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

(2008) BIOCHEMISTRY. 47(18). p.5235-5241
Author
Organization
Abstract
H-1 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 Cel9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCe19A. PttCe19A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar PttCe19A 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.
Keywords
STRAWBERRY, OLIGOSACCHARIDES, 4-GLUCANASE, ENDO-BETA-1, MECHANISM, PURIFICATION, 4-BETA-GLUCANASE, ENDO-1, PICHIA-PASTORIS, SUBSTRATE-BINDING, THERMOMONOSPORA-FUSCA, TRICHODERMA-REESEI

Citation

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Chicago
Rudsander, Ulla, Corine Sandstrom, Kathleen Piens, Emma Master, David Wilson, Harry Brumer, Lennart Kenne, and Tuula Teeri. 2008. “Comparative NMR Analysis of Cellooligosaccharide Hydrolysis by GH9 Bacterial and Plant Endo-1,4-ss-glucanases.” Biochemistry 47 (18): 5235–5241.
APA
Rudsander, U., Sandstrom, C., Piens, K., Master, E., Wilson, D., Brumer, H., Kenne, L., et al. (2008). Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-ss-glucanases. BIOCHEMISTRY, 47(18), 5235–5241.
Vancouver
1.
Rudsander U, Sandstrom C, Piens K, Master E, Wilson D, Brumer H, et al. Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-ss-glucanases. BIOCHEMISTRY. 1155 16TH ST, NW, WASHINGTON, DC 20036 USA: AMER CHEMICAL SOC; 2008;47(18):5235–41.
MLA
Rudsander, Ulla, Corine Sandstrom, Kathleen Piens, et al. “Comparative NMR Analysis of Cellooligosaccharide Hydrolysis by GH9 Bacterial and Plant Endo-1,4-ss-glucanases.” BIOCHEMISTRY 47.18 (2008): 5235–5241. Print.
@article{684836,
  abstract     = {H-1 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 Cel9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCe19A. PttCe19A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar PttCe19A 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.},
  author       = {Rudsander, Ulla and Sandstrom, Corine and Piens, Kathleen and Master, Emma and Wilson, David and Brumer, Harry and Kenne, Lennart and Teeri, Tuula},
  issn         = {0006-2960},
  journal      = {BIOCHEMISTRY},
  language     = {eng},
  number       = {18},
  pages        = {5235--5241},
  publisher    = {AMER CHEMICAL SOC},
  title        = {Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-ss-glucanases},
  url          = {http://dx.doi.org/10.1021/bi702193e},
  volume       = {47},
  year         = {2008},
}

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