Rombouts Sigrid, Fierens Ellen, Vandermarliere Elien, Voet Arnout, Gebruers Kurt, Beaugrand Johnny, Courtin Christophe M, Delcour Jan A, de Maeyer Marc, Rabijns Anja, Van Campenhout Steven, Volckaert Guido
Laboratory of Gene Technology, Katholieke Universiteit Leuven, Leuven, Belgium.
J Enzyme Inhib Med Chem. 2009 Feb;24(1):38-46. doi: 10.1080/14756360701841913.
Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.
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