Cellulomonas fimi beta -1,4-glycanase Cex The catalytic domain from Cex (cex-cd) is in many ways a prototype for the retaining beta-1,4-glycanase enzymes, which are of fundamental importance in the cleavage of common beta -1,4-linkages in saccharides and of practical interest in the alternate energy source industry in treating common forms of biomass. In collaboration with Drs. Steve Withers, Tony Warren and colleagues at the University of British Columbia, we have been able to study the X-ray structures of cex-cd both alone and in complex with intermediates in the catalytic mechanism of the enzyme. This has led to new insights into the recognition by this protein of specific saccharide moeities. It also helped address the long-standing debate about the nature of the intermediate of this reaction: we provided strong evidence supporting the covalent intermediate model. We have also been able to identify specific contacts between the enzyme and the substrate that may assist in forming the tranition state of the reaction.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001646-19
Application #
6491152
Study Section
Project Start
2001-08-15
Project End
2002-08-14
Budget Start
Budget End
Support Year
19
Fiscal Year
2001
Total Cost
$142,703
Indirect Cost
Name
Cornell University
Department
Type
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850
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