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%2F01%3A00004635" target="_blank" >RIV/00216224:14310/01:00004635 - isvavai.cz</a>

Alternative codes found

RIV/68081707:_____/01:17013057

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 (Zea mays) 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 wild-type enzyme wassolved at 2.05-A resolution, allowing molecular docking analysis to be conducted. This indicated that the enzyme specificity 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. These aglycone-active site interactions recently were hypothesized to determine substrate specificity in inactive enzyme substrate complexes of ZM-Glu1, an allozyme of Zm-p60.1. Here, we test 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 toward substrates with an aromatic aglycone. It was unexpected

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

<a href="/en/project/VS96096" target="_blank" >VS96096: Laboratory of Molecular Plant Physiology</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2001

Confidentiality

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

Name of the periodical

Plant Physiology

ISSN

0032-0889

e-ISSN

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Volume of the periodical

127

Issue of the periodical within the volume

3

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

973

UT code for WoS article

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EID of the result in the Scopus database

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