Catalysis by a rigid enzyme

Session: 
S4.4 Polysaccharide processing for biofuels
Code: 
OL4.4.4
Location (hall): 
Fucose
Start/end time: 
Tuesday, July 2, 2019 - 12:30 to 12:45
Fredj
Ben Bdira

F. Ben Bdira1, A. N.  Volkov2, E. AB3, S. Schröder1, J. Codee1, H.S.  Overkleeft1, J.M.F.G. Aerts1, H. van Ingen4, M. Ubbink1

1Leiden University, Leiden, The Netherlands, 2VIB, Brussels, Belgium, 3ZoBio BV, Leiden, The Netherlands, 4Utrecht University, Utrecht, The Netherlands

Many enzymes are dynamic entities, sampling conformational states that are relevant for catalytic activity. Nevertheless, crystal structures of catalytic intermediates suggest that other enzymes do not require structural changes for activity. The single domain enzyme xylanase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose. It is demonstrated that BCX in solution is undergoing minimal structural changes during catalysis. A rigid protein matrix provides a frame for fast substrate binding, followed slow distortion induced by the enzyme to enable hydrolysis. Thus, the dynamics of the substrate rather than the enzyme are essential for catalysis. 

Acknowlegements

Czech Science Foundation project 18-00150S and the joint Czech-Italian AVČR-CNR (V.K. & S.R.) mobility project No. CNR-16-30 are acknowledged.

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