Comparative NMR Analysis of Cellooligosaccharide Hydrolysis by GH9 Bacterial and Plant Endo-1,4-β-glucanases
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...
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| Veröffentlicht in: | Biochemistry (Easton) 2008-05, Vol.47 (18), p.5235-5241 |
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| container_title | Biochemistry (Easton) |
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| creator | Rudsander, Ulla J Sandstrom, Corine Piens, Kathleen Master, Emma R Wilson, David B Brumer III, Harry Kenne, Lennart Teeri, Tuula T |
| description | 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. |
| doi_str_mv | 10.1021/bi702193e |
| format | Article |
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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. 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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. 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| subjects | Actinomycetales - enzymology Actinomycetales - genetics Cellulase - chemistry Cellulase - genetics Cellulase - metabolism Hydrolysis Kinetics Magnetic Resonance Spectroscopy Models, Biological Molecular Structure Mutation - genetics Oligosaccharides - chemistry Oligosaccharides - metabolism Populus - enzymology |
| title | Comparative NMR Analysis of Cellooligosaccharide Hydrolysis by GH9 Bacterial and Plant Endo-1,4-β-glucanases |
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