Functional characterization of phenylalanine ammonia-lyase- and cinnamate 4-hydroxylase-encoding genes from Lycoris radiata, a galanthamine-producing plant
文献类型：期刊论文
| 作者 | Li, Wei2,3; Yang, Yun2,3; Qiao, Chong2,3; Zhang, Guolin2; Luo, Yinggang1,2 |
| 刊名 | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
 |
| 出版日期 | 2019-10-01 |
| 卷号 | 117期号:2018页码:1264-1279 |
| 关键词 | Lycoris radiata Galanthamine Phenylalanine ammonia-lyase Cinnamate 4-hydroxylase Biosynthesis |
| ISSN号 | 0141-8130 |
| DOI | 10.1016/j.ijbiomac.2018.06.046 |
| 产权排序 | 1 |
| 文献子类 | Article |
| 英文摘要 | Galanthamine (GAL), the well-known Amaryllidaceae alkaloid, is a clinically used drug for the treatment of Alzheimer's disease. L-Phenylalanine (Phe) and trans-cinnamic acid (CA) were enzymatically transformed into the catechol portion of GAL Herein, a Phe ammonia-lyase-encoding gene LrPAL3 and a cinnamate 4hydroxylase-encoding gene LrC4H were cloned from Lycoris radiata, a GAL-producing plant. LrPAL3 was overexpressed in Escherichia coli and purified to homogeneity. LrPAL3 catalyzes the forward deamination conversion of L-Phe into trans-CA. The 3-chloro- and 4-fluoro-L-Phe were deaminated to generate the corresponding 3-chloro- and 4-fluoro-trans-CA by LrPAL3. LrPAL3-catalyzed reverse hydroamination was confirmed by the conversion of trans-CA into L-Phe with exceptional regio- and stereo-selectivity. LrC4H was overexpressed in E. coli with tCamCPR, a cytochrome P450 reductase-encoding gene. LrC4H catalyzes the regioselective parahydroxylation on trans-CA to form p-coumaric acid. The transcriptional levels of both LrPAL3 and LrC4H were positively associated with the GAL contents within the leaves and flowers of L radiata, which suggested that their expression and function are co-regulated and involved in the biosynthesis of GAL The present investigations on the biosynthetic genes of GAL will promote the development of synthetic biology platforms for this kind of important drug via metabolic engineering. (C) 2018 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry ; Biophysics |
| URL标识 | 查看原文 |
| WOS关键词 | AMARYLLIDACEAE ALKALOIDS ; AMINO-ACIDS ; BIOSYNTHESIS ; MECHANISM ; ENZYME ; BINDING ; CYTOCHROME-P450 ; NORBELLADINE ; BIOCATALYSIS ; AMINOMUTASE |
| WOS研究方向 | Biochemistry & Molecular Biology ; Chemistry ; Polymer Science |
| 语种 | 英语 |
| WOS记录号 | WOS:000442057700144 |
| 出版者 | ELSEVIER SCIENCE BV |
| 源URL | [http://210.75.237.14/handle/351003/30148]  |
| 专题 | 国家天然药物工程技术研究中心_天然产物研究 |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, Shanghai 200032, Peoples R China; 2.Chinese Acad Sci, Chengdu Inst Biol, Ctr Nat Prod Res, 9 Sect 4,Renmin Rd South, Chengdu 610041, Sichuan, Peoples R China; 3.Univ Chinese Acad Sci, 19A Yuquan Rd, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, Wei,Yang, Yun,Qiao, Chong,et al. Functional characterization of phenylalanine ammonia-lyase- and cinnamate 4-hydroxylase-encoding genes from Lycoris radiata, a galanthamine-producing plant[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2019,117(2018):1264-1279. |
| APA | Li, Wei,Yang, Yun,Qiao, Chong,Zhang, Guolin,&Luo, Yinggang.(2019).Functional characterization of phenylalanine ammonia-lyase- and cinnamate 4-hydroxylase-encoding genes from Lycoris radiata, a galanthamine-producing plant.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,117(2018),1264-1279. |
| MLA | Li, Wei,et al."Functional characterization of phenylalanine ammonia-lyase- and cinnamate 4-hydroxylase-encoding genes from Lycoris radiata, a galanthamine-producing plant".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 117.2018(2019):1264-1279. |
入库方式： OAI收割
来源：成都生物研究所
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