Molecular Characterization of Cinnamate 4-Hydroxylase gene in Red Hot Pepper (Capsicum annuum L.)
2005
Kim, K.W. (National Institute of Agricultural Biotechnology, RDA, Suwon, Republic of Korea) | Kim, E.J. (Jinju National University, Jinju, Republic of Korea) | Kim, J.G. (Kyungpook National University, Daegu, Republic of Korea) | Ha, S.H. (National Institute of Agricultural Biotechnology, RDA, Suwon, Republic of Korea) | Cho, K.J. (National Institute of Agricultural Biotechnology, RDA, Suwon, Republic of Korea) | Lee, S.W. (National Institute of Agricultural Biotechnology, RDA, Suwon, Republic of Korea), E-mail: shinwlee@jinju.ac.kr | Lee, M.K. (Jinju National University, Jinju, Republic of Korea) | Yu, J.J. (Jinju National University, Jinju, Republic of Korea)
Three different cDNAs for cinnamate 4-hydroxylase (C4H) which are involved in the second step of the general phenylpropanoid pathway were isolated and designated as pc4h1 (1,755 bp), pc4h2 (1,655 bp), and pc4h3 (1,316 bp), respectively. The nucleotide sequence analysis revealed that both pc4h1 and pc4h2 clones encode polypeptides of 505 amino acids frame but pc4h3 clone was truncated at the 5'-end of coding region. The alignment of the deduced amino acid sequences showed that PC4H1 and PC4H2 are highly homologous (95.8 identical) with each other and contain three conserved domains which are typical in cytochrome p450 monooxygenase: proline-rich region, threonine-containing binding pocket for the oxygen molecule, and heme binding region.
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