Information on EC 3.2.1.91 - cellulose 1,4-beta-cellobiosidase (non-reducing end) and Organism(s) Acetivibrio thermocellus and UniProt Accession Q59325
for references in articles please use BRENDA:EC3.2.1.91
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The taxonomic range for the selected organisms is: Acetivibrio thermocellus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
enzyme preferentially cleaves the second or the fourth glycosidic bond, cleaves the second bond between putative sub-sites -2 and -1 or +1 and +2, cleaves the fourth bond between putative sub-sites -1 and +1
2.45 mol bound by one pair of immunoglobulin-like module and catalytic module in the wild-type enzyme, the metal content is similar in the mutant enzymes, overview
the enzyme is composed of an N-terminal carbohydrate-binding module of family 4 CBD4, an immunoglobulin-like module Ig, a catalytic module of glycoside hydrolase family 9 GH9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 CBD3, and finally a C-terminal dockerin module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of doamin coupling, overview
the enzyme is composed of an N-terminal carbohydrate-binding module of family 4 CBD4, an immunoglobulin-like module Ig, a catalytic module of glycoside hydrolase family 9 GH9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 CBD3, and finally a C-terminal dockerin module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of doamin coupling, overview
the enzyme is composed of an N-terminal carbohydrate-binding module of family 4, an immunoglobulin-like module, a catalytic module of glycoside hydrolase family 9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 and finally a C-terminal dockerin module, elimination of the immunoglobulin-like module leads to complete inactivation of the catalytic module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of secondary and tertiary structure of the enzyme, overview
sitting drop vapor diffusion method, using in 0.2 M ammonium iodide, 20% (w/v) polyethylene glycol 3350 pH 6.2 or 0.2 M CaCl2, 20% (w/v) polyethylene glycol 3350 pH 5.1
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
recombinant His-tagged enzyme domain constructs from Escherichia coli strain BL21(DE3) to near homogeneity by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) to near homogeneity by nickel affinity chromatography and gel filtration
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide might influence substrate specificity by affecting the local structure of the CelK-specific N-terminal region containing an immunoglobulin-like domain
Isolation and characterisation of a major cellobiohydrolase (S8) and a major endoglucanase (S11) subunit from the cellulosome of Clostridium thermocellum