Information on EC 3.2.1.38 - beta-D-fucosidase

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

EC NUMBER
COMMENTARY hide
3.2.1.38
-
RECOMMENDED NAME
GeneOntology No.
beta-D-fucosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-34-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achatina balteata
african snail
-
-
Manually annotated by BRENDA team
increased activity after acclimation with cellobiose
-
-
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
VTT E-011941, isolated from a sample of compost, containing paper machine fines, chicken manure, and wood bark
-
-
Manually annotated by BRENDA team
thai rosewood
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Ovis aries aries
sheep
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
glycoside hydrolase family 5 enzyme
-
-
Manually annotated by BRENDA team
glycoside hydrolase family 5 enzyme
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
show the reaction diagram
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
?
show the reaction diagram
-
amygdalin, low activity
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
100% activity
-
-
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
sophorose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
laminaribiose
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
-
increased activity after acclimation of bacteria to cellobiose medium
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
show the reaction diagram
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
59% activity compared to 2-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
show the reaction diagram
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
activity measured in whole fly homogenates, substrate concentration of 6 mM in citrate buffer
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
130% activity compared to 2-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
4% activity compared to 2-nitrophenyl beta-D-galactopyranoside
-
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
show the reaction diagram
Achatina balteata
-
-
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
6-bromo-2-naphthyl-beta-D-fucoside + H2O
6-bromo-2-naphthol + beta-D-fucose
show the reaction diagram
Achatina balteata
-
-
-
?
6-bromo-2-naphthyl-beta-D-galactoside + H2O
6-bromo-2-naphthol + beta-D-galactose
show the reaction diagram
Achatina balteata
-
-
-
?
6-bromo-2-naphthyl-beta-D-glucoside + H2O
6-bromo-2-naphthol + beta-D-glucose
show the reaction diagram
Achatina balteata
-
-
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
gentiobiose
-
?
beta-D-fucoside + H2O
beta-D-fucose + D-fucose
show the reaction diagram
beta-D-glucoside + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
20% more activity than on beta-D-fucoside, addition of D-glucose leads to formation of fucosylglucose as a product of transglycosylation reaction
-
?
colanic acid + H2O
?
show the reaction diagram
de-O-acetylated colanic acid + H2O
?
show the reaction diagram
-
substrate structure, substrate and product purification and analysis, overview, de-O-acetylation of the substrate increases the activity, while depyruvylation reduces it
-
-
?
de-pyruvylated colanic acid + H2O
?
show the reaction diagram
-
substrate structure, substrate and product purification and analysis, overview, de-O-acetylation of the substrate increases the activity, while depyruvylation reduces it
-
-
?
lactulose + H2O
D-galactose + D-fructose
show the reaction diagram
o-nitrophenyl-beta-D-galactoside + H2O
o-nitrophenol + beta-D-galactose
show the reaction diagram
Achatina balteata
-
-
-
?
o-nitrophenyl-beta-D-glucoside + H2O
o-nitrophenol + beta-D-glucose
show the reaction diagram
Achatina balteata
-
-
-
?
p-nitrophenyl-2-amino-2-deoxy-D-glucoside + H2O
p-nitrophenol + 2-amino-2-deoxy-D-glucose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-galactoside + H2O
p-nitrophenol + alpha-D-galactose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-L-arabinoside + H2O
p-nitrophenol + alpha-L-arabinose
show the reaction diagram
p-nitrophenyl-beta-D-fucoside + H2O
p-nitrophenol + beta-D-fucose
show the reaction diagram
p-nitrophenyl-beta-D-galactoside + H2O
p-nitrophenol + beta-D-galactose
show the reaction diagram
p-nitrophenyl-beta-D-glucoside + H2O
p-nitrophenol + beta-D-glucose
show the reaction diagram
p-nitrophenyl-beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
show the reaction diagram
p-nitrophenyl-beta-L-fucoside + H2O
p-nitrophenol + beta-L-fucose
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-fucoside + H2O
beta-D-fucose + D-fucose
show the reaction diagram
beta-D-glucoside + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
20% more activity than on beta-D-fucoside, addition of D-glucose leads to formation of fucosylglucose as a product of transglycosylation reaction
-
?
colanic acid + H2O
?
show the reaction diagram
-
degradation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
stimulation at 25 mM
K+
-
stimulation at 25 mM
KCl
the activity of the enzyme in 2.5 M and 4 M KCl relative to 4 M NaCl is 34% and 40%, respectively
Li+
-
stimulation at 25 mM
Mg2+
-
stimulation at 25 mM
Mn2+
-
stimulation at 25 mM
Na+
-
stimulation at 25 mM
NaCl
optimally active at 4 M NaCl
Sr2+
-
stimulation at 25 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-amino-1-deoxy-D-glucose
-
-
1-butanol
-
inhibition above 50 mM
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
1-propanol
-
inhibition above 50 mM
2-amino-2-deoxy-D-glucose
-
non-competitive inhibition
4-O-alpha-D-glucopyranosyl-D-glucose
Ovis aries aries
-
effective inhibitor at 50 mM
4-O-beta-D-galactopyranosyl-D-glucose
4-O-beta-D-glucopyranosyl-D-glucose
acetone
-
inhibition at low concentrations
acetonitrile
-
inhibition at low concentrations
arsenate
-
-
Ba2+
-
strong inhibition at 25 mM
beta-D-fructofuranosyl-alpha-D-glucopyranoside
-
-
beta-D-fucose
beta-D-galactose
beta-D-glucose
Ca2+
Achatina balteata
-
slight inhibition at 50 mM, beta-D-fucosidase II not affected
Co2+
Achatina balteata
-
50% inhibition at 50 mM for beta-D-fucosidase I, 22% inhibition for beta-D-fucosidase II
colanic acid
-
substrate inhibition at high concentrations
conduritol B epoxide
-
loss of activity towards both substrates beta-D-glucoside and beta-D-fucoside, inactivation followed an all-or-none-type of modification, inactivation reduced in the presence of Tris
CuSO4
-
64% inhibition at 1 mM, alpha-L-arabinosidase activity less affected
D-fucono-1,4-lactone
-
50% inhibition at 0.057 mM
D-fucono-gamma-lactone
D-Galactono-1,4-lactone
Dicarbonic acid diethyl ester
-
-
ethanol
-
inhibition above 50 mM
F-
Achatina balteata
-
slight inhibition at 50 mM, beta-D-fucosidase II less affected
Fe3+
-
complete inhibition at 25 mM
glucono 1,5-lactone
glycerol
interferes with enzyme activity
iodoacetate
-
strong inhibition
KI
Achatina balteata
-
lactose protects against inactivation
La3+
-
strong inhibition at 25 mM
methanol
-
inhibition above 50 mM
Mn2+
Achatina balteata
-
slight inhibition at 50 mM, beta-D-fucosidase II less affected
N-Acetylimidazole
Achatina balteata
-
progressive inactivation
N-bromosuccinimide
-
-
N-ethylmaleimide
-
strong inhibition
Ni2+
Achatina balteata
-
47% inhibition at 50 mM for beta-D-.fucosidase I, 25% inhibition at 50 mM for beta-D-fucosidase II
p-chloromercuribenzoate
p-nitrophenyl-beta-D-fucoside
-
competitive inhibition of beta-D-glucosidase
p-nitrophenyl-beta-D-glucoside
-
competitive inhibition of beta-D-fucosidase
Tetranitromethane
Achatina balteata
-
lactose protects against inactivation
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
beta-D-fructose
-
promotes beta-D-fucosidase activity, not beta-D-glucosidase activity
beta-D-fucose
-
activation at high concentrations, inhibition of beta-D-galactosidase and beta-D-glucosidase activity
beta-D-galactose
-
activation at high concentrations, inhibition of beta-D-galactosidase activity
beta-D-glucose
beta-D-mannose
-
promotes beta-D-fucosidase activity, not beta-D-glucosidase activity
beta-D-xylose
-
promotes beta-D-fucosidase activity, not beta-D-glucosidase activity
glycerol
-
activation
Salicin
-
activation
Serum albumin
-
activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.87
2-nitrophenyl beta-D-galactoside
pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity
2.56
4-nitrophenyl-beta-D-fucopyranoside
-
25°C, recombinant mutant H540V/N604T of beta-galactosidase, EC 3.2.1.22
0.26 - 8
p-nitrophenyl-beta-D-fucoside
0.25 - 3.5
p-nitrophenyl-beta-D-galactoside
0.1 - 5.37
p-nitrophenyl-beta-D-glucoside
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.5
4-nitrophenyl-beta-D-fucopyranoside
Escherichia coli
-
25°C, recombinant mutant H540V/N604T of beta-galactosidase, EC 3.2.1.22
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
partially purified enzyme
42
substrate: 2-nitrophenyl beta-D-galactosidepH 7.2, 22°C, the enzyme also shows beta-fucosidase activity
48
-
for beta-D-glucosidase activity
54.6
-
for beta-D-fucosidase activity
62
-
for beta-D-fucosidase activity
63
Achatina balteata
-
-
67.3
-
for beta-D-glucosidase activity
additional information
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.5
-
-
4.5 - 5.5
Ovis aries aries
-
-
5.7
-
assay at, pH-optimum estimated for
6 - 6.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
-
-
4.5 - 7.5
-
-
5 - 7
-
90% activity between pH 5-7, 70% activity remained at pH 4.5 and pH 8.5
5.2 - 5.6
Achatina balteata
-
for both beta-fucosidase I + II
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
51 - 52
Achatina balteata
-
beta-fucosidase I
54 - 55
Achatina balteata
-
beta-fucosidase II
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Achatina balteata
-
two forms, beta-fucosidase I and beta-fucosidase II
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
whole fly homogenates
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
SDS-PAGE, gel filtration
47000 - 48000
-
native gradient PAGE, SDS-PAGE
49000 - 51000
-
gel filtration, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
57000
-
SDS-PAGE, gel filtration
78000
2 * 78000, SDS-PAGE
105000 - 120000
Achatina balteata
-
beta-fucosidase II, gel filtration, ultracentrifugation
110000
Achatina balteata
-
1 * 110000, beta-fucosidase II, SDS-PAGE, gel filtration, ultracentrifugation
170000
Achatina balteata
-
1 * 170000 + 1 * 190000, beta-fucosidase I, SDS-PAGE, gel filtration, ultracentrifugation
180000
gel filtration
190000
Achatina balteata
-
1 * 170000 + 1 * 190000, beta-fucosidase I, SDS-PAGE, gel filtration, ultracentrifugation
300000 - 360000
Achatina balteata
-
beta-fucosidase I, gel filtration, ultracentrifugation
337000
-
2 * 337000, SDS-PAGE, the enzyme is part of a high-molecular weight multiprotein complex of at least 6 individual proteins
775000
-
native PAGE, the enzyme is part of a high-molecular weight multiprotein complex of at least 6 individual proteins
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50000, SDS-PAGE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Achatina balteata
-
contains galactose, glucose, mannose, fucose, 15.5%, w/w, for beta-fucosidase I, 7.5%, w/w, for beta-fucosidase II, contains hexosamines, 6.1%, w/w, for beta-fucosidase I, 5.2%, w/w, for beta-fucosidase II, no sialic acid found
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.2 A resolution, space group C222. The overall topology consists of a central catalytic (alpha/beta)8 barrel composed of residues Thr14 through Phe413 flanked by amino- and carboxy-terminal extensions that consist of sheets that form an independent beta-sandwich domain. This small beta domain associates with the backside of the catalytic domain, and two domains associate through hydrophobic interactions
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
rapid inactivation at 50°C within 10 min
136333
4.5
-
rapid inactivation below pH 4.5
136332
5 - 7.5
Achatina balteata
-
beta-fucosidase II
136330
5
-
protein precipitates below
714243
5.5 - 7
7.5
-
rapid inactivation above
136323
8.5
-
80% activity after 2 h at 25°C
136333
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
stable in 3 M NaCl for several days at room temperature
30
-
stable below
53
Achatina balteata
-
beta-fucosidase I, 60% loss of activity
55
Achatina balteata
-
beta-fucosidase II, 50% loss of activity
60
-
important inactivation at and above
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is irreversibly lost within min in low salt buffers, below 0.5 M
freezing and thawing inactivates
-
repeated freezing and thawing cycles don't affect fucosidase II, 30% loss of activity for beta-fucosidase I after 3 cycles
Achatina balteata
-
stable against repeated freezing and thawing cycles, activity unstable in SDS
Ovis aries aries
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
sorbitol
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol, 20 mM required during purification
-
136317
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% loss of activity when stored overnight
4°C, 0.01 M citrate pH 5.5, 0.02% sodium azide, several months
-
4°C, 18% loss of activity when stored overnight
4°C, 50 mM sodium acetate, pH 5.4, several months
Achatina balteata
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
17fold, partially, by anion exchange chromatography, and gel filtration
-
isoelectric focusing
-
partial
-
pH 8 treatment, 2step chromatography, activities towards beta-D-fucoside, beta-D-galactoside, beta-D-glucoside and alpha-L-arabinoside remain in the same protein peak
-
to homogeneity
Achatina balteata
-
to homogeneity by 2step chromatography technique
-
to homogeneity by anion exchange and gel chromatography
-
to homogeneity by aqueous two phase separation, chromatography steps
-
to homogeneity by chromatography steps
-
to homogeneity by isoelectric focusing and chromatography steps
-
to homogeneity by several chromatography steps
-
to homogeneity by several chromatography steps, isoelectric focusing
Ovis aries aries
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli LMG194 cells
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E205A
-
complete loss of activity
E239A
-
complete loss of activity
E205A
-
complete loss of activity
-
E239A
-
complete loss of activity
-
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
50% recovery for beta-fucosidase II, 25% recovery for beta-fucosidase I after treatment with 6 M urea
Achatina balteata
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
synthesis
-
synthesis of fucosylsugars using the transglycosylation activity