{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(1)"],"submitter":["Biundo A"],"pubmed_abstract":["The activity of the esterase (Cbotu_EstA) from Clostridium botulinum on the polyester poly(ethylene terephthalate) (PET) was improved by concomitant engineering of two different domains. On the one hand, the zinc-binding domain present in Cbotu_EstA was subjected to site-directed mutagenesis. On the other hand, a specific domain consisting of 71 amino acids at the N-terminus of the enzyme was deleted. Interestingly, a combination of substitution of residues present in the zinc-binding domain (e.g. S199A) synergistically increased the activity of the enzyme on PET seven fold when combined to the truncation of 71 amino acids at the N-terminus of the enzyme only. Overall, when compared to the native enzyme, the combination of truncation and substitutions in the zinc-binding domain lead to a 5"],"journal":["Scientific reports"],"pagination":["3745"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5829244"],"repository":["biostudies-literature"],"pubmed_title":["Synergistic effect of mutagenesis and truncation to improve a polyesterase from Clostridium botulinum for polyester hydrolysis."],"pmcid":["PMC5829244"],"pubmed_authors":["Guebitz GM","Ribitsch D","Reich J","Biundo A"],"additional_accession":[]},"is_claimable":false,"name":"Synergistic effect of mutagenesis and truncation to improve a polyesterase from Clostridium botulinum for polyester hydrolysis.","description":"The activity of the esterase (Cbotu_EstA) from Clostridium botulinum on the polyester poly(ethylene terephthalate) (PET) was improved by concomitant engineering of two different domains. On the one hand, the zinc-binding domain present in Cbotu_EstA was subjected to site-directed mutagenesis. On the other hand, a specific domain consisting of 71 amino acids at the N-terminus of the enzyme was deleted. Interestingly, a combination of substitution of residues present in the zinc-binding domain (e.g. S199A) synergistically increased the activity of the enzyme on PET seven fold when combined to the truncation of 71 amino acids at the N-terminus of the enzyme only. Overall, when compared to the native enzyme, the combination of truncation and substitutions in the zinc-binding domain lead to a 5","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Feb","modification":"2026-04-30T09:33:29.43Z","creation":"2019-03-26T23:04:59Z"},"accession":"S-EPMC5829244","cross_references":{"pubmed":["29487314"],"doi":["10.1038/s41598-018-21825-9"]}}