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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Triticum aestivum and UniProt Accession Q1XH05
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EC Tree
3.2.1.21 beta-glucosidaseIUBMB 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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Word Map
- 3.2.1.21
- cellobiose
- cellulase
- beta-galactosidase
- glycoside
- lysosomal
- alpha-glucosidase
- gaucher
- trichoderma
- aglycone
- endoglucanase
- glycosidases
-
cellulolytic
- almond
- xylanase
- reesei
- beta-xylosidase
-
saccharification
- alpha-mannosidase
- p-nitrophenyl
- alpha-galactosidase
-
lignocellulosic
- urease
- cellobiohydrolase
- avicel
-
cellulosic
- straw
- glucosylceramide
- cassava
- beta-n-acetylglucosaminidase
- xylan
- beta-d-glucopyranoside
- cmcase
- hemicellulose
-
microcrystalline
- beta-mannosidase
- arylamidase
- arbutin
- cellulomonas
-
transglucosylation
- stover
- alpha-l-fucosidase
- alpha-l-arabinofuranosidase
- cellotetraose
- bagasse
- azoreductase
- carboxymethylcellulase
- endo-beta-1,4-glucanase
- cellodextrins
- glucocerebroside
-
xylanolytic
- industry
- biofuel production
- medicine
- nutrition
- degradation
- analysis
- synthesis
- food industry
- molecular biology
- biotechnology
The taxonomic range for the selected organisms is: Triticum aestivum
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
beta-D-glucosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -
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
9001-22-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
2,4-dihydroxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2,4-dihydroxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one glucoside + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-hydroxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2-hydroxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-hydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2-hydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
biochanin A 7-O-beta-D-glucopyranoside + H2O
biochanin A + beta-D-glucose
-
-
-
-
?
luteolin-beta-D-glucoside + H2O
luteolin + beta-D-glucose
-
weak activity
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
weak activity
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
weak activity
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
weak activity
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
Ser464 and Leu465 are critical in the substrate specificity for the substrate of isozyme TaGlu1a
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
Ser464 and Leu465 are critical in the substrate specificity for the substrate of isozyme TaGlu1a
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside
-
30°C, pH 5.5
0.32
2-hydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside
-
30°C, pH 5.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
202.3
-
hydrolysis of 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside
311.9
purified recombinant His-tagged isozyme TaGlu1a
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
young, isozyme TaGlu1b, isozyme expression profile, overview
young, isozyme TaGlu1a, isozyme expression profile, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HGL1B_WHEAT
569
0
64482
Swiss-Prot
Chloroplast (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozyme
additional information
formation of both homo- and heterohexamers by the isozyme
additional information
formation of both homo- and heterohexamers by the isozyme
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozymes
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
6 * 64085.41, recombinant His-tagged TaGlu1b, SDS-PAGE, gel filtration, and mass spectrometry
hexamer
additional information
hexamer
6 * 64141.25, recombinant His-tagged isozyme TaGlu1a, SDS-PAGE, gel filtration, and mass spectrometry
hexamer
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with a substrate aglycone, 20°C, hanging drop vapour diffusion method, 0.001 ml of 3.7 mg/ml protein in solution mixed with 0.001 ml reservoir solution containing 10 mM HEPES, pH 7.2, 1 M LiSO4, and 150 mM NaCl, X-ray diffraction structure determination and preliminary analysis at 1.7 A resolution, molecular replacement
-
purified recombinant isozyme TaGlu1a, X-ray diffraction structure determination and analysis at 1.8 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E191A
site-directed mutagenesis, inactive TaGlu1a mutant
E407A
site-directed mutagenesis, inactive TaGlu1a mutant
F198A
site-directed mutagenesis, the TaGlu1a mutant shows reduced activity with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one with highly incresed Km values, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged Glu1b from Escherichia coli by nickel affinity chelating chromatography, ultrafiltration, and gel filtration
-
recombinant wild-type and mutant isozyme TaGlu1a from Escherichia coli by metal affinity chromatography and gel filtration to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme TaGlu1b, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression in Escherichia coli
isozyme TaGlu1a, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression of wild-type and mutant isozyme TaGlu1a in Escherichia coli
isozyme TaGlu1c, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression in Escherichia coli
overexpression of His-tagged Glu1b in Escherichia coli as soluble protein
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sue, M.; Ishihara, A.; Iwamura, H.
Purification and characterization of a hydroxamic acid glucoside beta-glucosidase from wheat (Triticum aestivum L.) seedlings
Planta
210
432-438
2000
Triticum aestivum
Sue, M.; Yamazaki, K.; Kouyama, J.; Sasaki, Y.; Ohsawa, K.; Miyamoto, T.; Iwamura, H.; Yajima, S.
Purification, crystallization and preliminary X-ray analysis of a hexameric beta-glucosidase from wheat
Acta Crystallogr. Sect. F
61
864-866
2005
Triticum aestivum
Sue, M.; Yamazaki, K.; Yajima, S.; Nomura, T.; Matsukawa, T.; Iwamura, H.; Miyamoto, T.
Molecular and structural characterization of hexameric beta-D-glucosidases in wheat and rye
Plant Physiol.
141
1237-1247
2006
Triticum aestivum (Q1XH04), Triticum aestivum (Q1XH05), Triticum aestivum (Q1XIR9), Secale cereale (Q9FYS3)
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