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Molecular and in silico cloning, identification, and preharvest period expression analysis of a putative cytochrome P450 monooxygenase gene from Camellia sinensis (L.) Kuntze (tea)

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Cytochrome P450 monooxygenases are one of the largest heme-containing protein groups, and the majority of them catalyze hydroxylation reactions dependent on nicotinamide adenine dinucleotide phosphate and oxygen. | Turkish Journal of Biology Turk J Biol (2018) 42: 1-11 © TÜBİTAK doi:10.3906/biy-1606-54 http://journals.tubitak.gov.tr/biology/ Research Article Molecular and in silico cloning, identification, and preharvest period expression analysis of a putative cytochrome P450 monooxygenase gene from Camellia sinensis (L.) Kuntze (tea) 1, 1 1 2 3 Ayşenur EMİNOĞLU *, Yeşim AKTÜRK DİZMAN , Şule GÜZEL , Ali Osman BELDÜZ Molecular Biology Research Laboratories, Department of Biology, Recep Tayyip Erdoğan University, Rize, Turkey 2 Plant Ecology Research Laboratories, Department of Biology, Recep Tayyip Erdoğan University, Rize, Turkey 3 Department of Biology, Faculty of Science, Karadeniz Technical University, Trabzon, Turkey Received: 17.06.2016 Accepted/Published Online: 01.11.2016 Final Version: 15.02.2018 Abstract: Cytochrome P450 monooxygenases are one of the largest heme-containing protein groups, and the majority of them catalyze hydroxylation reactions dependent on nicotinamide adenine dinucleotide phosphate and oxygen. Cytochrome P450 (CYP) enzymes function in a wide range of monooxygenation reactions essential in primary and secondary metabolism in plants. Camellia sinensis (L.) Kuntze is a commercially and economically valuable plant due to its medicinally important secondary metabolites and as a beloved beverage. Cytochrome P450 monooxygenases play a significant role in the biosynthesis of a variety of secondary metabolites in tea. Although the biosynthesis of secondary metabolites has been investigated in detail, there have been limited studies conducted on identifying the genetic mechanisms of CYP-catalyzed secondary metabolic pathways in the C. sinensis (tea) plant. In our study, we characterized a putative C. sinensis (L.) Kuntze cytochrome P450 monooxygenase gene (Csp450), which has 1759 bp full-length cDNA with 49 bp of 5ʹ and 183 bp of 3ʹ untranslated regions. The CDS of the gene is 1527 bp and 508 amino acids in length. BLAST results of the deduced

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