In silico identification and structure function analysis of a putative coclaurine N-methyltransferase from Aristolochia fimbriata
文献类型：期刊论文
| 作者 | Ali, Roshan4; Jiao, Yuannian5 ; Wall, P. Kerr; Patching, Simon G.; Ahmad, Irshad4; Lutfulla, Ghosia3; dePamphilis, Claude W.
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| 刊名 | COMPUTATIONAL BIOLOGY AND CHEMISTRY
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| 出版日期 | 2020 |
| 卷号 | 85 |
| 关键词 | Coclaurine N-methyltransferase Aristolochia fimbriata Basal angiosperm Aristolochic acid Reaction mechanism Homology model |
| ISSN号 | 1476-9271 |
| DOI | 10.1016/j.compbiolchem.2020.107201 |
| 文献子类 | Article |
| 英文摘要 | In this study we isolated and performed in silico analysis of a putative coclaurine N-methyltransferase (CNMT) from the basal angiosperm Aristolochia fimbriata. The Aristolochiaceae plant family produces alkaloids similar to the Papavaraceae family, and CNMTs are central enzymes in biosynthesis pathways producing compounds of ethnopharmacological interest. We used bioinformatics and computational tools to predict a three-dimensional homology model and to investigate the putative function of the protein and its mechanism for methylation. The putative CNMT is a unique (S)-adenosyl-L-methionine (SAM)-dependent N-methyltransferase, catalyzing transfer of a methyl group from SAM to the amino group of coclaurine. The model revealed a mixed alpha/beta structure comprising seven twisted beta-strands surrounded by twelve alpha-helices. Sequence comparisons and the model indicate an N-terminal catalytic Core domain and a C-terminal domain, of which the latter forms a pocket for coclaurine. An additional binding pocket for SAM is connected to the coclaurine binding pocket by a small opening. CNMT activity is proposed to follow an S(N)2-type mechanism as observed for a similarly conformed enzyme. Residues predicted for the methyl transfer reaction are Tyr79 and Glu96, which are conserved in the sequence from A. fimbriata and in homologous N-methyltransferases. The isolated CNMT is the first to be investigated from any basal angiosperm. |
| 学科主题 | Biology ; Computer Science, Interdisciplinary Applications |
| 出版地 | OXFORD |
| 电子版国际标准刊号 | 1476-928X |
| WOS关键词 | CRYSTAL-STRUCTURE ; S-ADENOSYLHOMOCYSTEINE ; SUBSTRATE RECOGNITION ; RNA METHYLTRANSFERASE ; WEB SERVER ; ACID ; BIOSYNTHESIS ; PROTEINS ; DOMAIN ; DATABASE |
| WOS研究方向 | Life Sciences & Biomedicine - Other Topics ; Computer Science |
| 语种 | 英语 |
| WOS记录号 | WOS:000528339900005 |
| 出版者 | ELSEVIER SCI LTD |
| 资助机构 | Higher Education Commission of PakistanHigher Education Commission of Pakistan |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/21793]  |
| 专题 | 植物研究所_系统与进化植物学研究中心_系统与进化植物学研究中心_学位论文 |
| 作者单位 | 1.Patching, Simon G.] Univ Leeds, Sch Biomed Sci, Leeds, W Yorkshire, England 2.Univ Peshawar, Ctr Biotechnol & Microbiol, Peshawar, Pakistan 3.Patching, Simon G.] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds, W Yorkshire, England 4.[Ali, Roshan; Jiao, Yuannian; Wall, P. Kerr; dePamphilis, Claude W.] Penn State Univ, Dept Biol, Life Sci Bldg, University Pk, PA 16802 USA 5.Khyber Med Univ, Inst Basic Med Sci, Dept Mol Biol & Genet, Peshawar, Pakistan 6.Chinese Acad Sci, Inst Bot, Beijing, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ali, Roshan,Jiao, Yuannian,Wall, P. Kerr,et al. In silico identification and structure function analysis of a putative coclaurine N-methyltransferase from Aristolochia fimbriata[J]. COMPUTATIONAL BIOLOGY AND CHEMISTRY,2020,85. |
| APA | Ali, Roshan.,Jiao, Yuannian.,Wall, P. Kerr.,Patching, Simon G..,Ahmad, Irshad.,...&dePamphilis, Claude W..(2020).In silico identification and structure function analysis of a putative coclaurine N-methyltransferase from Aristolochia fimbriata.COMPUTATIONAL BIOLOGY AND CHEMISTRY,85. |
| MLA | Ali, Roshan,et al."In silico identification and structure function analysis of a putative coclaurine N-methyltransferase from Aristolochia fimbriata".COMPUTATIONAL BIOLOGY AND CHEMISTRY 85(2020). |
入库方式： OAI收割
来源：植物研究所
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