the enzyme before it is placed in the nonaqueous medium. For instance, lyophilization of subtilisin from aqueous solution containing competitive inhibitors (followed by their removal) created an enzyme which was up to 100 times more active than the enzyme lyophilized in the absence of such ligands. This phenomenon of ligand-induced "enzyme memory" also extends to the stability, affinity, and substrate specificity of subtilisin in organic solvents.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Binding, Competitive
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Enzyme Activation / drug effects
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Enzyme Inhibitors / pharmacology*
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Esterification
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Freeze Drying
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Hydrolysis
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Kinetics
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Protein Conformation / drug effects
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Solvents*
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Substrate Specificity
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Subtilisins / antagonists & inhibitors
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Subtilisins / metabolism*
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Tryptophan / analogs & derivatives
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Tryptophan / pharmacology
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Tyrosine / analogs & derivatives
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Tyrosine / pharmacology
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Water
Substances
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Enzyme Inhibitors
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Solvents
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Water
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N-acetyltyrosylamide
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N-acetyltryptophanamide
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Tyrosine
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Tryptophan
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Subtilisins