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• W2022378511 endingPage "1011" @default.
• W2022378511 startingPage "1006" @default.
• W2022378511 abstract "α-Lytic protease is a bacterial serine protease widely studied as a model system of enzyme catalysis. Here we report that lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity. This effect of lyophilization permits a unique opportunity for investigating the relationship between histidine ring dynamics and catalytic activity. The results demonstrate that His 57 in resting enzymes is more mobile than previously thought, especially when protonated. The histidine motion and its correlation to enzyme activity lend support to the reaction-driven ring flip hypothesis." @default.
• W2022378511 created "2016-06-24" @default.
• W2022378511 creator A5003681632 @default.
• W2022378511 creator A5026040172 @default.
• W2022378511 creator A5061974401 @default.
• W2022378511 creator A5079399311 @default.
• W2022378511 date "2005-01-18" @default.
• W2022378511 modified "2023-09-27" @default.
• W2022378511 title "α-Lytic protease can exist in two separately stable conformations with different His ⁵⁷ mobilities and catalytic activities" @default.
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• W2022378511 doi "https://doi.org/10.1073/pnas.0409279102" @default.
• W2022378511 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/545854" @default.
• W2022378511 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15657134" @default.
• W2022378511 hasPublicationYear "2005" @default.
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