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Information on EC 3.2.1.126 - coniferin beta-glucosidase
for references in articles please use BRENDA:EC3.2.1.126
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.126 coniferin beta-glucosidase
IUBMB Comments
Also hydrolyses syringin, 4-cinnamyl alcohol β-glucoside and, more slowly, some other aryl β-glycosides. A plant cell-wall enzyme involved in the biosynthesis of lignin.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.2.1.126
- monolignols
- glucosides
- lignin
- syringin
-
lignification
-
coniferyl
-
pinus
-
cinnamyl
- contorta
-
p-coumaryl
- xylem
-
phenylpropanoid
-
gymnosperms
-
apoplastic
-
bglus
-
latifolia
- pastoris
-
lodgepole
showSynonyms
os4bglu18, os4bglu16, bglu46, os4bglu14, bglu45, coniferin beta-glucosidase, more
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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
MetaCyc
coniferin metabolism
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
-
Substrates: 57% of the activity with coniferin
Products: -
Products: -
?
2-nitrophenyl beta-D-xyloside + H2O
2-nitrophenol + D-xylose
-
Substrates: poor substrate
Products: -
Products: -
?
4-coumaryl alcohol glucoside + H2O
D-glucose + 4-coumaryl alcohol
Substrates: -
Products: -
Products: -
?
4-coumaryl beta-D-glucoside
coumaric acid + D-glucose
Substrates: -
Products: -
Products: -
?
4-coumaryl beta-D-glucoside + H2O
coumaric acid + D-glucose
-
Substrates: reaction at 25% (isozyme II) or 4% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucosaminide + H2O
4-methylumbelliferone + D-glucosamine
-
Substrates: poor substrate
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
Substrates: 16% of the activity with coniferin
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucoside
4-methylumbelliferol + beta-D-glucose
-
Substrates: 9% activity with BGLU46
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: 26% of the activity with coniferin
Products: -
Products: -
?
5-[4-(beta-D-glucopyranosyloxy)-3-methoxyphenylmethylene]-2-thioxothiazolidin-4-one-3-ethanoic acid + H2O
?
-
Substrates: synthetic coniferin analog, 45% of the activity with coniferin
Products: -
Products: -
?
arbutin
benzene-1,4-diol + beta-D-glucose
-
Substrates: 6% activity with BGLU46
Products: -
Products: -
?
coniferin
beta-D-glucose + coniferyl aldehyde
-
Substrates: 87% activity with BGLU45 and 8% activity with BGLU46
Products: -
Products: -
?
coniferin + H2O
?
-
Substrates: plant cell wall enzyme, involved in lignin biosynthesis
Products: -
Products: -
?
ferulic acid p-beta-glucoside + H2O
ferulic acid + D-glucose
-
Substrates: -
Products: -
Products: -
?
feruloyl glucoside + H2O
ferulic acid + glucose
-
Substrates: poor substrate
Products: -
Products: -
?
o-nitrophenyl beta-D-glucopyranoside + H2O
beta-D-glucose + o-nitrophenol
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl-beta-D-glucopyranoside
o-nitrophenol + beta-D-glucose
-
Substrates: 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
Products: -
Products: -
?
p-coumaryl beta-D-glucoside
p-coumaric acid + beta-D-glucose
-
Substrates: 6.9% activity with BGLU45 and 71% activity with BGLU46
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: with moderate efficiency
Products: -
Products: -
?
p-nitrophenyl beta-cellobioside + H2O
?
-
Substrates: releases only terminal glucose from the substrate
Products: -
Products: -
?
p-nitrophenyl beta-D-fucopyranoside + H2O
beta-D-fucose + p-nitrophenol
-
Substrates: with moderate efficiency
Products: -
Products: -
?
p-nitrophenyl beta-D-galactopyranoside + H2O
beta-D-galactose + p-nitrophenol
-
Substrates: with low efficiency
Products: -
Products: -
?
p-nitrophenyl beta-D-glucopyranoside + H2O
beta-D-glucose + p-nitrophenol
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
beta-D-xylose + p-nitrophenol
-
Substrates: 73% of the efficiency with p-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
p-nitrophenyl-beta-D-galactopyranoside
p-nitrophenol + beta-D-galactose
-
Substrates: 0.4% activity with BGLU45 and 21% activity with BGLU46
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucopyranoside
p-nitrophenol + beta-D-glucose
-
Substrates: 100% activity with BGLU45 and BGLU46
Products: -
Products: -
?
phenyl-beta-D-glucoside
phenol + beta-D-glucose
-
Substrates: 62% activity with BGLU46
Products: -
Products: -
?
salicin
beta-D-glucose + salicyl alcohol
-
Substrates: 100% activity with BGLU46
Products: -
Products: -
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + D-galactose
-
Substrates: reaction at 16% (isozyme I) or 13% (isozyme II) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
-
Substrates: best substrate
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
Substrates: reaction at 79% (isozyme II) or 51% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
-
Substrates: poor substrate, not
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: reaction at 56% (isozyme II) or 8% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
coniferin + H2O
coniferol + D-glucose
-
Substrates: reaction at 52% (isozyme I) or 38% (isozyme II) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
coniferin + H2O
coniferol + D-glucose
-
Substrates: i.e. coniferyl alcohol beta-D-glucoside, (E)-coniferin
Products: i.e. trans-coniferyl alcohol
Products: i.e. trans-coniferyl alcohol
?
coniferin + H2O
D-glucose + coniferol
-
Substrates: 20000fold preference for the natural substrate coniferin over cellobiose
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferol
-
Substrates: natural substrate
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferol
Substrates: -
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferol
-
Substrates: the native substrate is efficiently hydrolyzed, preferred substrates
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferol
-
Substrates: native substrate, may play a crucial role in stem lignification
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferyl alcohol
Substrates: -
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferyl alcohol
-
Substrates: -
Products: -
Products: -
?
picein + H2O
?
-
Substrates: reaction at 50% (isozyme II) or 12% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
salicin + H2O
?
-
Substrates: reaction at 25% (isozyme II) or 2% (isozyme I) the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
-
Substrates: 100% activity with BGLU45 and 6% activity with BGLU46
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
-
Substrates: poor substrate
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
Substrates: -
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
Substrates: -
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
-
Substrates: reaction at about 30% the rate of 2-nitrophenyl beta-D-glucoside hydrolysis
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
-
Substrates: 51% of the activity with coniferin
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a high transglycosylation activity in the presence of alcohols, transglycosylation mechanism
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: rice Os4BGlu18 beta-glucosidase catalyzes hydrolysis of the monolignol glucosides, coniferin, syringin, and 4-coumaryl alcohol glucoside more efficiently than other natural substrates
Products: -
Products: -
-
additional information
?
-
-
Substrates: not: disaccharide-containing glycoside, 4-nitrophenyl beta-cellobioside, 4-methylumbelliferyl alpha-glucoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: recombinant GST-tagged enzyme PbBGLU1 has a stronger activity and higher catalytic efficiency for coniferin than syringin. Isozyme GST-PbBGLU16 exhibits the higher activity and catalytic efficiency for the two substrates compared to isozyme GST-PbBGLU1
Products: -
Products: -
-
additional information
?
-
-
Substrates: recombinant GST-tagged enzyme PbBGLU16 has a stronger activity and higher catalytic efficiency for coniferin than syringin. Isozyme GST-PbBGLU16 exhibits the higher activity and catalytic efficiency for the two substrates compared to isozyme GST-PbBGLU1
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaryl alcohol glucoside + H2O
D-glucose + 4-coumaryl alcohol
Substrates: -
Products: -
Products: -
?
coniferin + H2O
?
-
Substrates: plant cell wall enzyme, involved in lignin biosynthesis
Products: -
Products: -
?
syringin + H2O
D-glucose + sinapyl alcohol
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: rice Os4BGlu18 beta-glucosidase catalyzes hydrolysis of the monolignol glucosides, coniferin, syringin, and 4-coumaryl alcohol glucoside more efficiently than other natural substrates
Products: -
Products: -
-
coniferin + H2O
D-glucose + coniferol
-
Substrates: natural substrate
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferol
-
Substrates: native substrate, may play a crucial role in stem lignification
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferyl alcohol
Substrates: -
Products: -
Products: -
?
coniferin + H2O
D-glucose + coniferyl alcohol
-
Substrates: -
Products: -
Products: -
?
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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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
4-coumaryl alcohol glucoside
recombinant enzyme, pH and temperature not specified in the publication
-
31.9
coniferin
recombinant enzyme, pH and temperature not specified in the publication
24
syringin
recombinant enzyme, pH and temperature not specified in the publication
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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
additional information
-
expression analysis of isozyme PbBGLU1 during fruit development, highest expression level in the early to middle developmental stages, overview
brenda
-
expression analysis of isozyme PbBGLU16 during fruit development, highest expression level in the early to middle developmental stages, overview
brenda
-
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
additional information
-
in situ hybridization analysis shows that PbBGLU1 transcripts are not only localized to some pulp cell walls, lignin deposition, and stone cell areas of a pear fruit, but also a small amount is enriched in normal pear flesh cells
brenda
additional information
-
in situ hybridization analysis shows that PbBGLU16 transcripts are only enriched in lignin deposition and stone cell areas of pear fruit
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
-
BGLU beta-glucosidases of glycoside hydrolase family 1 (GH1) are involved in many processes of plant secondary metabolism. In particular, its de-glycosylation function plays an important role in the transport of lignin monolignols. Enzyme PbBGLU1 is involved in lignin synthesis
physiological function
rice Os4BGlu18 is a monolignol beta-glucosidase which exhibits high substrate specificity for the monolignol glucosides, coniferin, syringin, and p-coumaryl alcohol glucoside
additional information
the Os4BGlu18 structure exhibits the typical (beta/alpha)8 TIM barrel of glycoside hydrolase family 1 (GH1), but the four variable loops and two disulfide bonds appear significantly different from other known structures of GH1 beta-glucosidases. Molecular docking studies of the Os4BGlu18 structure with monolignol substrate ligands places the glycone in a similar position to the delta-gluconolactone in the complex structure and reveals the interactions between protein and ligands. Molecular docking, multiple sequence alignment, and homology modeling identify amino acid residues at the aglycone-binding site involved in substrate specificity for monolignol beta-glucosides. Molecular dynamics simulation. Structural basis of substrate recognition and hydrolysis by monolignol beta-glucosidases, overview
evolution
-
the enzyme belongs to the glycoside hydrolase family 1, GH1. All PbBGLUs contain motif 1 (CTGGBSATEPYJVAHHQLLAHAAAVKLYREKYQA), and only two genes do not contain motif9 (WFEPASES KEDKAAALRALDF), suggesting that motif 1 and motif 9 are conserved gene motifs of PbBGLUs family
evolution
-
the enzyme belongs to the glycoside hydrolase family 1, GH1. All PbBGLUs contain motif1 (CTGGBSATEPYJVAHHQLLAHAAAVKLYREKYQA), and only two genes do not contain motif9 (WFEPASES KEDKAAALRALDF), suggesting that motif1 and motif9 are conserved gene motifs of PbBGLUs family
evolution
the enzyme belongs to the glycoside hydrolase family 1, GH1
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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
other Location (Reliability: 5)
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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
?
-
x * 78070, recombinant GST-tagged isozyme PbBGLU1, SDS-PAGE, x * 52070, recombinant detagged isozyme PbBGLU1, SDS-PAGE
?
-
x * 87230, recombinant GST-tagged isozyme PbBGLU16, SDS-PAGE, x * 61230, recombinant detagged isozyme PbBGLU1, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant free Os4BGlu18 and in complex with delta-gluconolactone, hanging drop vapor diffusion method, mixing of 3 mg/ml protein in 100 mM MES, pH 6.0, with reservoir solution containing 21% PEG 3350, 100 mM MES, pH 6.0, at 15°C, method optimization, crystals of the Os4BGlu18 are soaked in 1 mM delta-gluconolactone in cryoprotectant for 20 min before vitrification to obtain the Os4BGlu18-DG complex, X-ray diffraction structure determination and analysis at 1.7 and 2.1 A resolution, respectively, structure modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Arabidopsis thaliana bglu45 mutant is rescued by expression of Os4BGlu18 displaying lower levels for all three substrates, coniferin, syringin, and 4-coumaryl alcohol glucoside, when compared with non-rescued line
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, crude cell wall preparation, frozen with liquid nitrogen, at least 3 months
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4°C, in 0.025 M McIlvaine buffer, pH 5, 0.1 M NaCl, 0.02% NaN3, less than 10% loss of activity within 15 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged isozyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
-
recombinant N-terminally thioredoxin and His6-tagged Os4BGlu18 from Escherichia coli by nickel affinity chromatography, and cleavage of the tag by enterokinase, followed by dialysis and ultrafiltration
to apparent homogeneity by ammonium sulfate fractionation and hydrophobic interaction chromatography, BGLU45 8.8fold and BGLU46 13.7fold purified
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in the Arabidopsis bglu45-2 (monolignol beta-glucosidase) mutant. bglu45-2 line exhibits elevated monolignol glucoside levels, but lower amounts of coniferin, syringin, and p-coumaryl alcohol glucoside. Os4BGlu14 complements the defect
expression in the Arabidopsis bglu45-2 (monolignol beta-glucosidase) mutant. bglu45-2 line exhibits elevated monolignol glucoside levels, but lower amounts of coniferin, syringin, and p-coumaryl alcohol glucoside. Os4BGlu16 complements the defect
expression in the Arabidopsis bglu45-2 (monolignol beta-glucosidase) mutant. bglu45-2 line exhibits elevated monolignol glucoside levels, but lower amounts of coniferin, syringin, and p-coumaryl alcohol glucoside. Os4BGlu18 complements the defect
gene BGLU1, sequence comparisons and phylogenetic tree, recombinant expression of GST-tagged enzyme in wild-type Arabidopsis thaliana and in Arabidopsis thaliana At1g61810 bglu45-2 mutant, recombinant transient overexpression of PbBGLU1 in Pyrus bretschneideri fruits leading to highly increased contents of lignin and stone cells in fruits, recombinant expression of GFP-tagged enzyme in Nicotiana tabacum showing that the expressed GFP-tagged PbBGLU1 is specifically distributed in the extracellular region, recombinant overexpression of GST-tagged isozyme in Escherichia coli strain BL21(DE3)
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gene bglu16, sequence comparisons and phylogenetic tree, expression of GST-tagged enzyme in wild-type Arabidopsis thaliana and in Arabidopsis thaliana At1g61810 bglu45-2 mutant, recombinant transient overexpression of PbBGLU16 in Pyrus bretschneideri fruits leading to increased contents of lignin and stone cells in fruits, recombinant expression of GFP-tagged enzyme in Nicotiana tabacum showing that the expressed GFP-tagged PbBGLU16 is specifically distributed in the extracellular region, recombinant overexpression of GST-tagged isozyme in Escherichia coli strain BL21(DE3)
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gene BGLU18, recombinant expression of N-terminally thioredoxin and His6-tagged Os4BGlu18 in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hsel, W.; Surholt, E.; Borgmann, E.
Characterization of beta-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension cultures
Eur. J. Biochem.
84
487-492
1978
Cicer arietinum
brenda
Hsel, W.; Fiedler-Preiss, A.; Borgmann, E.
Relationship of coniferin beta-glucosidase to lignification in various plant cell suspension cultures
Plant Cell Tissue Organ Cult.
1
137-148
1982
Petroselinum crispum, Triticum aestivum
-
brenda
Marcinowski, S.; Grisebach, H.
Enzymology of lignification. Cell-wall bound beta-glucosidase for coniferin from spruce (Picea abies) seedlings
Eur. J. Biochem.
87
37-44
1978
Picea abies
brenda
Leinhos, V.; Udagama-Randeniya, P.V.; Savidge, R.A.
Purification of an acidic coniferin-hydrolysing beta-glucosidase from developing xylem of Pinus banksiana
Phytochemistry
37
311-315
1994
Pinus banksiana
brenda
Watt, D.K.; Ono, H.; Hayashi, K.
Agrobacterium tumefaciens beta-glucosidase is also an effective beta-xylosidase, and has a high transglycosylation activity in the presence of alcohols
Biochim. Biophys. Acta
1385
78-88
1998
Agrobacterium tumefaciens
brenda
Dharmawardhana, D.P.; Ellis, B.E.; Carlson, J.E.
A beta-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin
Plant Physiol.
107
331-339
1995
Pinus contorta
brenda
Escamilla-Trevino, L.L.; Chen, W.; Card, M.L.; Shih, M.C.; Cheng, C.L.; Poulton, J.E.
Arabidopsis thaliana beta-glucosidases BGLU45 and BGLU46 hydrolyse monolignol glucosides
Phytochemistry
67
1651-1660
2006
Arabidopsis thaliana
brenda
Tsuyama, T.; Takabe, K.
Coniferin beta-glucosidase is ionically bound to cell wall in differentiating xylem of poplar
J. Wood Sci.
61
438-444
2015
Populus sieboldii x Populus grandidentata
-
brenda
Baiya, S.; Mahong, B.; Lee, S.K.; Jeon, J.S.; Ketudat Cairns, J.R.
Demonstration of monolignol beta-glucosidase activity of rice Os4BGlu14, Os4BGlu16 and Os4BGlu18 in Arabidopsis thaliana bglu45 mutant
Plant Physiol. Biochem.
127
223-230
2018
Oryza sativa Japonica Group (Q7XPY7), Oryza sativa Japonica Group (Q7XSK2), Oryza sativa Japonica Group (Q7XSK0)
brenda
Wang, H.; Zhang, Y.; Feng, X.; Peng, F.; Mazoor, M.A.; Zhang, Y.; Zhao, Y.; Han, W.; Lu, J.; Cao, Y.; Cai, Y.
Analysis of the beta-glucosidase family reveals genes involved in the lignification of stone cells in Chinese white pear (Pyrus bretschneideri Rehd.)
Front. Plant Sci.
13
852001
2022
Pyrus x bretschneideri
brenda
Baiya, S.; Pengthaisong, S.; Kitjaruwankul, S.; Ketudat, J.
Structural analysis of rice Os4BGlu18 monolignol beta-glucosidase
PLoS ONE
16
e0241325
2021
Oryza sativa Japonica Group (Q7XSK0)
brenda
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