Substrate positioning in chitinase A, a processive chito-biohydrolase from Serratia marcescens |
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Authors: | Norberg Anne Line Dybvik Anette I Zakariassen Henrik Mormann Michael Peter-Katalini? Jasna Eijsink Vincent G H Sørlie Morten |
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Institution: | Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, ?s, Norway. |
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Abstract: | The contributions of the -3 subsite and a putative +3 subsite to substrate positioning in ChiA from Serratia marcescens have been investigated by comparing how ChiA and its -3 subsite mutant W167A interact with soluble substrates. The data show that Trp - GlcNAc stacking in the -3 subsite rigidifies the protein backbone supporting the formation of the intermolecular interaction network that is necessary for the recognition and positioning of the N-acetyl groups before the -1 subsite. The +3 subsite exhibits considerable substrate affinity that may promote endo-activity in ChiA and/or assist in expelling dimeric products from the +1 and +2 subsites during processive hydrolysis. |
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