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Your search keyword '"Kurt Gebruers"' showing total 2 results
Start Over Author "Kurt Gebruers" Publisher taylor & francis ltd
2 results on '"Kurt Gebruers"'

1. His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases

Author

Kurt Gebruers, Ellen Fierens, Johnny Beaugrand, Anja Rabijns, Sigrid Rombouts, Marc De Maeyer, Guido Volckaert, Elien Vandermarliere, Steven Van Campenhout, Arnout Voet, Jan A. Delcour, and Christophe M. Courtin

Subjects
Models, Molecular, Glycoside Hydrolases, Mutant, medicine.disease_cause, Pichia pastoris, Protein–protein interaction, Mutant protein, Drug Discovery, Glycoside hydrolase family 11, medicine, Histidine, Glycoside hydrolase, Cloning, Molecular, Site-directed mutagenesis, Triticum, Plant Proteins, Pharmacology, Mutation, Endo-1,4-beta Xylanases, biology, food and beverages, General Medicine, biology.organism_classification, Biochemistry, Mutagenesis, Site-Directed, Protein Binding
Abstract

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. ispartof: Journal of enzyme inhibition and medicinal chemistry vol:24 issue:1 pages:38-46 ispartof: location:England status: published

Published
2009

2. Purification and characterization of a XIP-type endoxylanase inhibitor from Rice (Oryza sativa)

Author

Christophe M. Courtin, Jan A. Delcour, Hans Goesaert, and Kurt Gebruers

Subjects
family, Bacillus subtilis, glycosidase inhibitors, Chromatography, Affinity, l, Gel permeation chromatography, wheat triticum-aestivum, affinity chromatography, Affinity chromatography, xip, Drug Discovery, Botany, Enzyme Inhibitors, different cereals, Peptide sequence, Pharmacology, Endo-1,4-beta Xylanases, Oryza sativa, biology, Molecular mass, rice, Aspergillus aculeatus, food and beverages, barley, Oryza, General Medicine, endoxylanase inhibitor, biology.organism_classification, taxi-type, Biochemistry, Chitinase, biology.protein, xylanase inhibitor, identification, protein
Abstract

A rice XIP-type inhibitor was purified by affinity chromatography with an immobilized Aspergillus aculeatus family 10 endoxylanase. Rice XIP is a monomeric protein, with a molecular mass of ca. 32 kDa and a pI of ca. 5.6. Its N-terminal amino acid sequence was identical to that of a rice chitinase homologue, demonstrating the difficulty when using sequence information to differentiate between endoxylanase inhibitors and (putative) chitinases in rice. Rice XIP inhibited different endoxylanases to a varying degree. In particular, it most strongly inhibited family 10 endoxylanases from A. niger and A. oryzae, while several family 11 enzymes from Bacillus subtilis, A. niger and Trichoderma sp. were not sensitive to inhibition. The above mentioned A. aculeatus endoxylanase was not inhibited either, although gel permeation chromatography revealed that it complexed rice XIP in a 1: 1 molar stoichiometric ratio. ispartof: Journal of enzyme inhibition and medicinal chemistry vol:20 issue:1 pages:95-101 ispartof: location:England status: published

Published
2005

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