{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rigouin C"],"funding":["BLRD VA","NIBIB NIH HHS"],"pagination":["10224"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5579231"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["L-asparaginase is a chemotherapy drug used to treat acute lymphoblastic leukemia (ALL). The main prerequisite for clinical efficacy of L-asparaginases is micromolar K<sub>M</sub> for asparagine to allow for complete depletion of this amino acid in the blood. Since currently approved L-asparaginases are of bacterial origin, immunogenicity is a challenge, which would be mitigated by a human enzyme. However, all human L-asparaginases have millimolar K<sub>M</sub> for asparagine. We recently identified the low K<sub>M</sub> guinea pig L-asparaginase (gpASNase1). Because gpASNase1 and human L-asparaginase 1 (hASNase1) share ~70% amino-acid identity, we decided to humanize gpASNase1 by generating chimeras with hASNase1 through DNA shuffling. To identify low K<sub>M</sub> chimeras we developed a "],"journal":["Scientific reports"],"pubmed_title":["Discovery of human-like L-asparaginases with potential clinical use by directed evolution."],"pmcid":["PMC5579231"],"funding_grant_id":["I01 BX001919","R01 EB013685"],"pubmed_authors":["Schalk AM","Lavie A","Rigouin C","Nguyen HA"],"additional_accession":[]},"is_claimable":false,"name":"Discovery of human-like L-asparaginases with potential clinical use by directed evolution.","description":"L-asparaginase is a chemotherapy drug used to treat acute lymphoblastic leukemia (ALL). The main prerequisite for clinical efficacy of L-asparaginases is micromolar K<sub>M</sub> for asparagine to allow for complete depletion of this amino acid in the blood. Since currently approved L-asparaginases are of bacterial origin, immunogenicity is a challenge, which would be mitigated by a human enzyme. However, all human L-asparaginases have millimolar K<sub>M</sub> for asparagine. We recently identified the low K<sub>M</sub> guinea pig L-asparaginase (gpASNase1). Because gpASNase1 and human L-asparaginase 1 (hASNase1) share ~70% amino-acid identity, we decided to humanize gpASNase1 by generating chimeras with hASNase1 through DNA shuffling. To identify low K<sub>M</sub> chimeras we developed a ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Aug","modification":"2026-05-04T06:32:36.296Z","creation":"2019-03-27T02:55:08Z"},"accession":"S-EPMC5579231","cross_references":{"pubmed":["28860480"],"doi":["10.1038/s41598-017-10758-4"]}}