{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["102(4)"],"submitter":["Haddad KC"],"pubmed_abstract":["alpha-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 His57 in resting enzymes is more mobile than previously th"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["1006-11"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC545854"],"repository":["biostudies-literature"],"pubmed_title":["alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities."],"pmcid":["PMC545854"],"pubmed_authors":["Sudmeier JL","Haddad KC","Bachovchin DA","Bachovchin WW"],"additional_accession":[]},"is_claimable":false,"name":"alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities.","description":"alpha-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 His57 in resting enzymes is more mobile than previously th","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Jan","modification":"2025-04-20T01:35:37.785Z","creation":"2019-03-27T01:08:32Z"},"accession":"S-EPMC545854","cross_references":{"pubmed":["15657134"],"doi":["10.1073/pnas.0409279102"]}}