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Identification and characterization of camptothecin tailoring enzymes in Nothapodytes tomentosa

Journal of Integrative Plant Biology 2024年第6期66卷 1158-1169页

作者： Yin Chen Jian-Ping Huang Yong-Jiang Wang Meng-Ling Tu Junheng Li Bingyan Xu Guoqing Peng Jing Yang Sheng-Xiong Huang State Key Laboratory of Phytochemistry and Plant Resources in West China and Yunnan Key Laboratory of Natural Medicinal Chemistry Kunming Institute of BotanyChinese Academy of SciencesKunming 650201China University of Chinese Academy of Sciences Beijing 100049China Key Laboratory for Economic Plants and Biotechnology Kunming Institute of BotanyChinese Academy of SciencesKunming 650201China

Camptothecin is a complex monoterpenoid indole alkaloid with remarkable antitumor *** that two C-10 modified camptothecin derivatives,topotecan and irinotecan,have been approved as potent anticancer agents,there is a critical need for methods to access other aromatic ringfunctionalized congeners(e.g.,C-9,C-10,etc.).However,contemporary methods for chemical oxidation are generally harsh and low-yielding when applied to the camptothecin scaffold,thereby limiting the development of modified *** herein,we have identified four tailoring enzymes responsible for C-9 modifications of camptothecin from Nothapodytes tomentosa,via metabolomic and transcriptomic *** consist of a cytochrome P450(Nt CPT9H)which catalyzes the regioselective oxidation of camptothecin to 9-hydroxycamptothecin,as well as two methyltransferases(Nt OMT1/2,converting 9-hydroxycamptothecin to 9-methoxycamptothecin),and a uridine diphosphate-glycosyltransferase(Nt UGT5,decorating 9-hydroxycamptothecin to9-β-D-glucosyloxycamptothecin).Importantly,the critical residues that contribute to the specific catalytic activity of Nt CPT9H have been elucidated through molecular docking and mutagenesis *** work provides a genetic basis for producing camptothecin derivatives through metabolic *** will hasten the discovery of novel C-9 modified camptothecin derivatives,with profound implications for pharmaceutical manufacture.

关键词： camptothecin biosynthesis enzymatic assay Nothapodytes tomentosa tailoring enzyme transcriptomic analysis

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Molecular cloning and functional identification of sterol C24-methyltransferase gene from Tripterygium wilfordii

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Acta Pharmaceutica Sinica B 2017年第5期7卷 603-609页

作者： Hongyu Guan Yujun Zhao Ping Su Yuru Tong Yujia Liu Tianyuan Hu Yifeng Zhang Xianan Zhang Jia Li Xiaoyi Wu Luqi Huang Wei Gao School of Traditional Chinese Medicine Capital Medical University State Key Laboratory Breeding Base of Dao-di Herbs National Resource Center for Chinese Materia Medica China Academy of Chinese Medical Sciences Beijing University of Chinese Medicine Third Affiliated Hospital

Sterol C24-methyltransferase(SMT) plays multiple important roles in plant growth and development. SMT1, which belongs to the family of transferases and transforms cycloartenol into 24-methylene cycloartenol, is involved in the biosynthesis of 24-methyl sterols. Here, we report the cloning and characterization of a cDNA encoding a sterol C24-methyltransferase from Tripterygium wilfordii(Tw SMT1). Tw SMT1(Gen Bank access number KU885950) is a 1530 bp cDNA with a 1041 bp open reading frame predicted to encode a 346-amino acid, 38.62 k Da protein. The polypeptide encoded by the SMT1 cDNA was expressed and purified as a recombinant protein from Escherichia coli(E. coli) and showed SMT activity. The expression of Tw SMT1 was highly up-regulated in T. wilfordii cell suspension cultures treated with methyl jasmonate(Me JA). Tissue expression pattern analysis showed higher expression in the phellem layer compared to the other four organs(leaf, stem, xylem and phloem), which is about ten times that of the lowest expression in leaf. The results are meaningful for the study of sterolbiosynthesis of T. wilfordii and will further lay the foundations for the research in regulating both the content of other main compounds and growth and development of T. wilfordii.

关键词： Cloning Cycloartenol C24-methyl transferase enzymatic assay Inducible expression Tissue expression

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LCAT酶学测定法方法学探讨

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重庆医科大学学报 1987年第2期 122-124页

作者：石小英徐葆元重庆医科大学第二医院内科重庆医科大学第二医院内科研究生

我们参照Nagasaki的卵磷脂胆固醇酰基转移酶(LCAT)活性测定法,以自身血清加入二软脂酰卵磷脂(DL)为底物,应用国产,酶试剂进行LCAT活性测定,并对方法学,特别是游离胆固醇显色反应进行了摸索。此方法具有两酶用量小,重复性好,操作简便的特... 详细信息

我们参照Nagasaki的卵磷脂胆固醇酰基转移酶(LCAT)活性测定法,以自身血清加入二软脂酰卵磷脂(DL)为底物,应用国产,酶试剂进行LCAT活性测定,并对方法学,特别是游离胆固醇显色反应进行了摸索。此方法具有两酶用量小,重复性好,操作简便的特点,适用于临床及实验室工作。

关键词： LCAT enzymatic assay

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