Information on EC 3.2.1.126 - coniferin beta-glucosidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.2.1.126
-
RECOMMENDED NAME
GeneOntology No.
coniferin beta-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
coniferin + H2O = D-glucose + coniferol
show the reaction diagram
-
-
-
-
coniferin + H2O = D-glucose + coniferol
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
coniferin metabolism
-
Phenylpropanoid biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
coniferin beta-D-glucosidase
Also hydrolyses syringin, 4-cinnamyl alcohol beta-glucoside and, more slowly, some other aryl beta-glycosides. A plant cell-wall enzyme involved in the biosynthesis of lignin.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-glucosidase
-
-
coniferin-hydrolyzing beta-glucosidase
-
-
-
-
glucosidase, coniferin beta-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
83869-30-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
chickpea
-
-
Manually annotated by BRENDA team
spruce
-
-
Manually annotated by BRENDA team
var. latifolia Engelm, 10-15 years old
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-amygdalin
?
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + D-galactose
show the reaction diagram
-
-
-
-
-
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + D-galactose
show the reaction diagram
-
reaction at 16% (isozyme I) or 13% (isozyme II) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
-
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
show the reaction diagram
-
best substrate
-
-
-
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
show the reaction diagram
-
57% of the activity with coniferin
-
?
2-nitrophenyl beta-D-xyloside + H2O
2-nitrophenol + D-xylose
show the reaction diagram
-
poor substrate
-
-
-
4-coumaryl beta-D-glucoside + H2O
coumaric acid + D-glucose
show the reaction diagram
-
reaction at 25% (isozyme II) or 4% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
4-methylumbelliferyl beta-D-glucosaminide + H2O
4-methylumbelliferone + D-glucosamine
show the reaction diagram
-
poor substrate
-
-
-
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
show the reaction diagram
-
reaction at 79% (isozyme II) or 51% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
-
16% of the activity with coniferin
-
?
4-methylumbelliferyl-beta-D-glucoside
4-methylumbelliferol + beta-D-glucose
show the reaction diagram
-
9% activity with BGLU46
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
show the reaction diagram
-
poor substrate, not
-
-
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
reaction at 56% (isozyme II) or 8% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
26% of the activity with coniferin
-
?
5-[4-(beta-D-glucopyranosyloxy)-3-methoxyphenylmethylene]-2-thioxothiazolidin-4-one-3-ethanoic acid + H2O
?
show the reaction diagram
-
synthetic coniferin analog, 45% of the activity with coniferin
-
?
arbutin
benzene-1,4-diol + beta-D-glucose
show the reaction diagram
-
6% activity with BGLU46
-
-
?
arbutin + H2O
?
show the reaction diagram
-
-
-
?
coniferin
beta-D-glucose + coniferyl aldehyde
show the reaction diagram
-
87% activity with BGLU45 and 8% activity with BGLU46
-
-
?
coniferin + H2O
coniferol + D-glucose
show the reaction diagram
-
-
-
-
-
coniferin + H2O
coniferol + D-glucose
show the reaction diagram
-
-
-
-
coniferin + H2O
coniferol + D-glucose
show the reaction diagram
-
reaction at 52% (isozyme I) or 38% (isozyme II) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
coniferin + H2O
coniferol + D-glucose
show the reaction diagram
-
i.e. coniferyl alcohol beta-D-glucoside, (E)-coniferin
i.e. trans-coniferyl alcohol
-
coniferin + H2O
D-glucose + coniferol
show the reaction diagram
-
natural substrate, 20000fold preference for the natural substrate coniferin over cellobiose
-
?
coniferin + H2O
D-glucose + coniferol
show the reaction diagram
-
the native substrate is efficiently hydrolyzed, preferred substrates, native substrate, may play a crucial role in stem lignification
-
?
coniferin + H2O
?
show the reaction diagram
-
plant cell wall enzyme, involved in lignin biosynthesis
-
-
-
ferulic acid p-beta-glucoside + H2O
ferulic acid + D-glucose
show the reaction diagram
-
-
-
-
-
o-nitrophenyl beta-D-glucopyranoside + H2O
beta-D-glucose + o-nitrophenol
show the reaction diagram
-
-
-
?
o-nitrophenyl-beta-D-glucopyranoside
o-nitrophenol + beta-D-glucose
show the reaction diagram
-
most rapidly hydrolysed by BGLU45 and BGLU46 with relative rates of 619% and 449%, respectively, of the rate of p-nitrophenyl-beta-D-glucoside degradation
-
-
-
p-coumaryl beta-D-glucoside
p-coumaric acid + beta-D-glucose
show the reaction diagram
-
6.9% activity with BGLU45 and 71% activity with BGLU46
-
-
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
show the reaction diagram
-
with moderate efficiency
-
?
p-nitrophenyl beta-cellobioside + H2O
?
show the reaction diagram
-
releases only terminal glucose from the substrate
-
?
p-nitrophenyl beta-D-fucopyranoside + H2O
beta-D-fucose + p-nitrophenol
show the reaction diagram
-
with moderate efficiency
-
?
p-nitrophenyl beta-D-galactopyranoside + H2O
beta-D-galactose + p-nitrophenol
show the reaction diagram
-
with low efficiency
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
beta-D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl beta-D-xylopyranoside + H2O
beta-D-xylose + p-nitrophenol
show the reaction diagram
-
73% of the efficiency with p-nitrophenyl beta-D-glucopyranoside
-
?
p-nitrophenyl-beta-D-galactopyranoside
p-nitrophenol + beta-D-galactose
show the reaction diagram
-
0.4% activity with BGLU45 and 21% activity with BGLU46
-
-
-
p-nitrophenyl-beta-D-glucopyranoside
p-nitrophenol + beta-D-glucose
show the reaction diagram
-
100% activity with BGLU45 and BGLU46
-
-
-
phenyl-beta-D-glucoside
phenol + beta-D-glucose
show the reaction diagram
-
62% activity with BGLU46
-
-
?
picein + H2O
?
show the reaction diagram
-
-
-
-
-
picein + H2O
?
show the reaction diagram
-
reaction at 50% (isozyme II) or 12% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
salicin
beta-D-glucose + salicyl alcohol
show the reaction diagram
-
100% activity with BGLU46
-
-
?
salicin + H2O
?
show the reaction diagram
-
-
-
?
salicin + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
salicin + H2O
?
show the reaction diagram
-
reaction at 25% (isozyme II) or 2% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
syringin
beta-D-glucose + sinapyl alcohol
show the reaction diagram
-
100% activity with BGLU45 and 6% activity with BGLU46
-
-
?
syringin + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
syringin + H2O
?
show the reaction diagram
-
reaction at about 30% the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
-
syringin + H2O
?
show the reaction diagram
-
51% of the activity with coniferin
-
?
feruloyl glucoside + H2O
ferulic acid + glucose
show the reaction diagram
-
poor substrate
-
-
-
additional information
?
-
-
very poor substrates are arbutin or indican, no substrates are alpha-glucosides, 4-methylumbelliferyl beta-cellobioside, 4-methylumbelliferyl beta-glucuronide, quercetin 3-rhamnosyl glucoside, quercetin 3-rhamnoside or cellobiose
-
-
-
additional information
?
-
-
enzyme has a high transglycosylation activity in the presence of alcohols, transglycosylation mechanism
-
?
additional information
?
-
-
not: disaccharide-containing glycoside, 4-nitrophenyl beta-cellobioside, 4-methylumbelliferyl alpha-glucoside
-
?
additional information
?
-
-
no activity with sinigrin, methyl-beta-D-glucoside, D(+)cellobiose, beta-gentiobiose, D(+)maltose, sucrose, p-nitrophenyl-1-thio-beta-D-glucopyranoside, p-nitrophenyl-alpha-D-glucopyranoside, p-nitrophenyl-N-acetyl-beta-D-glucosaminide, p-nitrophenyl-beta-D-mannopyranoside, p-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-L-fucopyranoside and p-nitrophenyl-beta-L-arabinopyranoside
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
coniferin + H2O
D-glucose + coniferol
show the reaction diagram
-
natural substrate
-
?
coniferin + H2O
D-glucose + coniferol
show the reaction diagram
-
native substrate, may play a crucial role in stem lignification
-
?
coniferin + H2O
?
show the reaction diagram
-
plant cell wall enzyme, involved in lignin biosynthesis
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
competitive inhibitor, p-nitrophenyl beta-D-glucopyranoside as substrate
deoxynojirimycin
-
strong, competitive inhibitor, p-nitrophenyl beta-D-glucopyranoside as substrate
glucono-1,5-lactone
-
-
glucuronolactone
-
strong, competitive inhibitor, p-nitrophenyl beta-D-glucopyranoside as substrate
isopropyl 1-thio-beta-D-glucopyranoside
-
competitive inhibitor, p-nitrophenyl beta-D-glucopyranoside as substrate
additional information
-
not inhibited by 24 mM xylose
-
additional information
-
not inhibited by bromoconduritol or conduritol B epoxide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-butanol
-
20 mM, activates due to transglycosylation activity with over 80% of p-nitrophenyl beta-D-glucopyranoside being converted to 1-butyl beta-D-glucopyranoside in the presence of Cbg1 and 100 mM 1-butanol
1-Heptanol
-
20 mM, activates
1-Hexanol
-
20 mM, activates
1-Octanol
-
20 mM, activates
1-Pentanol
-
20 mM, activates
1-Propanol
-
20 mM, activates, highest rate of consumption of p-nitrophenyl beta-D-glucopyranoside in the presence of 0.6 M 1-propanol
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
-
2-nitrophenyl beta-D-galactoside
-
-
0.9
-
4-Methylumbelliferyl beta-D-glucosaminide
-
-
0.4
-
4-methylumbelliferyl beta-D-glucoside
-
ferulic acid p-beta-glucoside, 4-nitrophenyl beta-D-glucoside
1
-
4-methylumbelliferyl beta-D-glucoside
-
hypocotyls
2.3
-
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 30C
0.7
-
4-nitrophenyl beta-D-glucoside
-
hypocotyls
1.9
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C
0.021
-
Arbutin
-
pH 6.5, 30C
0.023
-
coniferin
-
pH 6.5, 30C
0.18
-
coniferin
-
pH 5.5, 30C
0.38
-
coniferin
-
roots
0.8
-
coniferin
-
-
1.3
-
coniferin
-
hypocotyls
7
-
coniferin
-
BGLU45
0.06
-
o-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 30C
2.2
-
p-coumaryl beta-D-glucoside
-
BGLU46
0.27
-
p-nitrophenyl alpha-L-arabinofuranoside
-
pH 6.5, 30C
0.08
-
p-nitrophenyl beta-D-fucopyranoside
-
pH 6.5, 30C
4
-
p-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 30C
0.012
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 30C
0.005
-
p-nitrophenyl beta-D-xylopyranoside
-
pH 6.5, 30C
0.6
-
Picein
-
-
0.6
-
Picein
-
2-nitrophenyl beta-D-glucoside, 2-nitrophenyl beta-D-galactoside, hypocotyls
6.3
-
Picein
-
hypocotyls
0.045
-
Salicin
-
pH 6.5, 30C
0.29
-
syringin
-
pH 5.5, 30C
1.8
-
syringin
-
hypocotyls
5
-
syringin
-
4-nitrophenyl beta-D-glucoside
5.1
-
syringin
-
BGLU45
0.3
-
formononetin 7-beta-glucoside
-
2-nitrophenyl beta-glucoside
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
155
-
o-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 30C
118
-
p-nitrophenyl alpha-L-arabinofuranoside
-
pH 6.5, 30C
22.1
-
p-nitrophenyl beta-D-fucopyranoside
-
pH 6.5, 30C
46.6
-
p-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 30C
3.2
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 30C
95.4
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 30C
28.9
-
p-nitrophenyl beta-D-xylopyranoside
-
pH 6.5, 30C
3.15
-
Salicin
-
pH 6.5, 30C
86.7
-
Salicin
-
pH 6.5, 30C
106
-
coniferin
-
pH 6.5, 30C
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
D-glucose
-
pH 6.5, 30C
0.00078
-
deoxynojirimycin
-
pH 6.5, 30C
0.0039
-
glucuronolactone
-
pH 6.5, 30C
5.6
-
isopropyl 1-thio-beta-D-glucopyranoside
-
pH 6.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.1
-
-
BGLU45, crude extract
4.5
-
-
hypocotyls
6.6
-
-
pH 5.5, 30C
35.9
-
-
BGLU45, purified enzyme
39
41
-
pH 6.5, 30C
43.8
-
-
BGLU46, crude extract
599
-
-
BGLU46, purified enzyme
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
5.5
-
hypocotyls
5.4
5.9
-
optimum in the range at 30C
additional information
-
-
pI: 10 (isozyme I), pI: 10.3 (isozyme II)
additional information
-
-
pI: 3.8
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
6.5
-
about half-maximal activity at pH 3.5 and 6.5, hypocotyls
4
7.5
-
about 20% of maximal activity at pH 4 and 7.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
40
45
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
isoelectric focusing, pH gradient 4-7
4.5
-
-
chromatofocussing, pH gradient of 5.5 to 4
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
tissue distribution
Manually annotated by BRENDA team
-
BGLU45 and BGLU46 display increasing levels of expression from apex to base, matching the known increase in lignification
Manually annotated by BRENDA team
-
lignifying
Manually annotated by BRENDA team
-
exclusive presence in the differentiating xylem
Manually annotated by BRENDA team
additional information
-
BGLU45 and BGLU46 absent from rosette leaves or flowers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
58570
-
-
Picea abies, sedimentation equilibrium method
60000
-
-
gel filtration, native PAGE
90000
-
-
Pinus banksiana, 2 isozymes, MW 90000 and 110000
110000
-
-
Cicer arietinum, gel filtration
110000
-
-
Pinus banksiana, 2 isozymes, MW 90000 and 110000
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 98000, about, SDS-PAGE, x * 88289, sequence calculation
dimer
-
1 * 43000 + 1 * 63000, Cicer arietinum, SDS-PAGE
dimer
-
2 * 28000, SDS-PAGE
monomer
-
1 * 57000, Picea abies, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.5 M NaCl stabilizes, removal inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, in the presence of 0.5 M NaCl, several months
-
-20C, crude cell wall preparation, frozen with liquid nitrogen, at least 3 months
-
4C, in 0.025 M McIlvaine buffer, pH 5, 0.1 M NaCl, 0.02% NaN3, less than 10% loss of activity within 15 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant Cbg1
-
to apparent homogeneity by ammonium sulfate fractionation and hydrophobic interaction chromatography, BGLU45 8.8fold and BGLU46 13.7fold purified
-
to near homogeneity
-
hypocotyls
-
2 isozymes
-
2760fold
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
cDNAs encoding BGLU45 and BGLU46 expressed in Pichia pastoris
-