Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F02%3A00007120" target="_blank" >RIV/00216224:14310/02:00007120 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1
Original language description
The maize beta-glucosidase Zm-p60.1 has been implicated in regulation of plant development by the targeted release of free cytokinins from cytokinin-O-glucosides, their inactive storage forms. The crystal structure of the enzyme indicated that the enzymespecificity toward substrates with aryl aglycones is determined by aglycone aromatic system stacking with W373, and interactions with edges of F193, F200 and F461 located opposite W373 in a slot-like aglycone-binding site. Recently, these aglycone-active-site interactions were hypothesized to determine substrate specificity in inactive enzyme-substrate complexes of ZMGlu1, an allozyme of Zm-p60.1. We tested this hypothesis by kinetic analysis of F193I/Y/W mutants. The decreased Km of all mutants confirmed the involvement of F193 in determining enzyme affinity towards substrates with an aromatic aglycone. Unexpectedly, a 30-fold decrease in kcat was found in F193I mutant compared to the wild type. Kinetic analysis and computer modeling
Czech name
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Czech description
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Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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