Molecular basis for oligosaccharide epimerases and their related enzymes.

2015 Fiscal Year Final Research Report

• Project/Area Number: 26850059
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Applied biochemistry
• Research Institution: Hokkaido University
• Principal Investigator: SABURI Wataru 北海道大学, (連合)農学研究科(研究院), 助教 (00598089)
• Project Period (FY): 2014-04-01 – 2016-03-31
• Keywords: セロビオース2-エピメラーゼ / エピメラーゼ / イソメラーゼ

Outline of Final Research Achievements

Cellobiose 2-epimerase (CE) epimerizes the reducing end glucose residue of beta1-4 disaccharides to mannose residue. It shares the catalytic domain and site structures with other monosaccharide isomerases/epimerases. In this study, structure-function relationship of these enzymes was analyzed. Important amino acid residues for high selectivity for disaccharides in Rhodothermus marines CE were determined through site-directed mutation. Slight isomerization activity was observed in R. marines CE, and important structure for isomerase activity was determined based on the comparison of the structures between R. marines and Cardicellulosiruptor saccharolyticus CEs. A novel enzyme acting on mannose was found from function unknown proteins.

Free Research Field

応用生物化学