• 中文核心期刊
  • CSCD来源期刊
  • 中国科技核心期刊
  • CA、CABI、ZR收录期刊

Message Board

Respected readers, authors and reviewers, you can add comments to this page on any questions about the contribution, review,        editing and publication of this journal. We will give you an answer as soon as possible. Thank you for your support!

Name
E-mail
Phone
Title
Content
Verification Code
Volume 29 Issue 12
Dec.  2014
Turn off MathJax
Article Contents
KONG Xiang-rui, YANG Jun, WANG Rang-jian. A Bioinformatic Analysis on Caffeine Synthase in Plants[J]. Fujian Journal of Agricultural Sciences, 2014, 29(12): 1211-1218. doi: 10.19303/j.issn.1008-0384.2014.12.011
Citation: KONG Xiang-rui, YANG Jun, WANG Rang-jian. A Bioinformatic Analysis on Caffeine Synthase in Plants[J]. Fujian Journal of Agricultural Sciences, 2014, 29(12): 1211-1218. doi: 10.19303/j.issn.1008-0384.2014.12.011

A Bioinformatic Analysis on Caffeine Synthase in Plants

doi: 10.19303/j.issn.1008-0384.2014.12.011
  • Received Date: 2014-07-28
  • Publish Date: 2014-12-18
  • The amino acid sequences of caffeine synthase from Camellia sinensis, Theobroma cacao, Camellia japonica and other plants which were registered in GenBank, were analyzed and predicted by bioinformatic tools in subsequent aspects, including the isoelectric point, subcellular localization, signal peptide, transmembrane topologieal structure, conserved functional domain, motif, secondary structure and tertiary structure of protein.Resultsshowed that the caffeine synthase of plants which were located in cytoplasm and nuclei, and had phosphorylation, acylation, glycosylation sites could be divided into three different types based on gene sequences and conservative domains.Two of them, type I and type II protein, wereα-type soluble proteinases, and the secondary structure of type III proteinase was rich in random coil and has potential signal peptide, but they all did not have transmembrane helical structure.The result of tertiary structure prediction indicated that type I protein and type II protein were similar, they were all composed ofα-helix and horizontalβ-folded layers, but in the type III protein theα-helixes locateed in the lateral ends and were connected by verticalβ-folded layers.
  • loading
  • [1]
    周晨阳, 金基强, 姚明哲, 等.茶树等植物中嘌呤生物碱代谢研究进展[J].茶叶科学, 2011, 31 (2) :87-94.
    [2]
    ASHIHARA H, MONTEIRO A M, GILLIES F M, et al.Biosynthesis of caffeine in leaves of coffee[J].Plant Physiol, 1996, 111 (3) :747-753.
    [3]
    SCHULTHESS B H, MORATH P, BAUMANN T W.Caffeine biosynthesis starts with the metabolically channeled formation of 7-methyl-XMP-A new hypothesis[J].Phytochemistry, 1996, 41 (1) :169-175.
    [4]
    KATO M, KANEHARA T, SHIMIZU H, et al.Caffeine biosynthesis in young leaves of Camellia sinensis:in vitro studies on N-methyltransferase activity involved in the conversion of xanthosine to caffeine[J].Physiol Plantarum, 1996, 98 (3) :629-636.
    [5]
    NEGISHI O, OZAWA T, IMAGAWA H.Conversion of xanthosine into caffeine in tea plants[J].Agric Biol Chem, 1985, 49 (1) :251-253.
    [6]
    谭礼强, 齐桂年, 陈盛相, 等.植物中的咖啡碱:从合成途径研究到转基因作物[J].园艺学报, 2012, 39 (9) :1849-1858.
    [7]
    MALUF M P, SILVA C C, OLIVEIRA M P A, et al.Altered expression of the caffeine synthase gene in a naturally caffeinefree mutant of Coffea Arabica[J].Genet Mol Biol, 2009, 32 (4) :802-810.
    [8]
    KATO M, KITAO N, ISHIDA M, et al.Expression for caffeine biosynthesis and related enzymes in Camellia sinensis[J].Z Naturforsch C, 2010, 65 (3-4) :245-256.
    [9]
    冯艳飞, 梁月荣.茶树S-腺苷甲硫氨酸合成酶基因的克隆和序列分析[J].茶叶科学, 2001, 21 (1) :21-25.
    [10]
    YONEYAMA N, MORIMOTO H, YE C X, et al.Substrate specificity of N-methyltransferase involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme[J].Mol Genet Genomics, 2006, 275 (2) :125-135.
    [11]
    孔祥瑞.茶树候选功能基因电子克隆的可行性分析[J].分子植物育种, 2014, 12 (2) :332-337.
    [12]
    KUMAR S, DUDLEY J, NEI M, et al.MEGA:a biologistcentric software for evolutionary analysis of DNA and protein sequences[J].Briefings in bioinformatics, 2008, 9 (4) :299-306.
    [13]
    HALL T A.BioEdit:a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT[J].Nucl Acids Symp, 1999, 41:95-98.
    [14]
    TALAVERA G, CASTRESANA J.Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments[J].Systematic Biology, 2007, 56 (4) :564-577.
    [15]
    SIGRIST CJA, CERUTTI L, DE CASTRO E, et al.PROSITE, a protein domain database for functional characterization and annotation[J].Nucleic Acids Res, 2010, 38 (Database i) :161-166.
    [16]
    BENDTSEN J D, NIELSEN H, VON HEIJNE G, et al.Improved prediction of signal peptides:SignalP 3.0[J].J Mol Biol, 2004, 340 (4) :783-795.
    [17]
    BRIESEMEISTER S, BLUM T, BRADY S, et al.SherLoc2:a high-accuracy hybrid method for predicting subcellular localization of proteins[J]J.Proteome Res, 2009, 8 (11) :5363-5366.
    [18]
    GASTEIGER E, HOOGLAND C, GATTIKER A, et al.Protein identification and analysis tools on the ExPASy Server[M].In:John M, Walker. (Eds) The proteomics protocols handbook.Humana Press, 2005:571-607.
    [19]
    ANDERS K, BJORN L, GUNNAR VON H, et al.Predicting transmembrane protein topology with a hidden markov model:application to complete genomes[J].J Mol Biol, 2001, 305 (3) :567-580.
    [20]
    LUPAS A, VAN DYKE M, STOCK J.Predicting coiled coils from Protein sequences[J].Science, 1991, 252 (5009) :1162-1164.
    [21]
    CHENG J, RANDALL A, SWEREDOSKI M, et al.SCRATCH:a protein structure and structural feature prediction server[J].Nucleic Acids Res, 2005, 33 (Web Server) :72-76.
    [22]
    BIASINI M, BIENERT S, WATERHOUSE A, et al.SWISS-MODEL:modelling protein tertiary and quaternary structure using evolutionary information[J].Nucleic Acids Res, 2014, 42 (1) :252-258.
    [23]
    SCHWEDE T, KOPP J, GUEX N, et al.SWISS-MODEL:an automated protein homology-modeling server[J].Nucleic Acids Res, 2003, 31 (13) :3381-3385.
    [24]
    SWANEY D, PEDRO B, LEA S, et al.Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation[J].Nat Meth, 2013, 10 (7) :676-682.
    [25]
    YONEYAMA N, MORIMOTO H, YE C X, et al.Substrate specificity of N-methyl transferasc involved in purine alkaloids synthesis is dependent upon one amino acid residue of the enzyme[J].Mol Gen Genomics, 2006, 275 (2) :125-135.
  • 加载中

Catalog

    通讯作者: 陈斌, bchen63@163.com
    • 1. 

      沈阳化工大学材料科学与工程学院 沈阳 110142

    1. 本站搜索
    2. 百度学术搜索
    3. 万方数据库搜索
    4. CNKI搜索

    Article Metrics

    Article views (118) PDF downloads(0) Cited by()
    Proportional views
    Related

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return