{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Prasad S"],"funding":["NHLBI NIH HHS"],"pagination":["13785-90"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC283499"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["100(24)"],"pubmed_abstract":["Monovalent-cation-activated enzymes are abundantly represented in plants and in the animal world. Most of these enzymes are specifically activated by K+, whereas a few of them show preferential activation by Na+. The monovalent cation specificity of these enzymes remains elusive in molecular terms and has not been reengineered by site-directed mutagenesis. Here we demonstrate that thrombin, a Na+-activated allosteric enzyme involved in vertebrate blood clotting, can be converted into a K+-specific enzyme by redesigning a loop that shapes the entrance to the cation-binding site. The conversion, however, does not result into a K+-activated enzyme."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Redesigning the monovalent cation specificity of an enzyme."],"pmcid":["PMC283499"],"funding_grant_id":["R01 HL049413","HL58141","R29 HL049413","R01 HL073813","HL49413","HL73813","R01 HL058141"],"pubmed_authors":["Banerjee Roy D","Prasad S","Di Cera E","Bush LA","Cantwell AM","Wright KJ"],"additional_accession":[]},"is_claimable":false,"name":"Redesigning the monovalent cation specificity of an enzyme.","description":"Monovalent-cation-activated enzymes are abundantly represented in plants and in the animal world. Most of these enzymes are specifically activated by K+, whereas a few of them show preferential activation by Na+. The monovalent cation specificity of these enzymes remains elusive in molecular terms and has not been reengineered by site-directed mutagenesis. Here we demonstrate that thrombin, a Na+-activated allosteric enzyme involved in vertebrate blood clotting, can be converted into a K+-specific enzyme by redesigning a loop that shapes the entrance to the cation-binding site. The conversion, however, does not result into a K+-activated enzyme.","dates":{"release":"2003-01-01T00:00:00Z","publication":"2003 Nov","modification":"2025-04-26T04:21:10.777Z","creation":"2019-03-26T23:52:09Z"},"accession":"S-EPMC283499","cross_references":{"pubmed":["14612565"],"doi":["10.1073/pnas.2333109100"]}}