Critical F129 and L138 in loop III of bile salt hydrolase (BSH) in Lactobacillus plantarum B14 are essential for the catalytic activity and substrate specificity

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dc.authorid0000-0001-6906-5257en_US
dc.authorid0000-0003-2701-3250
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorÖnal, Cansu
dc.contributor.authorBa, Ndeye Mareme
dc.date.accessioned2021-06-23T19:50:44Z
dc.date.available2021-06-23T19:50:44Z
dc.date.issued2019
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractBile salt hydrolase (BSH) is a gut-bacterial enzyme that influences human health by altering the host fat digestion and cellular energy generation. BSH is essential for deconjugation of the glycine or taurine-conjugated bile salts in the small intestine of humans. Therefore, BSH may be a key microbiome target for the designing of new measures to control some diseases in humans. BSHs, a member of the N-terminal nucleophile (Ntn) hydrolase superfamily, exhibit higher variation in substrate specificity. The phenylalanine-129 (F129) and leucine-138 (L138) in loop III of BSH, thought to be responsible for substrate specificity, are partially conserved in this superfamily. In this study, the aromatic-hydrophobic F129 and aliphatic-hydrophobic L138 of C-terminally His-tagged BSH from Lactobacillus plantarum B14 (LbBSH) was substituted for aliphatic-hydrophobic isoleucine (I) and negatively charged polar glutamate (E) amino acid, respectively, by site-directed mutagenesis and characterized using an Escherichia coli BLR(DE3) expression system. Although both mutations resulted in an assembled and stable recombinant BSHs (rBSHs), they altered the catalytic activity and substrate specificity of rBSH. This is the first experimental finding which confirmed that F129 and L138 were critical amino acids for the catalytic activity and substrate specificity turnover of BSH.en_US
dc.identifier.doi10.1080/08905436.2019.1673172
dc.identifier.endpage337en_US
dc.identifier.issn0890-5436
dc.identifier.issn1532-4249
dc.identifier.issue4en_US
dc.identifier.scopus2-s2.0-85074820963en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage325en_US
dc.identifier.urihttps://doi.org/10.1080/08905436.2019.1673172
dc.identifier.urihttps://hdl.handle.net/20.500.12491/9849
dc.identifier.volume33en_US
dc.identifier.wosWOS:000494491700003en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorÖztürk, Mehmet
dc.institutionauthorBa, Ndeye Mareme
dc.language.isoenen_US
dc.publisherTaylor & Francis Incen_US
dc.relation.ispartofFood Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBile Salt Hydrolaseen_US
dc.subjectCatalytic Activityen_US
dc.subjectLactobacillus Plantarum B14en_US
dc.subjectSite-Directed Mutagenesisen_US
dc.subjectSubstrate Specificityen_US
dc.titleCritical F129 and L138 in loop III of bile salt hydrolase (BSH) in Lactobacillus plantarum B14 are essential for the catalytic activity and substrate specificityen_US
dc.typeArticleen_US

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