Conserved amino acid residues that affect structural stability of candida boidinii formate dehydrogenase

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dc.authoridHuri Bulut / 0000-0003-2706-9625en_US
dc.authoridNazlı Kara / 0000-0002-6765-2543en_US
dc.authorscopusidHuri Bulut / 57185264300
dc.authorwosidNazlı Kara / DXM-3032-2022
dc.authorwosidHuri Bulut / AAM-1432-2020
dc.contributor.authorBulut, Huri
dc.contributor.authorYüksel, Büşra
dc.contributor.authorGül, Mehmet
dc.contributor.authorEren, Meryem
dc.contributor.authorKarataş, Ersin
dc.contributor.authorKara, Nazlı
dc.contributor.authorYılmazer, Berin
dc.contributor.authorKoçyiğit, Abdurrahim
dc.contributor.authorLabrou, Nikolaos E.
dc.contributor.authorBi?nay, Barış
dc.date.accessioned2020-10-02T08:05:13Z
dc.date.available2020-10-02T08:05:13Z
dc.date.issued2021
dc.departmentİstinye Üniversitesi, Tıp Fakültesi, Temel Tıp Bilimleri Bölümüen_US
dc.description.abstractThe NAD+-dependent formate dehydrogenase (FDH; EC 1.2.1.2) from Candida boidinii (CboFDH) has been extensively used in NAD(H)-dependent industrial biocatalysis as well as in the production of renewable fuels and chemicals from carbon dioxide. In the present work, the effect of amino acid residues Phe285, Gln287, and His311 on structural stability was investigated by site-directed mutagenesis. The wild-type and mutant enzymes (Gln287Glu, His311Gln, and Phe285Thr/His311Gln) were cloned and expressed in Escherichia coli. Circular dichroism (CD) spectroscopy was used to determine the effect of each mutation on thermostability. The results showed the decisive roles of Phe285, Gln287, and His311 on enhancing the enzyme’s thermostability. The melting temperatures for the wild-type and the mutant enzymes Gln287Glu, His311Gln, and Phe285Thr/His311Gln were 64, 70, 77, and 73 °C, respectively. The effects of pH and temperature on catalytic activity of the wild-type and mutant enzymes were also investigated. Interestingly, the mutant enzyme His311Gln exhibits a large shift of pH optimum at the basic pH range (1 pH unit) and substantial increase of the optimum temperature (25 °C). The present work supports the multifunctional role of the conserved residues Phe285, Gln287, and His311 and further underlines their pivotal roles as targets in protein engineering studies.en_US
dc.identifier.citationBulut, H., Yuksel, B., Gul, M., Eren, M., Karatas, E., Kara, N., ... & Binay, B. (2020). Conserved Amino Acid Residues that Affect Structural Stability of Candida boidinii Formate Dehydrogenase. Applied Biochemistry and Biotechnology, 1-14.en_US
dc.identifier.doi10.1007/s12010-020-03429-0en_US
dc.identifier.issn0273-2289en_US
dc.identifier.pmid32974869en_US
dc.identifier.scopus2-s2.0-85091498245en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.urihttps://doi.org/10.1007/s12010-020-03429-0
dc.identifier.urihttps://hdl.handle.net/20.500.12713/1126
dc.identifier.wosWOS:000572586600001en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.institutionauthorBulut, Huri
dc.institutionauthorKara, Nazlı
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofApplied Biochemistry and Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCandida Boidiniien_US
dc.subjectFormate Dehydrogenaseen_US
dc.subjectMolecular Modelingen_US
dc.subjectSite-directed Mutagenesisen_US
dc.subjectThermostabilityen_US
dc.titleConserved amino acid residues that affect structural stability of candida boidinii formate dehydrogenaseen_US
dc.typeArticleen_US

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