Structure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from scytalidium thermophilum

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dc.authorid0000-0002-5689-8521en_US
dc.contributor.authorYüzügüllü, Yonca
dc.contributor.authorTrinh, Chi H.
dc.contributor.authorSmith, Mark A.
dc.contributor.authorPearson, Arwen R.
dc.contributor.authorPhillips, Simon E. V.
dc.contributor.authorSutay Kocabaş, Didem
dc.contributor.authorBakir, Ufuk
dc.date.accessioned2019-12-06T21:17:52Z
dc.date.available2019-12-06T21:17:52Z
dc.date.issued2013
dc.departmentKMÜ, Mühendislik Fakültesi, Gıda Mühendisliği Bölümüen_US
dc.descriptionWOS:000316742700010en_US
dc.descriptionPubMed: 23519415en_US
dc.description.abstractScytalidium thermophilum produces a catalase with phenol oxidase activity (CATPO) that catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds. A codon-optimized catpo gene was cloned and expressed in Escherichia coli. The crystal structures of native and recombinant S. thermophilum CATPO and two variants, H82N and V123F, were determined at resolutions of 2.7, 1.4, 1.5 and 1.9 angstrom, respectively. The structure of CATPO reveals a homotetramer with 698 residues per subunit and with strong structural similarity to Penicillium vitale catalase. The haem component is cis-hydroxychlorin -spirolactone, which is rotated 180 degrees with respect to small-subunit catalases. The haem-binding pocket contains two highly conserved water molecules on the distal side. The H82N mutation resulted in conversion of the native d-type haem to a b-type haem. Kinetic studies of the H82N and V123F mutants indicate that both activities are likely to be associated with the haem centre and suggest that the secondary oxidase activity may be a general feature of catalases in the absence of hydrogen peroxide.en_US
dc.description.sponsorshipMiddle East Technical UniversityMiddle East Technical University [BAP-08-11-DPT2002K120510]; OYP-DPTTurkiye Cumhuriyeti Kalkinma Bakanligi; Biotechnology and Biological Research CouncilBiotechnology and Biological Sciences Research Council (BBSRC); TUBITAKTurkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [IPDRFP-2219]en_US
dc.description.sponsorshipWe would like to thank the Middle East Technical University (BAP-08-11-DPT2002K120510), OYP-DPT, the Biotechnology and Biological Research Council for funding (MJM and SEVP) and TUBITAK (IPDRFP-2219). We are also grateful to Professor R. E. Sockett and Dr John Taylor (University of Nottingham) for providing vector pET28aTEV.en_US
dc.identifier.citationYüzügüllü, Y., Trinh, Chi H., Smith, Mark A., Pearson, Arwen R., Phillips, Simon E. V., Sutay Kocabaş, D., Bakir, U. (2013). Structure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from scytalidium thermophilum. Acta Crystallographica Section D-Structural Biology (2013). D69, 398-408.
dc.identifier.doi10.1107/S0907444912049001
dc.identifier.endpage408en_US
dc.identifier.issn2059-7983
dc.identifier.pmid23519415
dc.identifier.scopus2-s2.0-84875478084
dc.identifier.scopusqualityN/A
dc.identifier.startpage398en_US
dc.identifier.urihttps://dx.doi.org/10.1107/S0907444912049001
dc.identifier.urihttps://hdl.handle.net/11492/3202
dc.identifier.volume69en_US
dc.identifier.wosWOS:000316742700010
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Sceince
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorSutay Kocabaş, Didem
dc.language.isoen
dc.publisherInt Union Crystallographyen_US
dc.relation.journalActa Crystallographica Section D-Structural Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCatalasesen_US
dc.subjectPhenol Oxidasesen_US
dc.subjectScytalidium Thermophilumen_US
dc.subjectSite-Directed Mutagenesisen_US
dc.titleStructure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from scytalidium thermophilumen_US
dc.typeArticle

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