Project information
Functional architecture of an active site in a maize ß-glucosidase
- Project Identification
- GA203/02/0865
- Project Period
- 1/2002 - 12/2004
- Investor / Pogramme / Project type
-
Czech Science Foundation
- Standard Projects
- MU Faculty or unit
- Faculty of Science
- Cooperating Organization
-
Institute of Biophysics
- Responsible person prof. RNDr. Břetislav Brzobohatý, CSc.
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
2005
-
A new sensitive method for enzyme studies of rare glucosides
Biologia Plantarum Supplement to vol. 49, 2nd International Symposium Auxins and Cytokinins in Plant Development, year: 2005
2002
-
Folding of native and mutant maize beta-glucosidase in E. coli is facilitated by thioredoxin fusion.
European Journal of Biochemistry, year: 2002, volume: 269, edition: Supp. 1