All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Engineering the cytokinin-glucoside specificity of the maize beta-d-glucosidase Zm-p60.1 using site-directed random mutagenesis.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F12%3A00177633" target="_blank" >RIV/62156489:43210/12:00177633 - isvavai.cz</a>

  • Alternative codes found

    RIV/68081707:_____/12:00440809

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.phytochem.2011.10.008" target="_blank" >http://dx.doi.org/10.1016/j.phytochem.2011.10.008</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.phytochem.2011.10.008" target="_blank" >10.1016/j.phytochem.2011.10.008</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Engineering the cytokinin-glucoside specificity of the maize beta-d-glucosidase Zm-p60.1 using site-directed random mutagenesis.

  • Original language description

    The maize beta-d-glucosidase Zm-p60.1 releases active cytokinins from their storage/transport forms, and its over-expression in tobacco disrupts zeatin metabolism. The role of the active-site microenvironment in fine-tuning Zm-p60.1 substrate specificityhas been explored, particularly in the W373K mutant, using site-directed random mutagenesis to investigate the influence of amino acid changes around the 373 position. Two triple (P372T/W373K/M376L and P372S/W373K/M376L) and three double mutants (P372T/W373K, P372S/W373K and W373K/M376L) were prepared. Their catalytic parameters with two artificial substrates show tight interdependence between substrate catalysis and protein structure. P372T/W373K/M376L exhibited the most significant effect on naturalsubstrate specificity: the ratio of hydrolysis of cis-zeatin-O-beta-d-glucopyranoside versus the trans-zeatin-O-beta-d-glucopyranoside shifted from 1.3 in wild-type to 9.4 in favor of the cis- isomer. The P372T and M376L mutations in P372

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Phytochemistry

  • ISSN

    0031-9422

  • e-ISSN

  • Volume of the periodical

    74

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    40-48

  • UT code for WoS article

    300815700004

  • EID of the result in the Scopus database