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

CHEN Liang, LI Qing, CHEN Junfeng, FENG Jingxian, ZHANG Lei, CHEN Wansheng. Bioinformatics analysis of laccases involved in active lignans' biosynthesis in Isatis indigotica[J]. Journal of Pharmaceutical Practice and Service, 2017, 35(3): 208-214. doi: 10.3969/j.issn.1006-0111.2017.03.005
Citation: CHEN Liang, LI Qing, CHEN Junfeng, FENG Jingxian, ZHANG Lei, CHEN Wansheng. Bioinformatics analysis of laccases involved in active lignans' biosynthesis in Isatis indigotica[J]. Journal of Pharmaceutical Practice and Service, 2017, 35(3): 208-214. doi: 10.3969/j.issn.1006-0111.2017.03.005

Bioinformatics analysis of laccases involved in active lignans' biosynthesis in Isatis indigotica

doi: 10.3969/j.issn.1006-0111.2017.03.005
  • Received Date: 2017-02-21
  • Rev Recd Date: 2017-04-15
  • Objective Identifying laccases, as one of the key synthetases in the lariciresinol biosynthetic pathway, by analyzing the transcriptome sequencing results in Isatis indigotica would provide a dependable foundation for later functional study of Isatis indigotica's laccases. Methods Bioinformatical softwares and kinds of analytical methods online were used to find out the characteristics of the laccases from I. indigotica, including physical and chemical properties, homology, and the properties after induction of MeJA. Results The transcriptional results showed that Iilac3 and Iilac5 from I. indigotica were corresponded with the accumulation of the effective metabolites, making them the potential functional genes participated in lariciresinol synthesis. Conclusion Through the detailed bioinformatical analysis of Iilacs,which laid a solid foundation for the further study of the physiological and biochemical mechanisms and structural characteristics of the functional proteins.
  • [1] 国家药典委员会. 中华人民共和国药典2015版一部[S]. 北京:中国医药科技出版社,2015:205-206.
    [2] 李 彬. 板蓝根活性成分及品质评价[D]. 上海:第二军医大学, 2003.
    [3] Satake H, Ono E, Murata J. Recent advances in the metabolic engineering of lignan biosynthesis pathways for the production of transgenic plant-based foods and supplements[J]. J Agr Food Chem,2013, 61(48): 11721-11729.
    [4] Yang Z, Wang Y, Zheng Z, et al. Antiviral activity of Isatis indigotica root-derived clemastanin B against human and avian influenza A and B viruses in vitro[J]. Int J Mol Med, 2013, 31(4): 867-873.
    [5] Nakatsubo T, Mizutani M, Suzuki S, et al. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis[J]. J Biol Chem,2008, 283(23): 15550-15557.
    [6] Davin LB, Lewis NG. Dirigent proteins and dirigent sites explain the mystery of specificity of radical precursor coupling in lignan and lignin biosynthesis[J]. Plant Physiol,2000, 123(2): 453-462.
    [7] Bao W, O'Malley DM, Whetten R, et al. A laccase associated with lignification in loblolly pine xylem[J]. Science,1993, 260(5108): 672-674.
    [8] Wang GD, Li QJ, Luo B, et al. Ex planta phytoremediation of trichlorophenol and phenolic allelochemicals via an engineered secretory laccase[J]. Nat Biotechnol,2004,22(7):893-897.
    [9] Chen J, Dong X, Li Q, et al. Biosynthesis of the active compounds of Isatis indigotica based on transcriptome sequencing and metabolites profiling[J]. BMC Genomics,2013, 14(1): 857.
    [10] Berthet S, Demont-Caulet N, Pollet B, et al. Disruption of LACCASE 4 and 17 results in tissue-specific alterations to lignification of Arabidopsis thaliana stems[J]. Plant Cell,2011, 23(3): 1124-1137.
    [11] Zhao Q, Dixon RA. LACCASE is necessary and nonredundant with PEROXIDASE for lignin polymerization during vascular development in Arabidopsis[J]. Plant Cell,2013, 25(10): 3976-3987.
    [12] Cai X, Davis EJ, Ballif J, et al. Mutant identification and characterization of the laccase gene family in Arabidopsis[J]. J Exp Bot,2006, 57(11): 2563-2569.
  • 加载中
通讯作者: 陈斌, [email protected]
  • 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(3771) PDF downloads(964) Cited by()

Related
Proportional views

Bioinformatics analysis of laccases involved in active lignans' biosynthesis in Isatis indigotica

doi: 10.3969/j.issn.1006-0111.2017.03.005

Abstract: Objective Identifying laccases, as one of the key synthetases in the lariciresinol biosynthetic pathway, by analyzing the transcriptome sequencing results in Isatis indigotica would provide a dependable foundation for later functional study of Isatis indigotica's laccases. Methods Bioinformatical softwares and kinds of analytical methods online were used to find out the characteristics of the laccases from I. indigotica, including physical and chemical properties, homology, and the properties after induction of MeJA. Results The transcriptional results showed that Iilac3 and Iilac5 from I. indigotica were corresponded with the accumulation of the effective metabolites, making them the potential functional genes participated in lariciresinol synthesis. Conclusion Through the detailed bioinformatical analysis of Iilacs,which laid a solid foundation for the further study of the physiological and biochemical mechanisms and structural characteristics of the functional proteins.

CHEN Liang, LI Qing, CHEN Junfeng, FENG Jingxian, ZHANG Lei, CHEN Wansheng. Bioinformatics analysis of laccases involved in active lignans' biosynthesis in Isatis indigotica[J]. Journal of Pharmaceutical Practice and Service, 2017, 35(3): 208-214. doi: 10.3969/j.issn.1006-0111.2017.03.005
Citation: CHEN Liang, LI Qing, CHEN Junfeng, FENG Jingxian, ZHANG Lei, CHEN Wansheng. Bioinformatics analysis of laccases involved in active lignans' biosynthesis in Isatis indigotica[J]. Journal of Pharmaceutical Practice and Service, 2017, 35(3): 208-214. doi: 10.3969/j.issn.1006-0111.2017.03.005
Reference (12)

Catalog

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return