{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wieland M"],"funding":["European Research Council"],"pagination":["8462-8478"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12090219"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(10)"],"pubmed_abstract":["Photoswitchable unnatural amino acids are valuable engineering tools in biotechnology, particularly for the reversible control of enzymes with light. Here, we explore some basic principles of this protein engineering technique to simplify its approach and increase its success rate. To this end, we have selected <i>Escherichia coli</i> type II asparaginase (EcAII), which is a prominent chemotherapeutic enzyme that is limited by detrimental side effects associated with its promiscuous glutaminase activity. Incorporation of phenylalanine-4'-azobenzene (AzoF) combined with extensive biophysical characterizations identified two light-sensitive variants, in which glutamine hydrolysis could be reversibly (de)activated up to 9-fold, whereas asparaginase hydrolysis was only marginally light-respons"],"journal":["ACS catalysis"],"pubmed_title":["Reversible Substrate-Specific Photocontrol of the Chemotherapeutic Asparaginase(-Glutaminase) from &lt;i&gt;Escherichia coli&lt;/i&gt;."],"pmcid":["PMC12090219"],"funding_grant_id":["101112805","101158166","101088032"],"pubmed_authors":["Wieland M","Duran C","Luizaga J","Hiefinger C","Bruckmann A","Hupfeld A","Osuna S","Germscheid B","Rein J"],"additional_accession":[]},"is_claimable":false,"name":"Reversible Substrate-Specific Photocontrol of the Chemotherapeutic Asparaginase(-Glutaminase) from &lt;i&gt;Escherichia coli&lt;/i&gt;.","description":"Photoswitchable unnatural amino acids are valuable engineering tools in biotechnology, particularly for the reversible control of enzymes with light. Here, we explore some basic principles of this protein engineering technique to simplify its approach and increase its success rate. To this end, we have selected <i>Escherichia coli</i> type II asparaginase (EcAII), which is a prominent chemotherapeutic enzyme that is limited by detrimental side effects associated with its promiscuous glutaminase activity. Incorporation of phenylalanine-4'-azobenzene (AzoF) combined with extensive biophysical characterizations identified two light-sensitive variants, in which glutamine hydrolysis could be reversibly (de)activated up to 9-fold, whereas asparaginase hydrolysis was only marginally light-respons","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-01T07:53:21.802Z","creation":"2026-04-08T10:45:49.8Z"},"accession":"S-EPMC12090219","cross_references":{"pubmed":["40401100"],"doi":["10.1021/acscatal.5c01608"]}}