Substrate Binding and Catalytic Mechanism of a Barley β-d-Glucosidase/(1,4)-β-d-Glucan Exohydrolase
Open Access
- 1 May 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (18) , 11134-11143
- https://doi.org/10.1074/jbc.273.18.11134
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Protein fold recognition by prediction-based threadingJournal of Molecular Biology, 1997
- Activity Studies and Crystal Structures of Catalytically Deficient Mutants of Cellobiohydrolase I fromTrichoderma reeseiJournal of Molecular Biology, 1996
- The Crystal Structure of a Family 5 Endoglucanase Mutant in Complexed and Uncomplexed Forms Reveals an Induced Fit Activation MechanismJournal of Molecular Biology, 1996
- Barley β-D-Glucan Exohydrolases with β-D-Glucosidase ActivityJournal of Biological Chemistry, 1996
- β‐Glucosidase, β‐galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes wit 8‐fold β/α architecture and with two conserved glutamates near the carboxy‐terminal ends of β‐strands four and sevenFEBS Letters, 1995
- A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factorsInternational Immunology, 1993
- Assessment of protein models with three-dimensional profilesNature, 1992
- Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequencesFEBS Letters, 1987
- Changes in cell wall polysaccharides of germinating barley grainsPhytochemistry, 1978
- Preparation and base-catalyzed reactions of some β-halohydroperoxidesCanadian Journal of Chemistry, 1968