{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zheng C"],"funding":["U.S. Department of Health &amp; Human Services | NIH | National Institute of General Medical Sciences","DOE | SC | Basic Energy Sciences","NIGMS NIH HHS","U.S. Department of Health &amp; Human Services | National Institutes of Health"],"pagination":["1715-1721"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10906027"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(12)"],"pubmed_abstract":["The design and improvement of enzymes based on physical principles remain challenging. Here we demonstrate that the principle of electrostatic catalysis can be leveraged to substantially improve a natural enzyme's activity. We enhanced the active-site electric field in horse liver alcohol dehydrogenase by replacing the serine hydrogen-bond donor with threonine and replacing the catalytic Zn<sup>2+</sup> with Co<sup>2+</sup>. Based on the electric field enhancement, we make a quantitative prediction of rate acceleration-50-fold faster than the wild-type enzyme-which was in close agreement with experimental measurements. The effects of the hydrogen bonding and metal coordination, two distinct chemical forces, are described by a unified physical quantity-electric field, which is quantitative,"],"journal":["Nature chemistry"],"pubmed_title":["Enhanced active-site electric field accelerates enzyme catalysis."],"pmcid":["PMC10906027"],"funding_grant_id":["P30GM133894","GM118044","P30 GM133894","R35 GM118044","DE-AC02-76SF00515"],"pubmed_authors":["Boxer SG","Mathews II","Zheng C","Ji Z"],"additional_accession":[]},"is_claimable":false,"name":"Enhanced active-site electric field accelerates enzyme catalysis.","description":"The design and improvement of enzymes based on physical principles remain challenging. Here we demonstrate that the principle of electrostatic catalysis can be leveraged to substantially improve a natural enzyme's activity. We enhanced the active-site electric field in horse liver alcohol dehydrogenase by replacing the serine hydrogen-bond donor with threonine and replacing the catalytic Zn<sup>2+</sup> with Co<sup>2+</sup>. Based on the electric field enhancement, we make a quantitative prediction of rate acceleration-50-fold faster than the wild-type enzyme-which was in close agreement with experimental measurements. The effects of the hydrogen bonding and metal coordination, two distinct chemical forces, are described by a unified physical quantity-electric field, which is quantitative,","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2026-06-02T10:40:43.218Z","creation":"2025-04-04T01:23:55.049Z"},"accession":"S-EPMC10906027","cross_references":{"pubmed":["37563323"],"doi":["10.1038/s41557-023-01287-x"]}}