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Information on EC 3.2.1.126 - coniferin beta-glucosidase
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EC Tree
3.2.1.126 coniferin beta-glucosidaseIUBMB Comments
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.
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Word Map
- 3.2.1.126
- monolignols
- glucosides
- lignin
- syringin
-
lignification
-
coniferyl
-
pinus
-
cinnamyl
- contorta
-
p-coumaryl
- xylem
-
phenylpropanoid
-
gymnosperms
-
apoplastic
-
bglus
-
latifolia
- pastoris
-
lodgepole
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
os4bglu18, os4bglu16, bglu46, os4bglu14, bglu45, coniferin beta-glucosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
coniferin-hydrolyzing beta-glucosidase
-
-
-
-
glucosidase, coniferin beta-
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coniferin + H2O = D-glucose + coniferol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
83869-30-1
-
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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-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
-
57% of the activity with coniferin
-
?
2-nitrophenyl beta-D-xyloside + H2O
2-nitrophenol + D-xylose
-
poor substrate
-
-
?
4-coumaryl beta-D-glucoside
coumaric acid + D-glucose
-
-
-
?
4-coumaryl beta-D-glucoside + H2O
coumaric acid + D-glucose
-
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
-
poor substrate
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
16% of the activity with coniferin
-
?
4-methylumbelliferyl-beta-D-glucoside
4-methylumbelliferol + beta-D-glucose
-
9% activity with BGLU46
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
26% of the activity with coniferin
-
?
5-[4-(beta-D-glucopyranosyloxy)-3-methoxyphenylmethylene]-2-thioxothiazolidin-4-one-3-ethanoic acid + H2O
?
-
synthetic coniferin analog, 45% of the activity with coniferin
-
?
arbutin
benzene-1,4-diol + beta-D-glucose
-
6% activity with BGLU46
-
-
?
coniferin
beta-D-glucose + coniferyl aldehyde
-
87% activity with BGLU45 and 8% activity with BGLU46
-
-
?
o-nitrophenyl beta-D-glucopyranoside + H2O
beta-D-glucose + o-nitrophenol
-
-
-
?
o-nitrophenyl-beta-D-glucopyranoside
o-nitrophenol + beta-D-glucose
-
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
-
6.9% activity with BGLU45 and 71% activity with BGLU46
-
-
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
with moderate efficiency
-
?
p-nitrophenyl beta-cellobioside + H2O
?
-
releases only terminal glucose from the substrate
-
?
p-nitrophenyl beta-D-fucopyranoside + H2O
beta-D-fucose + p-nitrophenol
-
with moderate efficiency
-
?
p-nitrophenyl beta-D-galactopyranoside + H2O
beta-D-galactose + p-nitrophenol
-
with low efficiency
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
beta-D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl beta-D-xylopyranoside + H2O
beta-D-xylose + p-nitrophenol
-
73% of the efficiency with p-nitrophenyl beta-D-glucopyranoside
-
?
p-nitrophenyl-beta-D-galactopyranoside
p-nitrophenol + beta-D-galactose
-
0.4% activity with BGLU45 and 21% activity with BGLU46
-
-
?
p-nitrophenyl-beta-D-glucopyranoside
p-nitrophenol + beta-D-glucose
-
100% activity with BGLU45 and BGLU46
-
-
?
phenyl-beta-D-glucoside
phenol + beta-D-glucose
-
62% activity with BGLU46
-
-
?
salicin
beta-D-glucose + salicyl alcohol
-
100% activity with BGLU46
-
-
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + D-galactose
-
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
-
best substrate
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
reaction at 79% (isozyme II) or 51% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
-
poor substrate, not
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
reaction at 56% (isozyme II) or 8% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
?
coniferin + H2O
coniferol + D-glucose
-
reaction at 52% (isozyme I) or 38% (isozyme II) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
?
coniferin + H2O
coniferol + D-glucose
-
i.e. coniferyl alcohol beta-D-glucoside, (E)-coniferin
i.e. trans-coniferyl alcohol
?
coniferin + H2O
D-glucose + coniferol
-
natural substrate
-
?
coniferin + H2O
D-glucose + coniferol
-
20000fold preference for the natural substrate coniferin over cellobiose
-
?
coniferin + H2O
D-glucose + coniferol
-
-
-
?
coniferin + H2O
D-glucose + coniferol
-
the native substrate is efficiently hydrolyzed, preferred substrates
-
?
coniferin + H2O
D-glucose + coniferol
-
native substrate, may play a crucial role in stem lignification
-
?
picein + H2O
?
-
reaction at 50% (isozyme II) or 12% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
?
salicin + H2O
?
-
reaction at 25% (isozyme II) or 2% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
?
syringin + H2O
D-glucose + sinapyl alcohol
-
100% activity with BGLU45 and 6% activity with BGLU46
-
-
?
syringin + H2O
D-glucose + sinapyl alcohol
-
-
-
?
syringin + H2O
D-glucose + sinapyl alcohol
-
reaction at about 30% the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
-
-
?
syringin + H2O
D-glucose + sinapyl alcohol
-
51% of the activity with coniferin
-
?
additional information
?
-
-
enzyme has a high transglycosylation activity in the presence of alcohols, transglycosylation mechanism
-
?
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
-
-
?
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
?
-
-
not: disaccharide-containing glycoside, 4-nitrophenyl beta-cellobioside, 4-methylumbelliferyl alpha-glucoside
-
?
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NATURAL SUBSTRATE
NATURAL 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
coniferin + H2O
D-glucose + coniferol
-
natural substrate
-
?
coniferin + H2O
D-glucose + coniferol
-
native substrate, may play a crucial role in stem lignification
-
?
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INHIBITOR
ORGANISM
UNIPROT
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
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 bromoconduritol or conduritol B epoxide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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-propanol
-
20 mM, activates, highest rate of consumption of p-nitrophenyl beta-D-glucopyranoside in the presence of 0.6 M 1-propanol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
4-methylumbelliferyl beta-D-glucoside
-
ferulic acid p-beta-glucoside, 4-nitrophenyl beta-D-glucoside
0.6
Picein
-
2-nitrophenyl beta-D-glucoside, 2-nitrophenyl beta-D-galactoside, hypocotyls
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
BGLU45 and BGLU46 display increasing levels of expression from apex to base, matching the known increase in lignification
brenda
additional information
-
BGLU45 and BGLU46 absent from rosette leaves or flowers
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
OsBGlu16-GFP fusion protein is localized to the cell wall, when expressed in tobacco leaf epithelial cells
brenda
-
the enzyme is ionically bound to cell wall in differentiating xylem of poplar
brenda
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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). CBG_PINCO
513
0
58300
Swiss-Prot
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
88289
-
x * 98000, about, SDS-PAGE, x * 88289, sequence calculation
98000
-
x * 98000, about, SDS-PAGE, x * 88289, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer