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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Phanerodontia chrysosporium and UniProt Accession Q25BW4

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EC Tree
IUBMB Comments
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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This record set is specific for:
Phanerodontia chrysosporium
UNIPROT: Q25BW4
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Word Map
The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-glucosidase, linamarase, beta-glu, emulsin, bglu1, zm-p60.1, bgl1b, cel3a, novozyme 188, t-cell inhibitor, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amygdalase
-
-
-
-
amygdalinase
-
-
-
-
arbutinase
-
-
-
-
aryl-beta-glucosidase
-
-
-
-
beta-1,6-glucosidase
-
-
-
-
beta-D-glucosidase
-
-
-
-
beta-D-glucoside glucohydrolase
-
-
-
-
beta-glucoside hydrolase
-
-
-
-
BGA
-
-
-
-
cellobiase
-
-
-
-
elaterase
-
-
-
-
emulsin
-
-
-
-
gentiobiase
-
-
-
-
limarase
-
-
-
-
Novozyme 188
-
-
-
-
p-nitrophenyl beta-glucosidase
-
-
-
-
primeverosidase
-
-
-
-
salicilinase
-
-
-
-
T-cell inhibitor
-
-
-
-
vicianase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
show the reaction diagram
the putative acid/base catalyst is Glu170
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
show the reaction diagram
the putative acid/base catalyst is Glu170
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-22-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
show the reaction diagram
low activity
-
-
?
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
D-cellobiono-1,5-lactone + H2O
D-glucose + D-glucono-1,5-lactone
show the reaction diagram
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
D-cellobiono-1,5-lactone + H2O
D-glucose + D-glucono-1,5-lactone
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
delta-gluconolactone
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.02
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.619
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
10.2
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.229
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.752
4-nitrophenyl-beta-D-xylopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
4.06 - 114
cellobiose
0.12 - 0.2
p-nitrophenyl-beta-D-glucose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 9.15
4-nitrophenyl-beta-D-galactopyranoside
0.04 - 9.35
4-nitrophenyl-beta-D-glucopyranoside
0.9 - 67.6
4-nitrophenyl-beta-D-galactopyranoside
20.8
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.384
4-nitrophenyl-beta-D-xylopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
2.53 - 181
cellobiose
96.2 - 103.1
p-nitrophenyl-beta-D-glucose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
delta-gluconolactone
hydrolysis of p-nitrophenyl-beta-D-glucopyranoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
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
32
-
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
45
-
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
95
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
mutants V173C and D229N/K253A
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
pH-profile of wild-type isozyme BGL1B, overview
4.5 - 8
pH-profile of wild-type and mutant isozymes BGL1A, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme BGL1B; gene bgl1B, isozyme BGL1B
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BGL1B_PHACH
540
0
60665
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, recombinant His-tagged isozyme BGL1B, SDS-PAGE
116000
x * 116000, SDS-PAGE, wild-type BGL
133000
x * 133000, SDS-PAGE, recombinant BGL
46000
recombinant isozyme BGL1A, gel filtration
53000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, recombinant His-tagged isozyme BGL1B, SDS-PAGE
monomer
1 * 53000, recombinant isozyme BGL1A, SDS-PAGE
additional information
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 Tris–HCl, 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D229N
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
D229N/K253A
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
H231D
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
K253A
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
M177L
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
V173C
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozyme BGL1B from Escherichia coli by ammonium sulfate fractionation, hydrophobic interaction chromatography, and nickel affinity chromatography
recombinant and wild-type beta-glucosidase
recombinant His-tagged isozyme BGL1A from Escherichia coli by ammonium sulfate fractionation, hydrophobic interaction chromatography, and nickel affinity chromatography
recombinant His-tagged isozyme BGL1A from Escherichia coli by anion exchange and affinity chromatography, and gel filtration
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
expression in Pichia pastoris
expression of His-tagged isozyme BGL1A 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawai, R.; Yoshida, M.; Tani, T.; Igarashi, K.; Ohira, T.; Nagasawa, H.; Samejima, M.
Production and characterization of recombinant Phanerochaete chrysosporium beta-glucosidase in the methylotrophic yeast Pichia pastoris
Biosci. Biotechnol. Biochem.
67
1-7
2003
Phanerodontia chrysosporium (Q8TGC6), Phanerodontia chrysosporium
Manually annotated by BRENDA team
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
Appl. Microbiol. Biotechnol.
73
807-814
2006
Phanerodontia chrysosporium (Q25BW4), Phanerodontia chrysosporium (Q25BW5), Phanerodontia chrysosporium, Phanerodontia chrysosporium K-3 (Q25BW4), Phanerodontia chrysosporium K-3 (Q25BW5)
Manually annotated by BRENDA team
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
Biotechnol. Bioeng.
99
1295-1302
2008
Phanerodontia chrysosporium (Q25BW4), Phanerodontia chrysosporium (Q25BW5), Phanerodontia chrysosporium
Manually annotated by BRENDA team
Nijikken, Y.; Tsukada, T.; Igarashi, K.; Samejima, M.; Wakagi, T.; Shoun, H.; Fushinobu, S.
Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium
FEBS Lett.
581
1514-1520
2007
Phanerodontia chrysosporium (Q25BW5), Phanerodontia chrysosporium
Manually annotated by BRENDA team
Shrestha, P.; Ibanez, A.B.; Bauer, S.; Glassman, S.I.; Szaro, T.M.; Bruns, T.D.; Taylor, J,W.
Fungi isolated from Miscanthus and sugarcane: biomass conversion, fungal enzymes, and hydrolysis of plant cell wall polymers
Biotechnol. Biofuels
8
38
2015
Alternaria sp., Aspergillus sp., Aureobasidium sp., Chloridium sp., Phanerodontia chrysosporium, Cladosporium sp., Penicillium sp., Exophiala sp., Fusarium sp., Neurospora crassa, Phoma sp., Trichoderma reesei, Trichoderma sp., Postia placenta, Bipolaris sp., Epicoccum sp., Dothideomycetes sp., Microdochium sp., Nigrospora sp., Arthrinium sp., Cephalosporium sp., Sporothrix sp., Minimidochium sp. TMS-2011, Cordyceps sp.
Manually annotated by BRENDA team