LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 2 of total 2

Search options

  1. Article ; Online: Editorial: Innate immunity against intracellular bacteria: mechanisms and strategies.

    Tian, Jingfei / Liu, Han / Che, Jingai / Song, Lei

    Frontiers in immunology

    2024  Volume 15, Page(s) 1396114

    MeSH term(s) Immunity, Innate ; Inflammasomes ; Bacteria
    Chemical Substances Inflammasomes
    Language English
    Publishing date 2024-03-20
    Publishing country Switzerland
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2024.1396114
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article: [Effect of mutating subsite -7 on product specificity of cyclodextrin glucanotransferase from alkalophilic Bacillus clarkii].

    Yang, Dong / Tian, Jingfei / Chen, Sheng / Wu, Jing

    Sheng wu gong cheng xue bao = Chinese journal of biotechnology

    2012  Volume 28, Issue 2, Page(s) 191–202

    Abstract: To investigate the mechanism of high product specificity of gamma-clodextrin glucanotransferase (CGTase) from alkalophilic Bacillus clarkii 7364, we aligned protein sequence and structure model, found out that loss of 6 amino acids at subsite -7 probably ...

    Abstract To investigate the mechanism of high product specificity of gamma-clodextrin glucanotransferase (CGTase) from alkalophilic Bacillus clarkii 7364, we aligned protein sequence and structure model, found out that loss of 6 amino acids at subsite -7 probably affected its product specificity. Using overlapping PCR method, we inserted 6 amino acids into subsite -7 of CGTase. The mutant CGTase gene was ligated with pET-20b (+) and expressed in Escherichia coli BL21 (DE3). The extracellular recombinant enzyme was used to transform soluble starch into cyclodextrins (CDs). HPLC analysis results show that, compared to wild CGTase, the gamma-CDs produced by mutant enzyme decreased from 76.0% to 12.5%, whereas the ratio of alpha- and beta-CDs increased from 8.7% and 15.2% to 37.5% and 50%. The possible mechanism was that, compared to alpha-, beta-CGTase, wild gamma-CGTase lacks 6 amino acids in its subsite -7. This conformation provided more space for glucose combination and was thus advantageous for forming gamma-CD. When the 6 amino acids were inserted into the subsite -7 of wild gamma-CGTase, the space to bind with glucose reduced and consequently resulted in less gamma-CD production.
    MeSH term(s) Bacillus/enzymology ; Bacillus/genetics ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Glucosyltransferases/biosynthesis ; Glucosyltransferases/genetics ; Mutant Proteins/biosynthesis ; Mutant Proteins/genetics ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics
    Chemical Substances Mutant Proteins ; Recombinant Proteins ; Glucosyltransferases (EC 2.4.1.-) ; cyclomaltodextrin glucanotransferase (EC 2.4.1.19)
    Language Chinese
    Publishing date 2012-02
    Publishing country China
    Document type English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1042206-7
    ISSN 1000-3061 ; 1042-749X
    ISSN 1000-3061 ; 1042-749X
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top