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Comparative NMR Analysis of Cellooligosaccharide Hydrolysis by GH9 Bacterial and Plant Endo-1,4-β-glucanases.

Authors :
Rudsander, Ulla J.
Sandstrom, Corine
Piens, Kathleen
Master, Emma R.
Wilson, David B.
Brumer III, Harry
Kenne, Lennart
Teeri, Tuula T.
Source :
Biochemistry. 5/6/2008, Vol. 47 Issue 18, p5235-5241. 7p. 1 Diagram, 2 Charts, 12 Graphs.
Publication Year :
2008

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, Tf CeI9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCeI9A. PttCel9A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar Pt1CeI9A 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00062960
Volume :
47
Issue :
18
Database :
Academic Search Index
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
32037283
Full Text :
https://doi.org/10.1021/bi702193e