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Substrate positioning in chitinase A, a processive chito‐biohydrolase from Serratia marcescens
Author(s) -
Norberg Anne Line,
Dybvik Anette I.,
Zakariassen Henrik,
Mormann Michael,
Peter-Katalinić Jasna,
Eijsink Vincent G.H.,
Sørlie Morten
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.06.002
Subject(s) - serratia marcescens , chitinase , microbiology and biotechnology , substrate (aquarium) , enterobacteriaceae infections , serratia , chemistry , biology , enterobacteriaceae , biochemistry , bacteria , escherichia coli , enzyme , genetics , ecology , gene , pseudomonas
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.