Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-beta-glucanases

Biochemistry
Ulla J RudsanderT T Teeri

Abstract

1H NMR spectroscopy has been used to analyze the product profiles arising from the hydrolysis of cellooligosaccharides by family GH9 cellulases. The product profiles obtained with the wild type and several active site mutants of a bacterial processive endoglucanase, TfCel9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCel9A. PttCel9A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar PttCel9A was shown to catalyze the degradation of cellooligosaccharides by inversion of the configuration of the anomeric carbon. The product analyses showed that the number of interactions between the glucose units of the substrate and the aromatic residues in the enzyme active sites determines the point of cleavage in both enzymes.

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Citations

Aug 10, 2010·Analytical and Bioanalytical Chemistry·Liqun WangArthur J Ragauskas
Apr 29, 2009·Plant & Cell Physiology·Junko TakahashiEwa J Mellerowicz
Feb 3, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Alicia Lammerts van BuerenGideon J Davies
Mar 1, 2012·The Plant Journal : for Cell and Molecular Biology·Lenka Franková, Stephen C Fry
Jan 28, 2014·The Arabidopsis Book·Shundai LiYing Gu
Aug 7, 2013·Insect Biochemistry and Molecular Biology·João Paulo L Franco CairoFabio M Squina
Dec 14, 2018·Applied Microbiology and Biotechnology·Evandro Ares de AraújoIgor Polikarpov

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