In silico identification and structure function analysis of a putative coclaurine N-methyltransferase from Aristolochia fimbriata

doi:10.1016/j.compbiolchem.2020.107201

	In silico identification and structure function analysis of a putative coclaurine N-methyltransferase from Aristolochia fimbriata
	Ali, Roshan 1; Jiao, Yuannian2 ; Wall, P. Kerr ; Patching, Simon G.; Ahmad, Irshad 1; Lutfulla, Ghosia 5; dePamphilis, Claude W.
	2020
发表期刊	COMPUTATIONAL BIOLOGY AND CHEMISTRY
ISSN	1476-9271
卷号	85
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.
关键词	Coclaurine N-methyltransferase Aristolochia fimbriata Basal angiosperm Aristolochic acid Reaction mechanism Homology model
学科领域	Biology ; Computer Science, Interdisciplinary Applications
DOI	10.1016/j.compbiolchem.2020.107201
收录类别	SCI
语种	英语
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
WOS记录号	WOS:000528339900005
出版者	ELSEVIER SCI LTD
文献子类	Article
出版地	OXFORD
EISSN	1476-928X
资助机构	Higher Education Commission of PakistanHigher Education Commission of Pakistan
作者邮箱	roshanali.ibms@kmu.edu.pk ; s.g.patching@leeds.ac.uk
引用统计	被引频次：1[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.ibcas.ac.cn/handle/2S10CLM1/21793
专题	系统与进化植物学国家重点实验室
作者单位	1.[Ali, Roshan; Jiao, Yuannian; Wall, P. Kerr; dePamphilis, Claude W.] Penn State Univ, Dept Biol, Life Sci Bldg, University Pk, PA 16802 USA 2.Khyber Med Univ, Inst Basic Med Sci, Dept Mol Biol & Genet, Peshawar, Pakistan 3.Chinese Acad Sci, Inst Bot, Beijing, Peoples R China 4.Patching, Simon G.] Univ Leeds, Sch Biomed Sci, Leeds, W Yorkshire, England 5.Patching, Simon G.] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds, W Yorkshire, England 6.Univ Peshawar, Ctr Biotechnol & Microbiol, Peshawar, Pakistan
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).

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