Asparagine 79 is an important amino acid for catalytic activity and substrate specificity of bile salt hydrolase (BSH)

Basit Öğe Kaydı
dc.authorid0000-0001-6906-5257en_US
dc.authorid0000-0003-2701-3250
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorÖnal, Cansu
dc.date.accessioned2021-06-23T19:51:12Z
dc.date.available2021-06-23T19:51:12Z
dc.date.issued2019
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractMicrobial bile salt hydrolases (BSHs), a member of cholylglycine hydrolase (CGH) family, catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of human. BSH is evolutionarily related to penicillin V acylase (PVA) which hydrolyses a penicillin V and is also a member of CGH family. Although, five of the six amino acids, C2, R16, D19, N170, N79 and R223, supposed to be responsible for catalytic activity of BSH enzyme, are strictly conserved in all CGH family members, N79 is partially conserved in this family. In this study, in order to analyze the correlation between N79 and catalytic activity or substrate specificity of BSH, the polar and acidic N79 was substituted for the aliphatic and hydrophobic V79 by PCR-based site directed mutagenesis and mutant recombinant BSH was expressed in E. coli BLR(DE3). While the effects of the mutation on catalytic activity and substrate specificity of BSH were detected by ninhydrin assay. The effect of this mutation on the stability of the BSH was observed by SDS-PAGE analysis. Although V79 mutation resulted in stable BSH, it reduced the catalytic activity and altered substrate specificity of BSH. The results suggested that N79 might be important for substrate binding and catalytic turnover of BSH.en_US
dc.identifier.doi10.1007/s11033-019-04889-2
dc.identifier.endpage4368en_US
dc.identifier.issn0301-4851
dc.identifier.issn1573-4978
dc.identifier.issue4en_US
dc.identifier.pmid31154605en_US
dc.identifier.scopus2-s2.0-85066619566en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage4361en_US
dc.identifier.urihttps://doi.org/10.1007/s11033-019-04889-2
dc.identifier.urihttps://hdl.handle.net/20.500.12491/9944
dc.identifier.volume46en_US
dc.identifier.wosWOS:000478684300069en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorÖztürk, Mehmet
dc.institutionauthorÖnal, Cansu
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofMolecular Biology Reportsen_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.subjectHuman Bile Acidsen_US
dc.subjectLactobacillus Plantarum B14en_US
dc.subjectProbioticsen_US
dc.subjectSubstrate Specificityen_US
dc.titleAsparagine 79 is an important amino acid for catalytic activity and substrate specificity of bile salt hydrolase (BSH)en_US
dc.typeArticleen_US

Dosyalar

Orijinal paket
Listeleniyor 1 - 1 / 1
Küçük Resim Yok
İsim:
mehmet-ozturk.pdf
Boyut:
2.33 MB
Biçim:
Adobe Portable Document Format
Açıklama:
Tam Metin/Full Text
İndir

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
Biyoloji Bölümü Koleksiyonu
PubMed İndeksli Yayınlar Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu