Differential recognition of animal type beta4-galactosylated and alpha3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum

Glycobiology
Harry BoerAnu Koivula

Abstract

We report the purification of two glycosyl hydrolase family 18 chitinases, Chit33 and Chit42, from the filamentous fungus Trichoderma harzianum and characterization using a panel of different soluble chitinous substrates and inhibitors. We were particularly interested in the potential of these (alpha/beta)(8)-barrel fold enzymes to recognize beta-1,4-galactosylated and alpha-1,3-fucosylated oligosaccharides, which are animal-type saccharides of medical relevance. Three-dimensional structural models of the proteins in complex with chito-oligosaccharides were built to support the interpretation of the hydrolysis data. Our kinetic and inhibition studies are indicative of the substrate-assisted catalysis mechanism for both chitinases. Both T. harzianum chitinases are able to catalyze some transglycosylation reactions and cleave both simple chito-oligosaccharides and synthetically modified, beta-1,4-galactosylated and alpha-1,3-fucosylated chito-oligosaccharides. The cleavage data give experimental evidence that the two chitinases have differences in their substrate-binding sites, Chit42 apparently having a deeper substrate binding groove, which provides more tight binding of the substrate at subsites (-2-1-+1+2). On the other hand,...Continue Reading

Citations

Jan 17, 2009·Applied Microbiology and Biotechnology·Sanni P VoutilainenAnu Koivula
Dec 3, 2011·Applied Microbiology and Biotechnology·Lukas HartlVerena Seidl-Seiboth
May 11, 2010·Evolutionary Bioinformatics Online·Katarina IhrmarkMagnus Karlsson
Jul 19, 2013·Critical Reviews in Biotechnology·Anand NagpureRajinder K Gupta
Jul 28, 2010·Bioresource Technology·Laura Ramirez-CoutiñoKeiko Shirai
May 22, 2013·Biochimica Et Biophysica Acta·Hideyuki IharaYoshitaka Ikeda
Dec 22, 2016·Marine Drugs·Sara Skøtt PaulsenHenrique Machado

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