Project information

Functional architecture of an active site in a maize ß-glucosidase

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Project Identification
GA203/02/0865
Project Period
1/2002 - 12/2004
Investor / Pogramme / Project type
Czech Science Foundation
MU Faculty or unit
Faculty of Science
Cooperating Organization
Institute of Biophysics

In (-glucosidases, a substantial progress has been achieved in understanding the mechanism of glucoside bond cleavage, and two glutamic acid residues directly involved in the cleavage have been identified. However, only very recently the first residues involved in molecular determination of aglycone specificity in (-glucosidases were identified. Yet, given the tremendous diversity of aglycone moieties in natural glucosides which reflects their numerous biological functions, fine-tuning of diverse biological processes in plants relies, among others, on well defined specificity of a number of (-glucosidases towards their respective aglycones. Elucidation of aglycone specificity in (-glucosidases is a key prerequisite towards uncovering the exact role(s) of (-glucosidases in biological processes that involve glucosylation and de-glucosylation as regulatory steps. Simultaneously, the ability to modulate specificity in (-glucosidases holds considerable promise in terms of biotechnological applicati

Publications

Total number of publications: 2


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