TAILIEUCHUNG - Báo cáo khoa học: His374 of wheat endoxylanase inhibitor TAXI-I stabilizes complex formation with glycoside hydrolase family 11 endoxylanases

Wheat endoxylanase inhibitor TAXI-I inhibits microbial glycoside hydro-lase family 11 endoxylanases. Crystallographic data of an Aspergillus niger endoxylanase-TAXI-I complex showed His374 of TAXI-I to be a key resi-due in endoxylanase inhibition [Sansen S, De Ranter CJ, Gebruers K, Brijs K, Courtin CM, Delcour JA & Rabijns A (2004)J Biol Chem279, 36022– 36028]. Its role in enzyme–inhibitor interaction was further investigated by site-directed mutagenesis of His374 into alanine, glutamine or lysine | iFEBS Journal His374 of wheat endoxylanase inhibitor TAXI-I stabilizes complex formation with glycoside hydrolase family 11 endoxylanases Katleen Fierens1 Ann Gils2 Stefaan Sansen3 Kristof Brijs1 Christophe M. Courtin1 Paul J. Declerck2 Camiel J. De Ranter3 Kurt Gebruers1 Anja Rabijns3 Johan Robben1 Steven Van Campenhout4 Guido Volckaert4 and Jan A. Delcour1 1 Katholieke Universiteit Leuven Laboratory of Food Chemistry Leuven Belgium 2 Katholieke Universiteit Leuven Laboratory of PharmaceuticalBiology and Phytopharmacology Leuven Belgium 3 Katholieke Universiteit Leuven Laboratory of AnalyticalChemistry and MedicinalPhysicochemistry Leuven Belgium 4 Katholieke Universiteit Leuven Laboratory of Gene Technology Leuven Belgium Keywords endoxylanase inhibitor protein-protein interaction surface plasmon resonance TAXI Correspondence K. Fierens Katholieke Universiteit Leuven Laboratory of Food Chemistry Kasteelpark Arenberg 20 B-3001 Leuven Belgium Fax 32 16 321997 Tel 32 16 321634 E-mail Received 24 June 2005 revised 2 September 2005 accepted 22 September 2005 doi Wheat endoxylanase inhibitor TAXI-I inhibits microbial glycoside hydrolase family 11 endoxylanases. Crystallographic data of an Aspergillus niger endoxylanase-TAXI-I complex showed His374 of TAXI-I to be a key residue in endoxylanase inhibition Sansen S De Ranter CJ Gebruers K Brijs K Courtin CM Delcour JA Rabijns A 2004 J Biol Chem 279 3602236028 . Its role in enzyme-inhibitor interaction was further investigated by site-directed mutagenesis of His374 into alanine glutamine or lysine. Binding kinetics and affinities of the molecular interactions between A. niger Bacillus subtilis Trichoderma longibrachiatum endoxylanases and wild-type TAXI-I and TAXI-I His374 mutants were determined by surface plasmon resonance analysis. Enzyme-inhibitor binding was in accordance with a simple 1 1 binding model. Association and dissociation rate constants of .

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