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
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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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
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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
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