Cloning, expression, and characterization of a novel CTP synthase gene from Anoxybacillus gonensis G2

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dc.authorid0000-0002-7757-6812en_US
dc.contributor.authorSandallı, Cemal
dc.contributor.authorSaral, Ayşegül
dc.contributor.authorÜlker, Serdar
dc.contributor.authorKaraoğlu, Hakan
dc.contributor.authorBelduz, Ali Osman
dc.contributor.authorÇopur Çiçek, Ayşegül
dc.date.accessioned2021-10-27T06:50:38Z
dc.date.available2021-10-27T06:50:38Z
dc.date.issued2014
dc.departmentAÇÜ, Sağlık Bilimleri Fakültesi, Beslenme ve Diyetetik Bölümüen_US
dc.descriptionThis work was supported by Recep Tayyip Erdogan University Research Fund Grants BAP-2009.102.03.2 and BAP-2011.102.03.3.en_US
dc.description.abstractThe cytidine-5'-triphosphate (CTP) synthase (EC 6.4.3.2) gene (pyrG) was cloned and sequenced from the thermophilic bacterium Anoxybacillus gonensis G2 (Ago). The gene is 1590 bp in length and encodes a protein of 530 amino acids, with a molecular mass of 59.5 kDa. The amino acid sequence of CTP synthase shares approximately 90%-94% similarity to Bacillus sp., and it belongs to the triad glutamine amidotransferases, which utilize a Cys-His-Glu triad for activity. Multiple sequence alignments revealed that the enzyme includes conserved amino acids responsible for catalytic activity and the binding of a divalent metal ion (Mg+2). AgoCTP synthase (AgoG2CTPs) was overproduced in Escherichia coli BL21 (DE3) pLysS as recombinant and purified by nickel affinity chromatography. Its biochemical characterization showed that the enzyme had maximal activity at pH 9.0-10.0 and 65 degrees C. K-m, V-max, and k(cat) were found to be approximately 12.415 mM, 0.381 U/L, and 0.762 s(-1) at 65 degrees C, respectively. CTP synthase promotes the formation of CTP in dividing cells and is a recognized target for anticancer and antibacterial drugs. The results obtained from this study can be improved upon with the use of different species and substrates.
dc.identifier.citationSandallı, C., Saral, A., Ülker, S., Karaoğlu, H., Beldüz, A. O., & Çiçek, A. Ç. (2014). Cloning, expression, and characterization of a novel CTP synthase gene from Anoxybacillus gonensis G2. Turkish Journal of Biology, 38(1), 111-117.en_US
dc.identifier.doi10.3906/biy-1304-76
dc.identifier.endpage117en_US
dc.identifier.issue1en_US
dc.identifier.scopusqualityQ1
dc.identifier.startpage111en_US
dc.identifier.urihttps://hdl.handle.net/11494/3549
dc.identifier.volume38en_US
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.institutionauthorSaral, Ayşegül
dc.language.isoenen_US
dc.publisherTUBITAK Scientific & Technical Research Council Turkeyen_US
dc.relation.ispartofTurkish Journal of Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAnoxybacillus gonensisen_US
dc.subjectCytidine 5 '-triphosphate synthaseen_US
dc.subjectthermophilicen_US
dc.subjectNH3-dependent characterizationen_US
dc.titleCloning, expression, and characterization of a novel CTP synthase gene from Anoxybacillus gonensis G2en_US
dc.typeArticle

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