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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2006, Volume 103, Issue 12, pp. 4586 - 4591
Journal Article
Journal Article
Journal Article
The New Phytologist, ISSN 0028-646X, 1/2007, Volume 176, Issue 2, pp. 317 - 324
• Recently, the three-dimensional structure of chicory (Cichorium intybus) fructan 1-exohydrolase (1-FEH Ila) in complex with its preferential substrate,... 
Proteins | Enzymes | Fructans | Active sites | Sodium | Cell walls | Substrate specificity | Site directed mutagenesis | Plants | Mutant proteins | substrate binding cleft | fructan 1‐exohydrolase (1‐FEH IIa) | site‐directed mutagenesis | N‐glycosylation | invertase | substrate specificity | Fructan 1-exohydrolase (1-FEH IIa) | N-glycosylation | Site-directed mutagenesis | Substrate binding cleft | Invertase | site-directed mutagenesis | WHEAT TRITICUM-AESTIVUM | CICHORIUM-INTYBUS | ARABIDOPSIS-THALIANA | ACTIVE-SITE | CRYSTAL-STRUCTURE | X-RAY-DIFFRACTION | PLANT SCIENCES | FUNCTIONAL-ANALYSIS | fructan 1-exohydrolase (1-FEH IIa) | CELL-WALL INVERTASE | METABOLIZING ENZYMES | BETA-FRUCTOSIDASE | Arabidopsis - enzymology | Glycoside Hydrolases - genetics | Molecular Sequence Data | Substrate Specificity | Cell Wall - enzymology | beta-Fructofuranosidase - genetics | Arabidopsis Proteins - metabolism | Plant Proteins - chemistry | Glycoside Hydrolases - chemistry | Plant Proteins - metabolism | Binding Sites | Beta vulgaris - enzymology | Protein Structure, Tertiary | Amino Acid Sequence | Arabidopsis Proteins - genetics | Inulin - chemistry | Mutagenesis, Site-Directed | beta-Fructofuranosidase - chemistry | beta-Fructofuranosidase - metabolism | Models, Molecular | Glycosylation | Plant Proteins - genetics | Sequence Alignment | Inulin - genetics | Arabidopsis Proteins - chemistry | Inulin - metabolism | Glycoside Hydrolases - metabolism | Chicory - enzymology | Physiological aspects | Chemical properties | Oligosaccharides | Knowledge-based systems
Journal Article
Journal Article
BBA - General Subjects, ISSN 0304-4165, 2009, Volume 1790, Issue 10, pp. 1301 - 1306
Xylanases (EC 3.2.1.8) hydrolyze xylan, one of the most abundant plant polysaccharides found in nature, and have many potential applications in biotechnology.... 
Thermostability | Xylanase | Enzyme–substrate interaction | Enzyme-substrate interaction | G/11 XYLANASE | ACTIVE-SITE | TRICHODERMA-REESEI | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOSYL-ENZYME INTERMEDIATE | CONFORMATION | HYDROGEN-BONDS | BIOPHYSICS | MODELS | THERMOPHILIC XYLANASE | SIMULATIONS | PROTEINS
Journal Article