Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
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SYSTEMATIC NAME
IUBMB Comments
beta-D-glucoside glucohydrolase
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
determination and analysis of the subsite -1, i.e. glycone site, of isozyme BGL1A, overview, the loop region covering on the (beta/alpha)8 barrel is significantly deviated forming a unique subsite +1, i.e. aglycone site, of BGL1A
determination and analysis of the subsite -1, i.e. glycone site, of isozyme BGL1A, overview, the loop region covering on the (beta/alpha)8 barrel is significantly deviated forming a unique subsite +1, i.e. aglycone site, of BGL1A
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme BGL1A in substrate-free and gluconolactone complexed forms, sitting-drop vapor diffusion method at 25 °C, using a mixture of 0.001 ml of protein solution containing 10 mg/ml protein in 20 mM TrisHCl, pH 7.5, 150 mM NaCl, with or without 10 mM D-glucono-1,5-lactone, and 0.001 ml of a reservoir solution containing 12% isopropanol, 15% PEG 6000 and 0.1M sodium citrate, pH 5.8, the cryoprotectant solution contains 20% MPD, 15% PEG 6000 and 0.1M sodium citrate, pH 5.8, X-ray diffraction structure determination and analysis at 1.5-1.9 A resolution, modeling
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A
site-directed mutagenesis, mutation of the isozyme BGL1A residues from subsite +1 to the correspondent residues of isozyme BGL1B, the double mutant has a hydrolytic activity at neutral pH that is restored to that of the wild-type enzyme
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows catalytic efficiency similar to the wild-type BGL1A
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows catalytic efficiency similar to the wild-type BGL1A
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme BGL1B, DNA and amino acid sequence determination and analysis, transcription analysis, expression of C-terminally His-tagged enzyme in Escherichia coli
isozyme BGL1A, DNA and amino acid sequence determination and analysis, transcription analysis, expression of C-terminally His-tagged enzyme in Escherichia coli
Tsukada, T.; Igarashi, K.; Yoshida, M.; Samejima, M.
Molecular cloning and characterization of two intracellular beta-glucosidases belonging to glycoside hydrolase family 1 from the basidiomycete Phanerochaete chrysosporium
Tsukada, T.; Igarashi, K.; Fushinobu, S.; Samejima, M.
Role of subsite +1 residues in pH dependence and catalytic activity of the glycoside hydrolase family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium