{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Reynolds JA"],"funding":["NIH","NIGMS NIH HHS"],"pagination":["103069"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10060751"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["299(4)"],"pubmed_abstract":["Transferases are ubiquitous across all known life. While much work has been done to understand and describe these essential enzymes, there have been minimal efforts to exert tight and reversible control over their activity for various biotechnological applications. Here, we apply a rational, computation-guided methodology to design and test a transferase-class enzyme allosterically regulated by light-oxygen-voltage 2 sensing domain. We utilize computational techniques to determine the intrinsic allosteric networks within N-acyltransferase (Orf11/∗Dbv8) and identify potential allosteric sites on the protein's surface. We insert light-oxygen-voltage 2 sensing domain at the predicted allosteric site, exerting reversible control over enzymatic activity. We demonstrate blue-light regulation of "],"journal":["The Journal of biological chemistry"],"pubmed_title":["An engineered N-acyltransferase-LOV2 domain fusion protein enables light-inducible allosteric control of enzymatic activity."],"pmcid":["PMC10060751"],"funding_grant_id":["R35 GM134864"],"pubmed_authors":["Chirasani VR","Pritchard JR","Dokholyan NV","Vishweshwaraiah YL","Reynolds JA"],"additional_accession":[]},"is_claimable":false,"name":"An engineered N-acyltransferase-LOV2 domain fusion protein enables light-inducible allosteric control of enzymatic activity.","description":"Transferases are ubiquitous across all known life. While much work has been done to understand and describe these essential enzymes, there have been minimal efforts to exert tight and reversible control over their activity for various biotechnological applications. Here, we apply a rational, computation-guided methodology to design and test a transferase-class enzyme allosterically regulated by light-oxygen-voltage 2 sensing domain. We utilize computational techniques to determine the intrinsic allosteric networks within N-acyltransferase (Orf11/∗Dbv8) and identify potential allosteric sites on the protein's surface. We insert light-oxygen-voltage 2 sensing domain at the predicted allosteric site, exerting reversible control over enzymatic activity. We demonstrate blue-light regulation of ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2026-05-29T02:21:30.13Z","creation":"2025-02-19T02:23:43.569Z"},"accession":"S-EPMC10060751","cross_references":{"pubmed":["36841477"],"doi":["10.1016/j.jbc.2023.103069"]}}