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Information on EC 3.2.1.51 - alpha-L-fucosidase
for references in articles please use BRENDA:EC3.2.1.51
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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
3.2.1.51 alpha-L-fucosidase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 3.2.1.51
- lysosomal
- hydrolases
- oligosaccharide
- glycosidases
- fucosidosis
- alpha-d-mannosidase
- beta-d-galactosidase
- fucose
-
fucosylated
- lectin
-
sialic
- beta-d-glucuronidase
- neuraminidase
-
n-acetyl-beta-d-glucosaminidase
- beta-n-acetylglucosaminidase
- beta-d-glucosidase
- glycoconjugates
- alpha-d-galactosidase
-
fucose-containing
-
4-methylumbelliferyl
- alpha-d-glucosidase
- alpha-l-fucose
- angiokeratomas
-
fucosyltransferase
- i-cell
-
transglycosylation
-
exoglycosidase
- mucolipidosis
- hexosaminidase
- diagnostics
- diffusum
-
spaniel
- beta-mannosidase
- analysis
- almond
-
corporis
- medicine
- synthesis
-
springer
- food industry
-
intralysosomal
- arylsulphatase
- alpha-gal
- beta-n-acetylhexosaminidase
- europaeus
showSynonyms
alpha-l-fucosidase, acid hydrolase, fuca1, serum alpha-l-fucosidase, serum afu, alpha-fuc, fuca2, alf1_wf, alpha-l-fucosidase i, alphafuc, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alfA
alfB
alfC
alpha-fuc
alpha-fucosidase
-
-
-
-
alpha-L-fucosidase
alpha-L-fucosidase 2
alpha-L-fucosidase I
alpha-L-fucosidase iso2
Alpha-L-fucoside fucohydrolase
alpha-L-fucoside fucohydrolase 2
BcFucA
BF0028
BF0810
BF3242
BF3591
bfo_2737
entfuc
Eo0918
Eo3066
Eo3812
FucA
Fuca1
Fuca2
FucFA
OUC-Jdch16
TfFuc1
Alpha-L-fucoside fucohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an alpha-L-fucoside + H2O = L-fucose + an alcohol
-
-
-
-
an alpha-L-fucoside + H2O = L-fucose + an alcohol
the enzyme catalyses the transfer of L-fucose from donor structures such as alpha-L FucpOpNP and alpha-L-FucpF to various GlcpNac derivates and glCP, forming alpha-(1-3)linkages
-
an alpha-L-fucoside + H2O = L-fucose + an alcohol
the enzyme cleaves alpha1-6-, alpha1-3-, alpha1-4- and alpha1-2-O-fucolsyl bonds in fucosylated oligosaccharides
-
an alpha-L-fucoside + H2O = L-fucose + an alcohol
the enzyme cleaves alpha1-6-, alpha1-3-, alpha1-4- and alpha1-2-O-fucolsyl bonds in fucosylated oligosaccharides
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
xyloglucan degradation II (exoglucanase)
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SYSTEMATIC NAME
IUBMB Comments
alpha-L-fucoside fucohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9037-65-4
-
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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-acetamido-2-deoxy-3-O-(alpha-L-fucopyranosyl)-D-glucopyranose + H2O
?
Substrates: -
Products: -
Products: -
?
2-acetamido-2-deoxy-4-O-(alpha-L-fucopyranosyl)-D-glucopyranose + H2O
?
Substrates: -
Products: -
Products: -
?
2-acetamido-2-deoxy-6-O-(alpha-L-fucopyranosyl)-D-glucopyranose + H2O
?
Substrates: -
Products: -
Products: -
?
2-chloro-4-nitrophenyl alpha-L-fucopyranoside + H2O
2-chloro-4-nitrophenol + L-fucose
Substrates: pH 6.8, 37°C
Products: -
Products: -
?
2-chloro-4-nitrophenyl-alpha-L-fucopyranoside + H2O
2-chloro-4-nitrophenol + alpha-L-fucopyranoside
A0A8A6LMS6, A0A8A6LXU3, A0A8A6LSW7, A0A8A6LM44
Substrates: -
Products: -
Products: -
?
2-deoxy-2-fluoro-alpha-L-fucosyl fluoride + H2O
fluoride + 2-deoxy-2-fluoro-alpha-L-fucose
Substrates: -
Products: -
Products: -
?
2-fluoro-4-nitrophenyl alpha-L-fucopyranoside + H2O
2-fluoro-4-nitrophenol + L-fucose
Substrates: pH 6.8, 37°C
Products: -
Products: -
?
2-methyl-4-nitrophenyl alpha-L-fucopyranoside + H2O
2-methyl-4-nitrophenol + L-fucose
Substrates: pH 6.8, 37°C
Products: -
Products: -
?
2-nitrophenyl alpha-L-fucopyranoside + H2O
2-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
3-fucosyl-N,N'-diacetylchitobiose + H2O
?
Substrates: 7.9% compared to the activity with 4-nitrophenyl alpha-L-fucoside
Products: -
Products: -
?
3-fucosyllactose + H2O
alpha-L-fucose + lactose
Substrates: 2.2% compared to the activity with 4-nitrophenyl alpha-L-fucoside
Products: -
Products: -
?
3-fucosyllactose + H2O
L-fucose +
-
Substrates: cleavage of alpha-1,3 bond, low efficiency
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucopyranose
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl 2-sulfo-alpha-L-fucopyranoside + H2O
4-nitrophenol + 2-sulfo-alpha-L-fucopyranose
-
Substrates: hydrolysis at 1.9% compared to 4-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-Glc + H2O
alpha-L-fucose + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-Glc
-
Substrates: hydrolysis at 1.6% compared to 4-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-Fuc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc + H2O
alpha-L-fucose + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-Glc
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
Substrates: sodium acetate buffer 50 mM, pH 5.0, 37°C
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside
?
-
Substrates: assay at pH 4.5, 37°C for 3 h, reaction stopped by addition of borate buffer
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + N-acetyl-D-glucosamine + H2O
4-nitrophenol + alpha-L-Fuc-(1-3)-D-GlcNAc
4-nitrophenyl-alpha-L-fucopyranoside + N-acetyl-D-glucosamine + H2O
4-nitrophenol + alpha-L-fucose-(1-3)-D-GlcNAc
-
Substrates: catalytic residues Asp242, Glu58, and Glu292
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucoside + H2O
alpha-L-fucopyranose + 4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
6-fucosyl-N,N'-diacetylchitobiose + H2O
?
Substrates: 1.2% compared to the activity with 4-nitrophenyl alpha-L-fucoside
Products: -
Products: -
?
6-O-alpha-L-Fuc-N,N'-diacetylchitobiose + H2O
alpha-L-fucose + N,N'-diacetylchitobiose
Substrates: -
Products: -
Products: -
?
6-O-alpha-L-fucopyranosyl-N-acetylglucosamine + H2O
alpha-L-fucopyranose + N-acetyl-glucosamine
-
Substrates: Fuc-alpha-1,6-GlcNAc-linkage most susceptible
Products: -
Products: -
?
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-3)-D-GalNAc + H2O
alpha-L-fucose + beta-D-Gal-(1-3)-D-GalNAc
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me + H2O
alpha-L-fucose + beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me
alpha-L-Fuc-(1-2)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
-
Substrates: same yield of transglycosylation and hydrolysis products
Products: -
Products: -
?
alpha-L-Fuc-(1-3)-a-L-Fuc-O-4-NP + H2O
?
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-3)-alpha-L-Fuc-O-4-nitrophenyl ester + H2O
?
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-3)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
-
Substrates: slower hydrolysis than for the alpha-(1-6)- or alpha-(1-2)-isomers, transglycosylation activity
Products: -
Products: -
?
alpha-L-Fuc-(1-3)-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-4)-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-6)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-6)-D-GlcNAc + D-galactose
-
Substrates: same yield of transglycosylation and hydrolysis products
Products: -
Products: -
?
alpha-L-Fuc-(1-6)-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc-OMe + H2O
alpha-L-fucose + beta-D-Gal-(1->4)-beta-D-GlcNAc-OMe
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1->4)-GlcNAc-poly-acrylamide polymer + H2O
alpha-L-fucose + GlcNAc-poly-acrylamide polymer
Substrates: -
Products: -
Products: -
?
alpha-L-fucopyranosyl fluoride + methyl 2-(acetylamino)-2-deoxy-alpha-D-glucopyranoside
methyl 2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-alpha-D-glucopyranoside + fluoride
-
Substrates: -
Products: 13% yield based on the donor substrate
Products: 13% yield based on the donor substrate
?
alpha-L-fucopyranosyl fluoride + N-acetylglucosamine
2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-alpha-D-glucopyranose + fluoride
-
Substrates: -
Products: 7% yield based on the donor substrate
Products: 7% yield based on the donor substrate
?
alpha-L-fucopyranosyl fluoride + prop-2-en-1-yl 2-(acetylamino)-2-deoxy-alpha-D-glucopyranoside
prop-2-en-1-yl 2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-alpha-D-glucopyranoside + fluoride
-
Substrates: -
Products: 8% yield based on the donor substrate
Products: 8% yield based on the donor substrate
?
alpha-L-fucopyranosyl fluoride + prop-2-en-1-yl 2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
prop-2-en-1-yl 2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-glucopyranoside + fluoride
-
Substrates: -
Products: 34% yield based on the donor substrate
Products: 34% yield based on the donor substrate
?
alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-D-galactitol + H2O
alpha-L-fucose + beta-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-D-galactitol
-
Substrates: -
Products: -
Products: -
?
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose + H2O
alpha-L-fucose + D-galactose
Substrates: the enzyme does not hydrolyze other fucosyloligosaccharides or 4-nitrophenyl-alpha-L-fucoside
Products: -
Products: -
?
alpha-L-fucosyl fluoride + H2O
fluoride + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
antigen H type II trisaccharide + H2O
?
-
Substrates: -
Products: -
Products: -
?
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc + H2O
alpha-L-fucose + beta-D-Gal-(1-3)-D-GlcNAc
Substrates: slightly hydrolyzed, since fucose monosaccharide is detected after the reaction
Products: -
Products: -
?
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc + H2O
alpha-L-fucose + beta-D-Gal-(1->3)-D-GlcNAc
Substrates: i.e. Le(x) trisaccharide
Products: -
Products: -
?
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-OMe + H2O
?
Substrates: -
Products: -
Products: -
?
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc + H2O
alpha-L-fucose + beta-D-Gal-(1->4)-D-GlcNAc
Substrates: i.e. Le(a) trisaccharide
Products: -
Products: -
?
beta-D-GlcNAc-(1-4)-(alpha-L-Fuc-(1-6))-D-GlcNAc + H2O
alpha-L-fucose + beta-D-GlcNAc-(1-4)-D-GlcNAc
Fuc-alpha-(1-2)-Fuc-beta-4-nitrophenol + H2O
alpha-L-fucose + Fuc-beta-4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GalNAc-alpha-phenol + H2O
alpha-L-fucose + Gal-beta-(1-3)-N-acetyl-galactosaminyl-phenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
Fuc-alpha-(1-2)-Gal-beta-(1-3)-[Fuc-alpha-(1-4)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-[Fuc-alpha-(1-4)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: lacto-N-difucohexaitol I, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + alpha-L-fucose
Fuc-alpha-(1-2)-Gal-beta-4-nitrophenol + H2O
alpha-L-fucose + beta-galactosyl-4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Glc + H2O
alpha-L-fucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Xyl + H2O
alpha-L-fucose + D-xylose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-[Gal-alpha-(1-3)]-Gal-beta-phenol + H2O
alpha-L-fucose + Gal-alpha-(1-3)-Gal-beta-phenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-Glc + H2O
alpha-L-fucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc-beta-O(CH2)6NHCOCF3 + H2O
alpha-L-fucose + GlcNAc-beta-O(CH2)6NHCOCF3
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc-beta-phenol + H2O
alpha-L-fucose + N-acetyl-glucosaminyl-beta-phenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc-phenol + H2O
alpha-L-fucose + N-acetyl-glucosaminyl-beta-phenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-4)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-4)-GlcNAc-beta-phenol + H2O
alpha-L-fucose + beta-N-acetyl-glucosaminyl-phenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-4)-[Gal-beta-(1-3)]-GlcNAc-beta-phenol + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-phenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc-4-nitrophenol + H2O
alpha-L-fucose + GlcNAc-4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc-beta-Asn + H2O
alpha-L-fucose + N-acetyl-D-glucosaminyl-Asn
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-[Gal-beta-(1-3)]-GlcNAc-beta-OCH3 + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-OCH3
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1->2)-Gal-beta-(1->3)-[Fuc-alpha-(1->6)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc + H2O
alpha-L-fucose + Gal-beta-(1->3)-[Fuc-alpha-(1->6)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1->2)-Gal-beta-(1->3)-[Fuc-alpha-(1->6)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc + H2O + H2O
alpha-L-fucose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc + H2O
Bacillus fulminans
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-1,2-Gal + H2O
alpha-L-fucose + galactose
Substrates: -
Products: -
Products: -
?
Fuc-alpha-1,4-GlcNAc + H2O
alpha-L-fucose + N-acetyl D-glucosamine
-
Substrates: activity with alpha-L-fucosidase BF3242 (5.1%) and BF3591 (12.1%)
Products: -
Products: -
?
Fuc-alpha-1,6-GlcNAc + H2O
alpha-L-fucose + N-acetyl D-glucosamine
-
Substrates: activity with alpha-L-fucosidase BF3242 (9.3) and BF3591 (13.3)
Products: -
Products: -
?
fucose residues from fucose-containing oligosaccharide chains on porcine gastric mucin + H2O
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Gal-beta-(1-4)-GlcNAc-[Fuc-alpha-(1-4)]-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-4)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
GlcNAc-beta-(1-2)-Man-alpha-(1-6)-[GlcNAc-beta-(1-2)-Man-alpha-(1-3)]-[Xyl-beta-(1-2)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-pyridylaminoside + H2O
alpha-L-fucose + [GlcNAc-beta-(1-2)-Man-alpha-(1-6)]-[GlcNAc-beta-(1-2)-Man-alpha-(1-3)]-[Xyl-beta-(1-2)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-pyridylaminoside
-
Substrates: not completely hydrolysed due to steric hinderance by beta-(1-2)-GlcNAc residues
Products: -
Products: -
?
glycopeptide from desialyzed porcine submaxillary mucin + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: -
Products: -
Products: -
?
glycosphingolipid + H2O
alpha-L-fucose + ?
-
Substrates: blood-group active types B and H
Products: -
Products: -
?
gp120 oligosaccharide + H2O
alpha-L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
gp120 oligosaccharides + H2O
alpha-L-fucose + ?
-
Substrates: released from recombinant CHO cell-produced gp120, glycoproteins containing fucose in alpha-1,3- and alpha-1,6-linkages are no substrates
Products: -
Products: -
?
lacto-N-difucohexaose I + H2O
L-fucose + ?
-
Substrates: cleavage of alpha-1,4 bond
Products: -
Products: -
?
lacto-N-difucohexaose II + H2O
L-fucose + ?
-
Substrates: cleavage of alpha-1,4 bond
Products: -
Products: -
?
lacto-N-fucopentaitol II + H2O
alpha-L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
lactoferrin + H2O
alpha-L-fucose + ?
-
Substrates: low activity
Products: -
Products: -
?
Lewis Y antigen + H2O
alpha-L-fucose + ?
A0A8A6LMS6, A0A8A6LXU3, A0A8A6LSW7, A0A8A6LM44
Substrates: -
Products: -
Products: -
?
LH-beta peptic glycopeptide + H2O
alpha-L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
m-nitrophenyl alpha-L-fucopyranoside + H2O
m-nitrophenol + L-fucose
Substrates: pH 6.8, 37°C
Products: -
Products: -
?
Man-beta-(1-6)-[Man-alpha-(1-3)-Xyl-beta-(1-2)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-pyridylaminoside + H2O
alpha-L-fucose + Man-beta-(1-6)-[Man-alpha-(1-3)-Xyl-beta-(1-2)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-pyridylaminoside
-
Substrates: -
Products: -
Products: -
?
meconium X-1 + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: low activity
Products: -
Products: -
?
mono-sialylated-galactosylated biantennary N-glycan-core-substituted with alpha-(1->6)-linked fucose + H2O
L-fucose + ?
orosomucoid + H2O
alpha-L-fucose + ?
-
Substrates: low activity, higher activity if desialyzed
Products: -
Products: -
?
p-cyanophenyl alpha-L-fucopyranoside + H2O
p-cyanophenol + L-fucose
Substrates: pH 6.8, 37°C
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucopyranoside + methyl 2-(acetylamino)-2-deoxy-alpha-D-glucopyranoside
methyl 2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-alpha-D-glucopyranoside + p-nitrophenol
-
Substrates: -
Products: 29% yield based on the donor substrate
Products: 29% yield based on the donor substrate
?
p-nitrophenyl alpha-L-fucopyranoside + prop-2-en-1-yl 2-(acetylamino)-2-deoxy-alpha-D-glucopyranoside
prop-2-en-1-yl 2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-alpha-D-glucopyranoside + p-nitrophenol
-
Substrates: -
Products: 34% yield based on the donor substrate
Products: 34% yield based on the donor substrate
?
p-nitrophenyl alpha-L-fucopyranoside + prop-2-en-1-yl 2-(acetylamino)-2-deoxy-beta-D-glucopyranoside
prop-2-en-1-yl 2-(acetylamino)-2-deoxy-3-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-glucopyranoside + p-nitrophenol
-
Substrates: -
Products: 25% yield based on the donor substrate
Products: 25% yield based on the donor substrate
?
p-nitrophenyl-alpha-L-fucoside + H2O
L-fucose + p-nitrophenol
Substrates: the enzyme has low transglycosylation properties
Products: -
Products: -
?
phenyl alpha-L-fucopyranoside + H2O
phenol + L-fucose
Substrates: pH 6.8, 37°C
Products: -
Products: -
?
porcine submaxillary mucine, desialyzed + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: -
Products: -
Products: -
?
propyl alpha-L-fucopyranoside + H2O
propanol + alpha-L-fucopyranose
Substrates: -
Products: -
Products: -
?
propyl alpha-L-fucopyranosyl-(1->2)-alpha-L-fucopyranoside + H2O
?
Substrates: -
Products: -
Products: -
?
propyl alpha-L-fucopyranosyl-(1->3)-alpha-L-fucopyranoside + H2O
?
Substrates: -
Products: -
Products: -
?
propyl alpha-L-fucopyranosyl-(1->4)-alpha-L-fucopyranoside + H2O
?
Substrates: -
Products: -
Products: -
?
submaxilary mucin trisaccharide + H2O
alpha-L-fucose + disaccharide
-
Substrates: -
Products: -
Products: -
?
Xyl-beta-(1-2)-Man-beta-(1-4)-GlcNAc-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-pyridylaminoside + H2O
alpha-L-fucose + Xyl-beta-(1-2)-Man-beta-(1-4)-GlcNAc-beta-pyridylaminoside
-
Substrates: -
Products: -
Products: -
?
Xylalpha(1-6)Glcbeta(1-4)[Xylalpha(1-6)]Glcbeta(1-4)[Fucalpha(1-2)Galbeta(1-2)Xylalpha(1-6)]Glcbeta(1-4)Glc + H2O
Xylalpha(1-6)Glcbeta(1-4)[Xylalpha(1-6)]Glcbeta(1-4)[Galbeta(1-2)Xylalpha(1-6)]Glcbeta(1-4)Glc + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-[Fuc-alpha-(1->6)]GlcNAc + H2O
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + alpha-L-fucose
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: low activity
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: -
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: -
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: alpha-fucosidase I, cleavage of alpha-(1-3)- and alpha-(1-4)-linkages in oligosaccharides and glycopeptides, doesn't cleave Fuc-alpha-(1-2)-Gal- and Fuc-alpha-(1-6)-GlcNAc-linkages
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: alpha-fucosidase II highly active
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Substrates: -
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Substrates: -
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Substrates: 10.5% compared to the activity with 4-nitrophenyl alpha-L-fucoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Substrates: -
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Flavobacterium algicola 12076
Substrates: -
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: 4.03% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: 15.1% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: 6.49% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Lacticaseibacillus rhamnosus INIA P603
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: 4.03% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Lacticaseibacillus rhamnosus INIA P603
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: 15.1% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Lacticaseibacillus rhamnosus INIA P603
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: 6.49% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Substrates: -
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Pedobacter sp. CAU209
A0A7D3USC4
Substrates: 39% compared to the activity with 4-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
Pedobacter sp. CAU209
A0A7D3USC4
Substrates: 13.9% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
2'-fucosyllactose + H2O
alpha-L-fucose + lactose
A0A8A6LMS6, A0A8A6LXU3, A0A8A6LSW7, A0A8A6LM44
Substrates: -
Products: -
Products: -
?
3'-fucosyllactose + H2O
alpha-L-fucose + lactose
Pedobacter sp. CAU209
A0A7D3USC4
Substrates: 37.8% compared to the activity with 4-nitrophenyl alpha-L-fucopyranoside
Products: -
Products: -
?
3'-fucosyllactose + H2O
alpha-L-fucose + lactose
A0A8A6LMS6, A0A8A6LXU3, A0A8A6LSW7, A0A8A6LM44
Substrates: -
Products: -
Products: -
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: very low activity
Products: -
Products: -
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: low activity
Products: -
Products: -
?
3-fucosyllactose + H2O
L-fucose + ?
-
Substrates: cleavage of alpha-1,3 bond
Products: -
Products: -
?
3-fucosyllactose + H2O
L-fucose + ?
-
Substrates: cleavage of alpha-1,3 bond
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: induces acrosome reaction of guinea pig spermatozoa
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: responsible for the intralysosomal hydrolysis of fucose-containing glypeptide and glycolipids
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: involved in sperm-egg interactions
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-Fuc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc + H2O
alpha-L-fucose + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-Glc
-
Substrates: hydrolysis at 1.7% compared to 4-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-Fuc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc + H2O
alpha-L-fucose + 4-nitrophenyl beta-D-Gal-(1->4)-beta-D-Glc
-
Substrates: hydrolysis at 3.7% compared to 4-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
KXI90766.1
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Bacillus cereus 2-8
KXI90766.1
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Flavobacterium algicola 12076
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Lacticaseibacillus rhamnosus INIA P603
QUH15933.1, QUH16573.1, QUH16649.1
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: the enzyme shows a low transglycosylation potential
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Paenibacillus thiaminolyticus CCM 3599
Substrates: the enzyme shows a low transglycosylation potential
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Pedobacter sp. CAU209
A0A7D3USC4
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
A0A8A6LMS6, A0A8A6LXU3, A0A8A6LSW7, A0A8A6LM44
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Substrates: the enzyme shows a low transglycosylation potential
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
Substrates: transfucosylation of lactose occurrs at high substrate concentrations when reaction time is elongated to several days. The structure of the product trisaccharide is defined as 1-fucosyllactose, where fucose is alpha-linked to the anomeric carbon of the beta-glucose moiety of lactose
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
Substrates: transfucosylation of lactose occurrs at high substrate concentrations when reaction time is elongated to several days. The structure of the product trisaccharide is defined as 1-fucosyllactose, where fucose is alpha-linked to the anomeric carbon of the beta-glucose moiety of lactose
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: activity with alpha-L-fucosidase BF0028, BF0810, BF3242 and BF3591
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: activity with alpha-L-fucosidase BF0028, BF0810, BF3242 and BF3591
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
WP_057784261.1
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
Formosa algae KMM 3553T
WP_057784261.1
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: can cleave alpha-(1-2)-, alpha-(1-3)- and alpha-(1-4)- fucosyl linkages
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
Pedobacter sp. CAU209
A0A7D3USC4
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: can cleave alpha-(1-2)-, alpha-(1-3)- and alpha-(1-4)- fucosyl linkages
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
Substrates: substrate incubated with plasma sample of breast cancer patients treated with anti-cancer monoclonal antibody trastuzumbal
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucopyranoside + N-acetyl-D-glucosamine + H2O
4-nitrophenol + alpha-L-Fuc-(1-3)-D-GlcNAc
-
Substrates: transglycosylation activity
Products: no other isomer
Products: no other isomer
?
4-nitrophenyl-alpha-L-fucopyranoside + N-acetyl-D-glucosamine + H2O
4-nitrophenol + alpha-L-Fuc-(1-3)-D-GlcNAc
-
Substrates: transglycosylation activity
Products: no other isomer
Products: no other isomer
?
4-nitrophenyl-alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: activity measured in whole fly homogenates, substrate concentration of 6 mM in citrate buffer
Products: -
Products: -
?
4-nitrophenyl-alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-3)-D-GalNAc + H2O
alpha-L-fucose + beta-D-Gal-(1-3)-D-GalNAc
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-3)-D-GalNAc + H2O
alpha-L-fucose + beta-D-Gal-(1-3)-D-GalNAc
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me + H2O
alpha-L-fucose + beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me
-
Substrates: -
Products: -
Products: -
?
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me + H2O
alpha-L-fucose + beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me
-
Substrates: -
Products: -
Products: -
?
alpha-L-fucosyl fluoride + H2O
alpha-L-fucose + fluoride
-
Substrates: -
Products: -
Products: -
?
alpha-L-fucosyl fluoride + H2O
alpha-L-fucose + fluoride
Substrates: -
Products: -
Products: -
?
antigen H disaccharide + H2O
? + alpha-L-fucose
-
Substrates: structure: Fuc-alpha-1,2-Gal. Activity with alpha-L-fucosidase BF3242 (6.9%) and BF3591 (15.1%)
Products: -
Products: -
?
antigen H disaccharide + H2O
? + alpha-L-fucose
-
Substrates: structure: Fuc-alpha-1,2-Gal. Activity with alpha-L-fucosidase BF3242 (6.9%) and BF3591 (15.1%)
Products: -
Products: -
?
beta-D-GlcNAc-(1-4)-(alpha-L-Fuc-(1-6))-D-GlcNAc + H2O
alpha-L-fucose + beta-D-GlcNAc-(1-4)-D-GlcNAc
-
Substrates: -
Products: -
Products: -
?
beta-D-GlcNAc-(1-4)-(alpha-L-Fuc-(1-6))-D-GlcNAc + H2O
alpha-L-fucose + beta-D-GlcNAc-(1-4)-D-GlcNAc
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Bacillus fulminans
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: alpha-fucosidase I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: only hydrolysed by alpha-L-fucosidase II
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
Bacillus fulminans
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: only hydrolysed by alpha-fucosidase II
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-sorbitol + H2O
alpha-L-fucose + Gal-beta-(1-4)-sorbitol
-
Substrates: alpha-fucosidase II, does not cleave alpha-(1-4)-GlcNAc, alpha-(1-3)-GlcNAc or alpha-(1-6)-GlcNAc-linkages and does not act on lacto-N-fucopentaoitol I which has a Fuc-alpha-(1-2)-Gal-group
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-sorbitol + H2O
alpha-L-fucose + Gal-beta-(1-4)-sorbitol
-
Substrates: alpha-fucosidase II, does not cleave alpha-(1-4)-GlcNAc-, alpha-(1-3)-GlcNAc- or alpha-(1-6)-GlcNAc-linkages and does not act on lacto-N-fucopentaoitol I, which has a Fuc-alpha-(1-2)-Gal-group
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: NaBH4-reduced oligosaccharide, hydrolysis of Fuc-alpha-(1-2)-Gal- and Fuc-alpha-(1-4)-GlcNAc- and Fuc-alpha-(1-6)-GlcNAc- linkages but hardly the Fuc-alpha-(1-3)-GlcNAc-linkage
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: hydrolysis of Fuc-alpha-(1-2)-Gal- and Fuc-alpha-(1-4)-GlcNAc- and Fuc-alpha-(1-6)-GlcNAc- linkages but hardly the Fuc-alpha-(1-3)-GlcNAc-linkage
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: slow hydrolysis rate
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: slow hydrolysis rate
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
A0A8A6LMS6, A0A8A6LXU3, A0A8A6LSW7, A0A8A6LM44
Substrates: -
Products: -
Products: -
?
Fuc-alpha-1,3-GlcNAc + H2O
alpha-L-fucose + N-acetyl D-glucosamine
-
Substrates: activity with alpha-L-fucosidase BF3242 (13.4%) and BF3591 (98.7%)
Products: -
Products: -
?
Fuc-alpha-1,3-GlcNAc + H2O
alpha-L-fucose + N-acetyl D-glucosamine
-
Substrates: activity with alpha-L-fucosidase BF3242 (13.4%) and BF3591 (98.7%)
Products: -
Products: -
?
fucose residues from fucose-containing oligosaccharide chains on porcine gastric mucin + H2O
?
-
Substrates: fase I, not: fase II
Products: -
Products: -
?
fucose residues from fucose-containing oligosaccharide chains on porcine gastric mucin + H2O
?
-
Substrates: fase I, not: fase II
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity for alpha-L-fucosidase II
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-(1-4)-GlcNAc-[Fuc-alpha-(1-4)]-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-4)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose III
Products: -
Products: -
?
Gal-beta-(1-4)-GlcNAc-[Fuc-alpha-(1-4)]-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-4)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose III
Products: -
Products: -
?
Gal-beta-(1-4)[Fuc-alpha-(1-3)]-Glc + H2O
Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: NaBH4-reduced oligosaccharide, very slow hydrolysis
Products: -
Products: -
?
Gal-beta-(1-4)[Fuc-alpha-(1-3)]-Glc + H2O
Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: very slow hydrolysis, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-1,3-(Fuc-alpha-1,4)GlcNAc + H2O
? + alpha-L-fucose
-
Substrates: activity with alpha-L-fucosidase BF3242 (4.9%) and BF3591 (13.4%)
Products: -
Products: -
?
Gal-beta-1,3-(Fuc-alpha-1,4)GlcNAc + H2O
? + alpha-L-fucose
-
Substrates: activity with alpha-L-fucosidase BF3242 (4.9%) and BF3591 (13.4%)
Products: -
Products: -
?
Gal-beta-1,4-(Fuc-alpha-1,3)GlcNAc + H2O
? + alpha-L-fucose
-
Substrates: activity with alpha-L-fucosidase BF3242 (4.3%) and BF3591 (100%)
Products: -
Products: -
?
Gal-beta-1,4-(Fuc-alpha-1,3)GlcNAc + H2O
? + alpha-L-fucose
-
Substrates: activity with alpha-L-fucosidase BF3242 (4.3%) and BF3591 (100%)
Products: -
Products: -
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
-
Substrates: -
Products: -
Products: -
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
-
Substrates: low activity
Products: -
Products: -
?
gastric mucin + H2O
alpha-L-fucose + ?
-
Substrates: porcine
Products: -
Products: -
?
gastric mucin + H2O
alpha-L-fucose + ?
-
Substrates: porcine
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: from meconium H-1, H-2 and X-1
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: desialyzed porcine submaxillry mucin
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: desialyzed porcine submaxillary mucin
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: meconium H-1, H-2 and X-1
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
-
Substrates: cellular source of substrate
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
-
Substrates: not active on native glycoproteins
Products: -
Products: -
?
glycoprotein + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: specifically hydrolyses terminal alpha-(1-2)-fucosidic bonds of glycoproteins, glycopeptides and oligosaccharides
Products: -
Products: -
?
glycoprotein + H2O
alpha-L-fucose + ?
-
Substrates: salivary human type H
Products: -
Products: -
?
IgG Fc peptide + H2O
alpha-L-fucose + ?
-
Substrates: from human, rabbit, horse
Products: -
Products: -
?
IgG Fc peptide + H2O
alpha-L-fucose + ?
-
Substrates: human, rabbit, horse
Products: -
Products: -
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
-
Substrates: low activity for alpha-L-fucosidase II
Products: -
Products: -
?
lacto-N-fucopentaose + H2O
L-fucose +
-
Substrates: cleavage of alpha-1,3 bond
Products: -
Products: -
?
lacto-N-fucopentaose + H2O
L-fucose +
-
Substrates: cleavage of alpha-1,3 bond, low efficiency
Products: -
Products: -
?
lacto-N-fucopentaose + H2O
L-fucose +
-
Substrates: cleavage of alpha-1,3 bond
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: preferentially hydrolysed by alpha-fucosidase II
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: alpha-fucosidase II
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
methyl alpha-L-fucopyranoside + H2O
methanol + alpha-L-fucose
-
Substrates: or methanol or ethanol as acceptor
Products: -
Products: -
?
methyl alpha-L-fucopyranoside + H2O
methanol + alpha-L-fucose
-
Substrates: or methanol or ethanol as acceptor
Products: -
Products: -
?
mono-sialylated-galactosylated biantennary N-glycan-core-substituted with alpha-(1->6)-linked fucose + H2O
L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
mono-sialylated-galactosylated biantennary N-glycan-core-substituted with alpha-(1->6)-linked fucose + H2O
L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
oligosaccharide + H2O
alpha-L-fucose + ?
-
Substrates: di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
Products: -
Products: -
?
oligosaccharide + H2O
alpha-L-fucose + ?
-
Substrates: di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
Products: -
Products: -
?
oligosaccharides + H2O
alpha-L-fucose + ?
-
Substrates: di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
Products: -
Products: -
?
oligosaccharides + H2O
alpha-L-fucose + ?
-
Substrates: di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucopyranose
-
Substrates: -
Products: anomeric configuration of the produced fucopyranse
Products: anomeric configuration of the produced fucopyranse
?
p-nitrophenyl alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucopyranose
-
Substrates: or methanol or ethanol as acceptor
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucopyranose
-
Substrates: or methanol or ethanol as acceptor
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: fase II, not: fase I
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: fase II, not: fase I
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: fase II, not: fase I
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
saliva + H2O
alpha-L-fucose + ?
-
Substrates: Ulex europaeus
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: desialyzed and not, desialyzed mucine best substrate tested
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: one form, optimally active at pH 5, not able to hydrolyse p-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
thyroglobulin + H2O
alpha-L-fucose + ?
-
Substrates: from bovine
Products: -
Products: -
?
thyroglobulin + H2O
alpha-L-fucose + ?
-
Substrates: bovine
Products: -
Products: -
?
thyroglobulin + H2O
alpha-L-fucose + ?
-
Substrates: hydrolysis only after pronase or neuraminidase treatment
Products: -
Products: -
?
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-[Fuc-alpha-(1->6)]GlcNAc + H2O
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + alpha-L-fucose
-
Substrates: subscript OT is used to indicate NaBH4-reduced oligosaccharide
Products: -
Products: -
?
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-[Fuc-alpha-(1->6)]GlcNAc + H2O
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: p-nitrophenyl-alpha-L-fucoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: series of snapshots of the reaction coordinate. The Michaelis complex is observed in a 1C4 conformation, and a trapped covalent intermediate in the 3S1 skew boat which together provides structural evidence for a latitudinal Southern Hemisphere 1C4-3H4-3S1 pathway for terminal alpha-L-fucoside hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: series of snapshots of the reaction coordinate. The Michaelis complex is observed in a 1C4 conformation, and a trapped covalent intermediate in the 3S1 skew boat which together provides structural evidence for a latitudinal Southern Hemisphere 1C4-3H4-3S1 pathway for terminal alpha-L-fucoside hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
Substrates: Afc2 shows enzyme activities exclusively to Le(x) trisaccharide and Le(a) trisaccharide. Although 3-fucosyl-GlcNAc and 4-fucosyl-GlcNAc have the same fucosyl linkage with Le(x) or Le(a) trisaccharides, they are resistant to the hydrolysis by Afc2 because they do not have the branched Gal residues at the non-reducing end. Afc2 is a 1,3-1,4-alphs-L-fucosidase
Products: -
Products: -
?
additional information
?
-
Substrates: Afc2 shows enzyme activities exclusively to Le(x) trisaccharide and Le(a) trisaccharide. Although 3-fucosyl-GlcNAc and 4-fucosyl-GlcNAc have the same fucosyl linkage with Le(x) or Le(a) trisaccharides, they are resistant to the hydrolysis by Afc2 because they do not have the branched Gal residues at the non-reducing end. Afc2 is a 1,3-1,4-alphs-L-fucosidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes alpha-(1->6)-linked fucose exclusively
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme showed good hydrolytic activities towards various alpha1,3- and alpha1,4-bearing fucosyloligosaccharide glycan structures, whereas no defucosylation is observed with the tested alpha1,2- and alpha1,6-fucose containing oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can only cleave alpha1,3-linked fucose residues from 3-fucosyllactose and lacto-N-fucopentaose III with low efficiency
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyzes alpha-(1->6)-linked fucose exclusively
Products: -
Products: -
?
additional information
?
-
-
Substrates: negligible effect on hydrolyzing 2'-fucosyllactose. EntFuc can catalyze the synthesis of 2'-fucosyllactose via transfucosylation action from 4-nitrophenyl alpha-L-fucoside and lactose
Products: -
Products: -
-
additional information
?
-
-
Substrates: negligible effect on hydrolyzing 2'-fucosyllactose. EntFuc can catalyze the synthesis of 2'-fucosyllactose via transfucosylation action from 4-nitrophenyl alpha-L-fucoside and lactose
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme preferentially hydrolyzes the alpha-(1->4)-L-fucosidic linkage present in alpha-L-fucobiosides with different types of linkages. The enzyme is capable of catalyzing the transglycosylation reaction with alcohols (methanol, ethanol, and 1-propanol) and 4-nitrophenyl-containing monosaccharides as acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme preferentially hydrolyzes the alpha-(1->4)-L-fucosidic linkage present in alpha-L-fucobiosides with different types of linkages. The enzyme is capable of catalyzing the transglycosylation reaction with alcohols (methanol, ethanol, and 1-propanol) and 4-nitrophenyl-containing monosaccharides as acceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: unable to hydrolyze 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 2-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, and 4-nitrophenyl N-acetyl-beta-D-glucosaminide, lactose, melibiose, lactulose, maltose, or maltotriose
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is capable of transglycosylation on a variety of acceptor molecules, including saccharides, alcohols or chromogenic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to catalyse the hydrolysis of fucosyl units of Ascophyllum nodosum fucoidan
Products: -
Products: -
?
additional information
?
-
Pedobacter sp. CAU209
A0A7D3USC4
Substrates: transglycosylation activity with 4-nitrophenyl-alpha-L-fucopyranoside and lactose to 4-nitrophenol and 2'-fucosyllactose
Products: -
Products: -
-
additional information
?
-
-
Substrates: Two specific mutations, designed on the basis of the programmed -1 frameshifting mechanism, promotes transfucosylation reactions by following a retaining reaction mechanism.
Products: -
Products: -
?
additional information
?
-
-
Substrates: 4-nitrophenyl-alpha-L-arabinoside, 4-nitrophenyl-alpha-L-rhamnoside, 4-nitrophenyl-alpha-D-glucoside, 4-nitrophenyl-alpha-D-xyloside, 4-nitrophenyl-alpha-D-galactoside and 4-nitrophenyl-alpha-D-mannoside are not substrates for wild-type and mutant fucA1B
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
Substrates: TfFuc1 is a unique alpha(1,2)-fucosidase that also possesses alpha(1,6) specificity on small unbranched substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: TfFuc1 is a unique alpha(1,2)-fucosidase that also possesses alpha(1,6) specificity on small unbranched substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: behaviour of the catalytic residues is different from that of Sulfolobus solfataricus alpha-fuc
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild-type enzyme catalyzes oligosaccharide synthesis by transfer of a fucosyl residue from a 4-nitrophenyl-fucoside donor to 4-nitrophenyl-fucoside (self-condensation) with alpha-(1,3) regioselectivity or 4-nitrophenyl-galactoside (transglycosylation) with alpha-(1,2) regioselectivity at low yields (7%)
Products: -
Products: -
?
additional information
?
-
Substrates: the wild-type enzyme catalyzes oligosaccharide synthesis by transfer of a fucosyl residue from a 4-nitrophenyl-fucoside donor to 4-nitrophenyl-fucoside (self-condensation) with alpha-(1,3) regioselectivity or 4-nitrophenyl-galactoside (transglycosylation) with alpha-(1,2) regioselectivity at low yields (7%)
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the synthesis of fucosylated oligosaccharides using 4-nitrophenyl-fucose as donor substrate and lactose as acceptor, the presence of 1.1 M CaCl2 favors the rate of transfucosylation, and improves the yield of synthesis duplicating and triplicating it with lactose concentrations of 58 mM and 146 mM, respectively. CaCl2 does not significatively affect hydrolysis rate in these reactions. The combination of the activating effect of CaCl2, the decrement in water activity and lactose concentration has a synergistic effect favoring the synthesis of fucosylated oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-fucopyranoside, p-nitrophenyl N-acetyl-beta-D-glucosaminide, p-nitrophenyl alpha-mannopyranoside
Products: -
Products: -
?
additional information
?
-
A0A068B783
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
A0A068B2Y3
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
A0A068B3H5
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
A0A068B4L8
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
A0A068B4M2
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
A0A068B780
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
A0A068B1E8
Substrates: Mfuc5 is capable of both releasing fucose from citrus xyloglucan and and can also use it as a fucosyl-donor for synthesis of fucosyllactose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme can hydrolyze the partially degraded fragment of fucoidan. No free fucose can be released from alpha-Fuc-(1->2)-beta-Gal-(1->4)-Glc, beta-Gal-(1->4)-[alpha-Fuc-(1->3)]-Glc or alpha-Fuc-(1->6)-GlcNAc
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can hydrolyze the partially degraded fragment of fucoidan. No free fucose can be released from alpha-Fuc-(1->2)-beta-Gal-(1->4)-Glc, beta-Gal-(1->4)-[alpha-Fuc-(1->3)]-Glc or alpha-Fuc-(1->6)-GlcNAc
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
-
Substrates: -
Products: -
Products: -
?
6-O-alpha-L-fucopyranosyl-N-acetylglucosamine + H2O
alpha-L-fucopyranose + N-acetyl-glucosamine
-
Substrates: Fuc-alpha-1,6-GlcNAc-linkage most susceptible
Products: -
Products: -
?
alpha-L-Fuc-(1-2)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
-
Substrates: same yield of transglycosylation and hydrolysis products
Products: -
Products: -
?
alpha-L-Fuc-(1-3)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
-
Substrates: slower hydrolysis than for the alpha-(1-6)- or alpha-(1-2)-isomers, transglycosylation activity
Products: -
Products: -
?
alpha-L-Fuc-(1-6)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-6)-D-GlcNAc + D-galactose
-
Substrates: same yield of transglycosylation and hydrolysis products
Products: -
Products: -
?
alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-D-galactitol + H2O
alpha-L-fucose + beta-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-D-galactitol
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
Fuc-alpha-(1-2)-Gal-beta-(1-3)-[Fuc-alpha-(1-4)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-[Fuc-alpha-(1-4)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: lacto-N-difucohexaitol I, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-sorbitol + H2O
alpha-L-fucose + Gal-beta-(1-4)-sorbitol
-
Substrates: alpha-fucosidase II, does not cleave alpha-(1-4)-GlcNAc-, alpha-(1-3)-GlcNAc- or alpha-(1-6)-GlcNAc-linkages and does not act on lacto-N-fucopentaoitol I, which has a Fuc-alpha-(1-2)-Gal-group
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
Gal-beta-(1-4)-[Fuc-alpha-(1-3)]-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: hydrolysis of Fuc-alpha-(1-2)-Gal- and Fuc-alpha-(1-4)-GlcNAc- and Fuc-alpha-(1-6)-GlcNAc- linkages but hardly the Fuc-alpha-(1-3)-GlcNAc-linkage
Products: -
Products: -
?
Fuc-alpha-(1-2)-Glc + H2O
alpha-L-fucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Xyl + H2O
alpha-L-fucose + D-xylose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-Glc + H2O
alpha-L-fucose + D-glucose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-4)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc-beta-Asn + H2O
alpha-L-fucose + N-acetyl-D-glucosaminyl-Asn
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1->2)-Gal-beta-(1->3)-[Fuc-alpha-(1->6)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc + H2O
alpha-L-fucose + Gal-beta-(1->3)-[Fuc-alpha-(1->6)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1->2)-Gal-beta-(1->3)-[Fuc-alpha-(1->6)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc + H2O + H2O
alpha-L-fucose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)GlcNAc + H2O
Bacillus fulminans
-
Substrates: -
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Gal-beta-(1-4)-GlcNAc-[Fuc-alpha-(1-4)]-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-4)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Gal-beta-(1-4)[Fuc-alpha-(1-3)]-Glc + H2O
Gal-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: very slow hydrolysis, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
glycosphingolipid + H2O
alpha-L-fucose + ?
-
Substrates: blood-group active types B and H
Products: -
Products: -
?
gp120 oligosaccharides + H2O
alpha-L-fucose + ?
-
Substrates: released from recombinant CHO cell-produced gp120, glycoproteins containing fucose in alpha-1,3- and alpha-1,6-linkages are no substrates
Products: -
Products: -
?
IgG Fc peptide + H2O
alpha-L-fucose + ?
-
Substrates: human, rabbit, horse
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
lactoferrin + H2O
alpha-L-fucose + ?
-
Substrates: low activity
Products: -
Products: -
?
LH-beta peptic glycopeptide + H2O
alpha-L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
meconium X-1 + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: low activity
Products: -
Products: -
?
orosomucoid + H2O
alpha-L-fucose + ?
-
Substrates: low activity, higher activity if desialyzed
Products: -
Products: -
?
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-[Fuc-alpha-(1->6)]GlcNAc + H2O
[Man-alpha-(1->6)]-[Man-alpha-(1->3)]-Man-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + alpha-L-fucose
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to catalyse the hydrolysis of fucosyl units of Ascophyllum nodosum fucoidan
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: low activity
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: -
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: alpha-fucosidase I, cleavage of alpha-(1-3)- and alpha-(1-4)-linkages in oligosaccharides and glycopeptides, doesn't cleave Fuc-alpha-(1-2)-Gal- and Fuc-alpha-(1-6)-GlcNAc-linkages
Products: -
Products: -
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: alpha-fucosidase II highly active
Products: -
Products: -
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: very low activity
Products: -
Products: -
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
Bacillus fulminans
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: alpha-fucosidase I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose I
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: only hydrolysed by alpha-L-fucosidase II
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + H2O
Gal-beta-(1-3)-GlcNAc-beta-(1-4)-Glc + alpha-L-fucose
-
Substrates: lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
Bacillus fulminans
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: only hydrolysed by alpha-fucosidase II
Products: -
Products: -
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
-
Substrates: 2'-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: low activity
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
-
Substrates: 3-fucosyllactose
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: slow hydrolysis rate
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: slow hydrolysis rate
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity for alpha-L-fucosidase II
Products: -
Products: -
?
Gal-beta-(1-3)-GlcNAc-beta-(1-3)-[Fuc-alpha-(1-4)]-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
Products: -
Products: -
?
Gal-beta-(1-4)-GlcNAc-[Fuc-alpha-(1-4)]-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-4)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose III
Products: -
Products: -
?
Gal-beta-(1-4)-GlcNAc-[Fuc-alpha-(1-4)]-beta-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + Gal-beta-(1-4)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: lacto-N-fucopentaose III
Products: -
Products: -
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
-
Substrates: -
Products: -
Products: -
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
-
Substrates: low activity
Products: -
Products: -
?
gastric mucin + H2O
alpha-L-fucose + ?
-
Substrates: porcine
Products: -
Products: -
?
gastric mucin + H2O
alpha-L-fucose + ?
-
Substrates: porcine
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: desialyzed porcine submaxillary mucin
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: meconium H-1, H-2 and X-1
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
-
Substrates: cellular source of substrate
Products: -
Products: -
?
glycopeptide + H2O
alpha-L-fucose + ?
-
Substrates: not active on native glycoproteins
Products: -
Products: -
?
glycoprotein + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: specifically hydrolyses terminal alpha-(1-2)-fucosidic bonds of glycoproteins, glycopeptides and oligosaccharides
Products: -
Products: -
?
glycoprotein + H2O
alpha-L-fucose + ?
-
Substrates: salivary human type H
Products: -
Products: -
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
-
Substrates: low activity for alpha-L-fucosidase II
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: low activity
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: preferentially hydrolysed by alpha-fucosidase II
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: alpha-fucosidase II
Products: -
Products: -
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
-
Substrates: -
Products: -
Products: -
?
oligosaccharide + H2O
alpha-L-fucose + ?
-
Substrates: di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
Products: -
Products: -
?
oligosaccharide + H2O
alpha-L-fucose + ?
-
Substrates: di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
Products: -
Products: -
?
saliva + H2O
alpha-L-fucose + ?
-
Substrates: Ulex europaeus
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
Bacillus fulminans
-
Substrates: desialyzed and not, desialyzed mucine best substrate tested
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: one form, optimally active at pH 5, not able to hydrolyse p-nitrophenyl-alpha-L-fucopyranoside
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
submaxillary mucin + H2O
alpha-L-fucose + ?
-
Substrates: A-minus type and desialyzed, porcine
Products: -
Products: -
?
thyroglobulin + H2O
alpha-L-fucose + ?
-
Substrates: bovine
Products: -
Products: -
?
thyroglobulin + H2O
alpha-L-fucose + ?
-
Substrates: hydrolysis only after pronase or neuraminidase treatment
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
-
the hydrolytic activity displays a maximum increase of 138% in the presence of 1.1 M NaCl. The hydrolytic activity is higher when using CaCl2 compared to NaCl. In the synthesis of fucosylated oligosaccharides using 4-nitrophenyl-fucose as donor substrate and lactose as acceptor, the presence of 1.1 M CaCl2 favors the rate of transfucosylation, and improves the yield of synthesis duplicating and triplicating it with lactose concentrations of 58 mM and 146 mM, respectively. CaCl2 does not significatively affect hydrolysis rate in these reactions. The combination of the activating effect of CaCl2, the decrement in water activity and lactose concentration has a synergistic effect favoring the synthesis of fucosylated oligosaccharides
Co2+
Cu2+
Fe2+
Fe3+
Mg2+
Mn2+
NaCl
-
the hydrolytic activity displays a maximum increase of 67% in the presence of 0.8 M NaCl
Zn2+
additional information
Ca2+
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 1.11fold activation
Co2+
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 1.34fold activation
Fe3+
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 1.12fold activation
additional information
the addition of calcium, magnesium, cobalt, manganese, nickel, and zinc at 10 mM concentrations does not increase enzymatic rates
additional information
-
the addition of calcium, magnesium, cobalt, manganese, nickel, and zinc at 10 mM concentrations does not increase enzymatic rates
additional information
the enzyme is not significantly influenced by NaCl
additional information
-
the enzyme is not significantly influenced by NaCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3R,4S,5R)-2-(propan-2-yl)piperidine-3,4,5-triol
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
(2S,3R,4S,5S)-2-methyl-5-(phenylamino)pyrrolidine-3,4-diol
-
inhibitor shares the same absolute configuration as C(2,3,4,5) of alpha-L-fucopyranosides
(2S,3S,4R,5S)-2-(1H-benzimidazol-2-yl)-5-methylpyrrolidine-3,4-diol
-
inhibitor shares the same absolute configuration as C(2,3,4,5) of alpha-L-fucopyranosides
(2S,3S,4R,5S)-2-[(biphenyl-4-ylamino)methyl]-5-methylpyrrolidine-3,4-diol
-
inhibitor shares the same absolute configuration as C(2,3,4,5) of alpha-L-fucopyranosides
(5R,6R,7R)-6,7-dihydroxy-5-hydroxymethyl-4-azaspiro[2.4]heptane
-
1 mM, 50% inhibition
(5R,6S,7S)-6,7-dihydroxy-5-hydroxymethyl-4-azaspiro[2.4]heptane
-
1 mM, 41% inhibition
(5S,6R,7R)-6,7-dihydroxy-5-hydroxymethyl-4-azaspiro[2.4]heptane
-
1 mM, 49% inhibition
(5S,6R,7S)-6,7-dihydroxy-5-hydroxymethyl-4-azaspiro[2.4]heptane
-
1 mM, 55% inhibition
(5S,6R,7S)-6,7-dihydroxy-5-[(1S)-1,2-dihydroxyethyl]-4-azaspiro[2.4]heptane
-
1 mM,97 inhibition, competitive
1,5-dideoxy-1,5-([(2R,3R)-2,4-dihydroxy-3-(sulfooxy)butyl]-episulfoniumylidene)-L-fucitol inner salt
-
-
1,5-dideoxy-1,5-([(2R,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-episulfoniumylidene)-L-fucitol inner salt
-
-
1,5-dideoxy-1,5-([(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]-episulfoniumylidene)-L-fucitol inner salt
-
-
1,5-dideoxy-1,5-[5-methoxycarbonyl-1-pentyl-episulfoniumylidene]-L-fucitol tetrafluoroborate salt
-
-
1,5-dideoxy-1,5-[methyl-episulfoniumylidene]-L-fucitol tetrafluoroborate salt
-
-
1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate
-
complete inactivation at 22 mM
2-(1H-indol-3-yl)-N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
2-(hydroxymethyl)-5-methylpyrrolidine-3,4-diol
-
competitive or uncompetitive inhibition, Ki: 0.004-26 mM, depending on conformation
2-cyclopentyl-2-phenyl-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)acetamide
-
2-cyclopentyl-2-phenyl-N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
2-phenyl-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)quinoline-4-carboxamide
-
2-phenyl-tetrahydro-2H-pyran-3,4-diol
-
uncompetitive inhibition, Ki: 22-83 mM, depending on conformation
3-(1H-indol-3-yl)-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)propanamide
-
3-(1H-indol-3-yl)-N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]propanamide
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
4-hydroxy-2-methyltetrahydro-2H-pyran-3-yl acetate
-
competitive inhibition, Ki: 0.09 mM
4-nitrophenyl alpha-L-fucopyranoside
substrate inhibition at high concentrations
5-fluoro-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)-1H-indole-2-carboxamide
-
CoCl2
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 11.3% loss of activity
DMSO
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 10.4% loss of activity
FeCl2
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 8% loss of activity
glucose
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 5% loss of activity; 1 mM, 5.3% loss of activity
L-fucal
-
competitive inhibition, best inhibitor of glycal compounds tested, Ki: 0.05 mM
MnCl2
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 5.1% loss of activity; 1 mM, 6.8% loss of activity
N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1-benzofuran-2-carboxamide
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1H-indole-3-carboxamide
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
-
-
p-nitrophenyl alpha-L-fucoside
substrate inhibition at high concentration
Tween 80
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 24.1% loss of activity
ZnCl2
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 13.4% loss of activity; 1 mM, 17% loss of activity; 1 mM, 52.5% loss of activity
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
(2S,3R,4S,5R)-2-benzylpiperidine-3,4,5-triol
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
2-mercaptoethanol
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 2.7% loss of activity; 1 mM, 23.2% loss of activity; 1 mM, 9.2% loss of activity
4-chloromercuribenzoate
-
50% inhibition at 0.0015 mM, totally reversal by addition of 4 mM DTT
Ag+
-
complete inactivation at 0.1 mM, complete reversal by addition of 1.1 mM DTT
alpha-L-fucose
-
competivite inhibition of p-nitrophenyl alpha-L-fucopyranoside hydrolysis
fuconojirimycin
majority of C1-substituted fuconojirimycins act as reversible inhibitors of the human fucosidase
fuconojirimycin
-
majority of C1-substituted fuconojirimycins are slow tight-binding inhibitors of the Thermotoga enzyme, Tyr64 and Tyr267 are critically involved in closely interacting with the aglycon of inhibitors
Hg2+
-
complete inactivation at 0.1 mM, complete reversal by addition of 1.1 mM DTT
Hg2+
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 61% loss of activity; 1 mM, 69.7% loss of activity; 1 mM, 94.8% loss of activity
additional information
WP_057784261.1
the enzyme is inhibited by metabolites in the aqueous ethanol extract of Fucus evanescens
-
additional information
-
time-associated loss in the activity of alpha-fucosidase post infection. Sialic acid release is correlated with a gradual loss in activity of the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
azide
increases the rate of substrate cleavage in depending of azide concentration
formate
increases the rate of substrate cleavage in depending of azide concentration
glucose
QUH15933.1, QUH16573.1, QUH16649.1
1 mM, 1.07 fold activation
methanol
linear increase in enzyme-catalyzed cleavage of p-nitrophenyl alpha-L-fucoside and fucosyl fluoride
additional information
-
cell-bound enzyme activity increases sharply following permeabilization of intact sperm
-
additional information
-
the enzyme activity is increases with the ionic strength from 10 mM to 200 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.01
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose
pH 7, 37°C
3.1
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc
pH 7, 37°C
2.46
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc
pH 7, 37°C
1.23
propyl alpha-L-fucopyranosyl-(1->2)-alpha-L-fucopyranoside
pH 5.5, 37°C
3
propyl alpha-L-fucopyranosyl-(1->3)-alpha-L-fucopyranoside
pH 5.5, 37°C
0.53
propyl alpha-L-fucopyranosyl-(1->4)-alpha-L-fucopyranoside
pH 5.5, 37°C
0.0484
4-methylumbelliferyl alpha-L-fucopyranoside
-
30°C, pH not specified in the publication
0.06
4-methylumbelliferyl alpha-L-fucopyranoside
-
pH 5.0, 37°C, undifferentiated HT-29 cells
0.07
4-methylumbelliferyl alpha-L-fucopyranoside
-
pH 5.0, 37°C, differentiated HT-29 cells
0.14
4-methylumbelliferyl-alpha-L-fucopyranoside
-
4-5fold increase in fucosidosis patients
0.0681
4-nitrophenyl alpha-L-fucopyranoside
-
pH 5.0, 60°C, soluble enzyme
0.071
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 7.0
0.1
4-nitrophenyl alpha-L-fucopyranoside
-
pH 5.0, 60°C, immobilized enzyme
0.1
4-nitrophenyl alpha-L-fucopyranoside
pH 5.0, 37°C, mutant enzyme D276N
0.11
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 7.0
0.13
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 7.0
0.14
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 7.0
0.25
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
0.28
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 6.0
0.31
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 6.0
0.32
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, mutant enzyme E235Q
0.4
4-nitrophenyl alpha-L-fucopyranoside
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
30°C, pH 9.0
0.41
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, wild-type enzyme
0.55
4-nitrophenyl alpha-L-fucopyranoside
-
30°C, pH not specified in the publication
1 - 4
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, mutant enzyme H503A
1.03
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
1.32
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
3.3
4-nitrophenyl alpha-L-fucopyranoside
pH 7.0, 30°C
0.06
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A, at 70°C. Mutant T264A/Y267F/L322P, at 40°C
0.08
4-nitrophenyl alpha-L-fucoside
mutant G226S/Y237H/T264A/L322P, at 40°C
0.09
4-nitrophenyl alpha-L-fucoside
mutant P196L/Y237H/Y267F, at 40°C
0.09
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F, at 40°C
0.09
4-nitrophenyl alpha-L-fucoside
mutant G226S/T264A/Y267F/L322P, at 40°C
0.1
4-nitrophenyl alpha-L-fucoside
mutant P196L/Y237H/Y267F and mutant G226S/Y237H/T264A/L322P, at 70°C. Mutant M210V/Y237H/T264A, at 40°C
0.14
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F, at 70°C
0.14
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F/L322P, at 40°C
0.23
4-nitrophenyl alpha-L-fucoside
mutant Y237H/Y267F/L322P, at 70°C
0.25
4-nitrophenyl alpha-L-fucoside
mutant T264A/L322P7 and mutant M210V/Y237H/T264A/Y267F/L322P, at 70°C
0.29
4-nitrophenyl alpha-L-fucoside
mutant Y237H/Y267F/L322P, at 40°C
0.3
4-nitrophenyl alpha-L-fucoside
mutant G226S/T264A/Y267F/L322P, at 70°C
0.31
4-nitrophenyl alpha-L-fucoside
mutant T264A/Y267F/L322P, at 70°C
0.028
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, wild-type enzyme
0.028
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 6.3, in the presence of sodium phosphate
0.033
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme D146G
0.056
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme E292G
0.06
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E292G, at pH 6.3, in the presence of sodium phosphate
0.06
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme M210V/Y237H/T264A
0.06
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme T264A/Y267F/L322P
0.065
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme T264A
0.07
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme T264A
0.08
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme G226S/Y237H/T264A/L322P
0.088
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme D124G
0.09
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E292G, at pH 4.6, in the presence of sodium acetate
0.09
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme P196L/Y237H/Y267F
0.09
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme M210V/Y237H/T264A/Y267F
0.09
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme G226S/T264A/Y267F/L322P
0.1
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme P196L/Y237H/Y267F
0.1
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme M210V/Y237H/T264A
0.1
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme G226S/Y237H/T264A/L322P4
0.13
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme R147G/L322P
0.14
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme M210V/Y237H/T264A/Y267F
0.14
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P
0.19
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme T264A/L322P
0.23
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme Y237H/Y267F/L322P
0.25
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme T264A/L322P
0.25
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P
0.26
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65°C, wild-type enzyme
0.26
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 5.0, in the presence of sodium citrate
0.28
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme R147G/L322P
0.29
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme Y237H/Y267F/L322P
0.3
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme G226S/T264A/Y267F/L322P
0.31
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme T264A/Y267F/L322P
0.6
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium acetate
1.1
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium formate
1.6
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium citrate
2.9
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 6.3, in the presence of sodium phosphate and NaN3
4.37
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65°C, mutant enzyme H46G
17
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme H46G
0.0287
4-nitrophenyl-alpha-L-fucoside
-
wild-type and mutant fucA1B
0.6
4-nitrophenyl-alpha-L-fucoside
wild-type enzyme, pH 8, 45°C
5.8
4-nitrophenyl-alpha-L-fucoside
mutant enzyme W392A, pH 8, 45°C
0.11
p-nitrophenyl alpha-L-fucopyranoside
mutant E289Q, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity
0.12
p-nitrophenyl alpha-L-fucopyranoside
mutant E289G, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity
0.27
p-nitrophenyl alpha-L-fucopyranoside
mutant D258G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.28
p-nitrophenyl alpha-L-fucopyranoside
50 mM sodium phosphate buffer, pH 6.8, 37°C
0.28
p-nitrophenyl alpha-L-fucopyranoside
mutant E70G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.28
p-nitrophenyl alpha-L-fucopyranoside
mutant E135G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.28
p-nitrophenyl alpha-L-fucopyranoside
mutant D158G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.28
p-nitrophenyl alpha-L-fucopyranoside
mutant E275G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.28
p-nitrophenyl alpha-L-fucopyranoside
mutant D276G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.3
p-nitrophenyl alpha-L-fucopyranoside
mutant E79G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
1.04
p-nitrophenyl alpha-L-fucopyranoside
mutant D225G, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity
1.06
p-nitrophenyl alpha-L-fucopyranoside
mutant D225N, 50 mM sodium phosphate buffer, pH 6.8, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.4
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose
pH 7, 37°C
26.9
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc
pH 7, 37°C
23.6
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc
pH 7, 37°C
0.059
4-nitrophenyl alpha-L-fucopyranoside
pH 5.0, 37°C, mutant enzyme D276N
0.8
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, mutant enzyme E235Q
14
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, mutant enzyme H503A
19.4
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
24.2
4-nitrophenyl alpha-L-fucopyranoside
-
pH 5.0, 60°C, immobilized enzyme
99
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, wild-type enzyme
99.9
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
363.3
4-nitrophenyl alpha-L-fucopyranoside
-
pH 5.0, 60°C, soluble enzyme
1022.7
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
0.48
4-nitrophenyl alpha-L-fucoside
mutant G226S/T264A/Y267F/L322P, at 40°C
0.5
4-nitrophenyl alpha-L-fucoside
mutant T264A/Y267F/L322P, at 40°C
0.73
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F/L322P, at 40°C
2.7
4-nitrophenyl alpha-L-fucoside
mutant G226S/Y237H/T264A/L322P, at 40°C
4.3
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F, at 40°C
6.4
4-nitrophenyl alpha-L-fucoside
mutant G226S/T264A/Y267F/L322P, at 70°C
8.2
4-nitrophenyl alpha-L-fucoside
mutant T264A/Y267F/L322P, at 70°C
14.8
4-nitrophenyl alpha-L-fucoside
mutant Y237H/Y267F/L322P, at 40°C
15
4-nitrophenyl alpha-L-fucoside
mutant R147G/L322P, mutant P196L/Y237H/Y267F and mutant T264A, at 40°C
20
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A, at 40°C
20
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F/L322P, at 70°C
39
4-nitrophenyl alpha-L-fucoside
mutant G226S/Y237H/T264A/L322P, at 70°C
56
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A/Y267F, at 70°C
65
4-nitrophenyl alpha-L-fucoside
mutant M210V/Y237H/T264A, at 70°C
96
4-nitrophenyl alpha-L-fucoside
mutant Y237H/Y267F/L322P, at 70°C
164
4-nitrophenyl alpha-L-fucoside
mutant P196L/Y237H/Y267F, at 70°C
0.48
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme G226S/T264A/Y267F/L322P
0.5
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme T264A/Y267F/L322P
0.73
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P
1.86
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E292G at pH 6.3 in the presence of sodium phosphate or at pH 4.6 in the presence of sodium acetate
1.96
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme E292G
2.7
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme G226S/Y237H/T264A/L322P
3.6
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme T264A/L322P
4.3
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme M210V/Y237H/T264A/Y267F
6.4
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme G226S/T264A/Y267F/L322P
8.2
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme T264A/Y267F/L322P
9.66
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant D242G, in the presence of 2 M sodium azide
14.8
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme Y237H/Y267F/L322P
15
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme R147G/L322P
15
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme P196L/Y237H/Y267F
20
4-nitrophenyl-alpha-L-fucopyranoside
40°C, mutant enzyme M210V/Y237H/T264A
20
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P
39
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme G226S/Y237H/T264A/L322P4
50
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme T264A/L322P
56
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme M210V/Y237H/T264A/Y267F
65
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme M210V/Y237H/T264A
96
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme Y237H/Y267F/L322P
143
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium citrate
164
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme P196L/Y237H/Y267F
169
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme T264A
198
4-nitrophenyl-alpha-L-fucopyranoside
70°C, mutant enzyme R147G/L322P
224
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme D146G
240
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme D124G
287
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, wild-type enzyme
287
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 6.3, in the presence of sodium phosphate
419
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme H46G
419
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65°C, mutant enzyme E292G
430
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65°C, wild-type enzyme
495
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65°C, mutant enzyme H46G
586
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium acetate
679
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 6.3, in the presence of sodium phosphate and NaN3
846
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium formate
0.003
p-nitrophenyl alpha-L-fucopyranoside
mutant D225G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.003
p-nitrophenyl alpha-L-fucopyranoside
mutant D225N, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.039
p-nitrophenyl alpha-L-fucopyranoside
mutant E289Q, 50 mM sodium phosphate buffer, pH 6.8, 37°C
0.048
p-nitrophenyl alpha-L-fucopyranoside
mutant E289G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
12.5
p-nitrophenyl alpha-L-fucopyranoside
mutant D258G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
16
p-nitrophenyl alpha-L-fucopyranoside
mutant E135G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
16.3
p-nitrophenyl alpha-L-fucopyranoside
mutant E79G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
16.7
p-nitrophenyl alpha-L-fucopyranoside
mutant D276G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
16.9
p-nitrophenyl alpha-L-fucopyranoside
mutant E70G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
16.9
p-nitrophenyl alpha-L-fucopyranoside
mutant D158G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
16.9
p-nitrophenyl alpha-L-fucopyranoside
mutant E275G, 50 mM sodium phosphate buffer, pH 6.8, 37°C
17.1
p-nitrophenyl alpha-L-fucopyranoside
50 mM sodium phosphate buffer, pH 6.8, 37°C
245
p-nitrophenyl alpha-L-fucoside
-
pH 6.5, 65°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.56
alpha-L-fucopyranosyl-(1->2)-D-galactopyranose
pH 7, 37°C
8.66
beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc
pH 7, 37°C
9.56
beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc
pH 7, 37°C
0.6
4-nitrophenyl alpha-L-fucopyranoside
pH 5.0, 37°C, mutant enzyme D276N
1
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, mutant enzyme H503A
2.5
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, mutant enzyme E235Q
14.7
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
96.6
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
240
4-nitrophenyl alpha-L-fucopyranoside
-
pH 5.0, 60°C, immobilized enzyme
241
4-nitrophenyl alpha-L-fucopyranoside
pH 6.5, 37°C, wild-type enzyme
3978.7
4-nitrophenyl alpha-L-fucopyranoside
QUH15933.1, QUH16573.1, QUH16649.1
pH 7.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
(2S,3S,4R,5S)-2-[(biphenyl-4-ylamino)methyl]-5-methylpyrrolidine-3,4-diol
-
-
0.0016
(5S,6R,7S)-6,7-dihydroxy-5-[(1S)-1,2-dihydroxyethyl]-4-azaspiro[2.4]heptane
-
-
0.000475
2-(1H-indol-3-yl)-N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
-
-
0.004 - 26
2-(hydroxymethyl)-5-methylpyrrolidine-3,4-diol
-
competitive or uncompetitive inhibition, depending on conformation
0.000018
2-cyclopentyl-2-phenyl-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)acetamide
-
0.001
2-cyclopentyl-2-phenyl-N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
-
-
0.0000117
2-phenyl-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)quinoline-4-carboxamide
-
22 - 83
2-phenyl-tetrahydro-2H-pyran-3,4-diol
-
uncompetitive inhibition, depending on conformation
0.0000056
3-(1H-indol-3-yl)-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)propanamide
-
0.000105
3-(1H-indol-3-yl)-N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]propanamide
-
-
0.0000097
5-fluoro-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)-1H-indole-2-carboxamide
-
0.000441
N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1-benzofuran-2-carboxamide
-
-
0.000427
N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1H-indole-3-carboxamide
-
-
0.0045
N-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
-
-
12
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25°C, epididymis
15
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25°C, kidney
125
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25°C
28
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25°C, kidney
58
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25°C
188
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25°C, epididymis
0.0000152
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
0.0000163
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
-
0.00002
1-deoxyfuconojirimycin
-
30°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000064
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
Homo sapiens
-
0.000052
(2S,3R,4R,5R,6S)-2-(hydroxymethyl)-6-methylpiperidine-3,4,5-triol
Homo sapiens
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
14.9 - 17.1
-
recombinant enzyme, value depending on expression systems and buffer
190
substrate: 4-nitrophenyl-alpha-L-fucoside, mutant enzyme W392A, pH 8, 45°C
275
substrate: 4-nitrophenyl-alpha-L-fucoside, wild-type enzyme, pH 8, 45°C
additional information
additional information
-
0.08 U/ml, incubation at 37°C for 1 h, decreased migratory process of immune cells and less lectin-binding
additional information
-
6.1 micromol/min/l, spectrophotometer citrate buffer pH 4.5, 3 h incubation at 37°C, optical density at 405 nm, average over all patient
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, flies of arid regions tend to produce more alpha-fucosidase activity than those originating in sugar-rich environments
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.3 - 6.3
4 - 4.5
-
a broad acidic optimum at pH 4.0-4.5 and a second neutral optimum at pH 6.4-7.4
4.3
5 - 6
5.3
5.5
5.6 - 6
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A8A6LWW9
-
5.7
5.8
6 - 6.5
6.3
6.4 - 7.4
-
a broad acidic optimum at pH 4.0-4.5 and a second neutral optimum at pH 6.4-7.4
6.5
6.8
6.9
7.5
5
-
optimal hydrolysis rate for 2'-fucosyllactose and Fuc-alpha-(1-6)-GlcNAc
5
-
gonad fluid enzyme sharper pH dependence curve than the sperm-bound enzyme
6
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
-
6
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A8A6LWW9
-
7
-
fluorogenic substrate, natural substrates, isolated from dog brain, more readily digested at acidic pH
7
-
optimal hydrolysis rate for 4-methylumbelliferyl-alpha-L-fucopyranoside
7
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
-
7
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A8A6LWW9
-
9
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
-
9
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A8A6LWW9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.2 - 5
pH 2.2: about 650% of maximal activity, pH 5.0: about 70% of maximal activity
3 - 5
3.5 - 6
pH 3.5: about 50% of maximal activity, pH 6.0: about 60% of maximal activity
3.5 - 6.3
-
pH 3.5: about 55% of maximal activity, pH 6.25: 50% of maximal activity
4
QUH15933.1, QUH16573.1, QUH16649.1
pH 4.0: about 25% of maximal activity, pH 7.0: about 35% of maximal activity
4 - 6
QUH15933.1, QUH16573.1, QUH16649.1
pH 4.0: about 30% of maximal activity, pH 6.0: about 40% of maximal activity
4 - 6.5
pH 4.0: about 60% of maximal activity, pH 6.5: about 70% of maximal activity
4 - 7
-
pH 4.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity
4.5 - 6.5
Pedobacter sp. CAU209
A0A7D3USC4
pH 4.5: about 80% of maximal activity, pH 6.5: about 40% of maximal activity
4.5 - 7
Pedobacter sp. CAU209
A0A7D3USC4
pH 4.5: about 70% of maximal activity, pH 7.0: about 60% of maximal activity
5 - 7
pH 5.0: about 75% of maximal activity, pH 7.0: about30 % of maximal activity, hydrolysis of 4-nitrophenyl alpha-L-fucopyranoside
5 - 8
-
pH 5.0: about 40% of maximal activity, pH 8.0: about 45% of maximal activity
5.5 - 7
5.5 - 8.5
pH 5.5: about 40% of maximal activity, pH 8.5: about 35% of maximal activity
6 - 8.5
-
pH 6.0: about 30% of maximal activity, pH 8.5: about 50% of maximal activity
6.5 - 8.8
-
pH 6.5: about 50% of maximal activity, pH 8.8: about 55% of maximal activity
additional information
-
alpha-fucosidase from the uninfected semen displays a broad acidic pH range of 4.55.5 and a subsequent neutral optimum of pH 6.87.2. There is an absence of the neutral pH optimum for the pathological semen
3 - 5
KXI90766.1
pH 3.0: about 55% of maximal activity, pH 5.0: about 45% of maximal activity
3 - 5
QUH15933.1, QUH16573.1, QUH16649.1
pH 3.0: about 10% of maximal activity, pH 5.0: about 60% of maximal activity
5.5 - 7
-
pH 5.5: about 60% of maximal activity, pH 7.0: about 70% of maximal activity
5.5 - 7
-
pH 5.5: about 40% of maximal activity, pH 7.0: about 60% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
39
40
41
45
50
55
60
70
95
25
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A8A6LWW9
-
95
-
the activity increases sharply up to the optimal temperature of 95°C, the highest temperature tested
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 42
-
5°C: about 55% of maximal activity, 42°C: about 50% of maximal activity
20 - 35
20 - 40
24 - 45
Pedobacter sp. CAU209
A0A7D3USC4
25°C: about 70% of maximal activity, 45°C: about 60% of maximal activity
25 - 50
-
25°C: about 70% of maximal activity, 50°C: about 30% of maximal activity
25 - 60
QUH15933.1, QUH16573.1, QUH16649.1
25°C: about 60% of maximal activity, 60°C: about 70% of maximal activity
30 - 50
-
30°C: about 40% of maximal activity, 50°C: about 70% of maximal activity
30 - 60
QUH15933.1, QUH16573.1, QUH16649.1
30°C: about 55% of maximal activity, 60°C: about 35% of maximal activity
30 - 70
30°C: about 50% of maximal activity, 70°C: about 85% of maximal activity
35 - 60
KXI90766.1
35°C: about 50% of maximal activity, 60°C: about 60% of maximal activity
37 - 60
37°C: about 50% of maximal activity, 60°C: about 25% of maximal activity
40 - 60
QUH15933.1, QUH16573.1, QUH16649.1
40°C: about 50% of maximal activity, 60°C: maximal activity
40 - 70
40°C: about 55% of maximal activity, 70°C: about 90% of maximal activity, 45 min reaction
50 - 70
-
50°C: about 60% of maximal activity, 70°C: about 80% of maximal activity
additional information
-
comparison of temperature range depending of wild-type and mutant enzyme, the reaction catalyzed by the mutant D242G depends less on temperature
20 - 35
20°C: about 50% of maximal activity, 35°C: about 50% of maximal activity, hydrolysis of 4-nitrophenyl alpha-L-fucopyranoside
20 - 35
20°C: about 50% of maximal activity, 35°C: about 50% of maximal activity
20 - 40
-
20°C: about 45% of maximal activity, 40°C: about 50% of maximal activity
20 - 40
Pedobacter sp. CAU209
A0A7D3USC4
20°C: about 80% of maximal activity, 40°C: about 70% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
isoelectric focusing indicates that the purified enzyme consists of multiple isoforms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
putative alpha-L-fucosidase, precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
putative uncharacterized protein; CB15, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
probable glycosyl hydrolase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
brenda
alpha-L-fucosidase, putative; W83, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
SH1, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
UniProt
brenda
putative glycosyl hydrolase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
Q9Z4I9
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
alpha-L-fucosidase family protein; ATCC35405, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
strain pv. Citri str.306, comparative and phylogenetic analysis of alpha-L-fucosidase genes
Q8PI26
SwissProt
brenda
pv. campestris str. 8004, comparative and phylogenetic analysis of alpha-L-fucosidase genes
UniProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
probable alpha-L-fucosidase; YCH46, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
putative alpha-L-fucosidase protein; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
putative alpha-L-fucosidase; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
putative exported alpha-L-fucosidase protein; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
putative exported hydrolase; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
YCH46, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
VPI5482, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
probable glycosyl hydrolase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
glycosyl hydrolase, putative alpha-L-fucosidase; KPA171202, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
KPA171202, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SWissProt
brenda
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
-
208705, 208707, 208715, 208716, 208719, 208721, 208723, 208724, 208727, 208735, 208736, 208737, 208738, 654935, 655418, 655733, 656821, 656888, 664629, 667006
-
-
brenda
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
MS119, putative fucosidase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
MS120, putative fucosidase; RE1, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
MS119, putative fucosidase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
MS120, putative fucosidase; RE1, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
putative uncharacterized protein; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
clone ZZZ276 mRNA sequence; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
Q9Z4I9
SwissProt
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
brenda
alpha-L-fucosidase, putative; comparative and phylogenetic analysis of alpha-L-fucosidase genes
Uniprot
brenda
-
A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B783, A0A8A6LWW9
UniProt
brenda
soil-derived metagenome
A0A068B1E8, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B783
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
anterior midgut is the only midgut fraction that responds to the blood meal in terms of alpha-L-fucosidase production
brenda
-
gastric cancer cell. Cells infected with Helicobacter pylori secrete isoform Fuc2A
brenda
-
the mean value of serum AFU activity in patients with hepatocellular carcinoma is significantly higher than in patients with cirrhosis, chronic hepatitis, other malignant neoplasms, other diseases and control subjects
brenda
-
one form tightly bound to the sperm plasma membrane, one form present in the gonad fluid
brenda
-
fucosidase is broadly distributed over the membrane systems of human sperm, but is relatively enriched within the equatorial segment. Cell-bound enzyme activity increases sharply following permeabilization of intact sperm, representing cryptic fucosidase that is relatively stable and corresponds with strong fluorescence in the equatorial segment and other sperm membranes. Fucosidase has a role in the intimate species signature interactions between sperm and oocyte
brenda
the enzyme is localized in the sperm plasma membrane over the acrosome and the tail
brenda
localized in the sperm plasma membrane over the acrosome and the tail
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of liver cancer cell, not detected in adjacent tissue
-
brenda
additional information
-
normally a lysosomal glycoprotein, released by secretion and/or cell lysis
-
brenda
-
increasing activity up to aggregation stage, not detectable in the growth phase
-
brenda
-
most induction of enzyme synthesis if cells grown in 2% active sludge hydrolyzate medium
-
brenda
-
induction of enzyme synthesis by addition of L-fucose to the medium
-
brenda
-
gastric cancer cells infected with Helicobacter pylori secrete isoform Fuc2A
-
brenda
-
maximal enzyme synthesis by growth on porcine gastric mucin containing media
-
brenda
-
is present to some degree in most of the sperm membranes, with a portion detectable on the outer surface of intact sperm. Larger quantities are present within cells, and particularly within the acrosomal compartment, and in the equatorial segment of the human sperm cell
brenda
-
fucosidase is broadly distributed over the membrane systems of human sperm, but is relatively enriched within the equatorial segment
brenda
-
overlying the acrosome, integral membrane protein terminally mannosylated, with the catalytic site oriented towards the extracellular space
brenda
-
specifically localized to the convex region of the prinicipal segment of testicular and cauda epididymal sperm heads
brenda
additional information
all the detectable activity is found in the non-membrane associated fraction comprising both the cytoplasmic and periplasmic content
-
brenda
additional information
-
all the detectable activity is found in the non-membrane associated fraction comprising both the cytoplasmic and periplasmic content
-
brenda
additional information
-
all the detectable activity is found in the non-membrane associated fraction comprising both the cytoplasmic and periplasmic content
-
-
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
physiological function
physiological function
enzyme is involved in gamete recognition. Recombinant enzyme interacts with alpha-L-fucose residues present on the micropyle of the Drosophila melanogaster eggshell, confirming that it is a good candidate as receptor involved in gamete interactions in fruit fly
physiological function
the enzyme is involved in metabolism of alpha-L-fucosylated molecules, compounds with a fundamental role in different life essential processes including immune response, fertilization
physiological function
the enzyme interacts with the egg coats through its core fucose residues and has a potential role in sperm-egg interactions in Drosophila
physiological function
the enzyme can hydrolyze the partially degraded fragment of fucoidan, which suggests that the enzyme may contribute to the final degradation of fucoidan in cells of Wenyingzhuangia fucanilytica
physiological function
the biological role of the enzyme may well be in the metabolism of short oligosaccharides in the periplasm, thereby indirectly contributing to the virulence of this organism
physiological function
-
besides its digestive role, the enzyme may also be important in host/parasite interactions
physiological function
WP_057784261.1
the enzyme is involved in fucoidan metabolism
physiological function
role of this glycosidase in sperm-egg interactions in Drosophila. The oligosaccharide recognition ability of the enzyme with defined carbohydrate chains that can functionally mimic egg glycoconjugates is analzed. The enzyme binds to fucose residue and in particular it prefers N-glycans carrying core alpha1,6-linked fucose and core alpha1,3-linked fucose in N-glycans carrying only a terminal mannose residue
physiological function
the enzyme may be involved in the catabolism of core-fucosylated N-glycans in Bombyx mori
physiological function
-
the biological role of the enzyme may well be in the metabolism of short oligosaccharides in the periplasm, thereby indirectly contributing to the virulence of this organism
-
physiological function
Paenibacillus thiaminolyticus CCM 3599
-
the enzyme is involved in metabolism of alpha-L-fucosylated molecules, compounds with a fundamental role in different life essential processes including immune response, fertilization
-
Show AA Sequence and Transmembrane Helices (6287 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
200000
230000
285000
38100
-
originates from the translational termination of the ribosome at the OCH codon of the fucA1 N-terminal ORF, Western blot analysis
50000
508000
51000
54000
55000
55971
-
1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry
56000
57000
57700
x * 57700, calculated, x * 80000, recombinant GFP fusion protein including His-tag, SDS-PAGE
59000
60000
67847
-
1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry
78700
-
originates from frameshifting in either site A or B of fucA1, Western blot analysis
80000
80000
x * 57700, calculated, x * 80000, recombinant GFP fusion protein including His-tag, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homooligomer
monomer
nonamer
oligomer
tetramer
additional information
?
x * 57700, calculated, x * 80000, recombinant GFP fusion protein including His-tag, SDS-PAGE
dimer
-
alpha-fucosidase I, 2 * 50000, SDS-PAGE, can aggregate to tetra- and hexamers
monomer
-
alpha-fucosidase II, 1 * 50000, SDS-PAGE, less-biologically active form, can aggregate to tetra- and hexamers
monomer
-
1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry
additional information
-
comparison of elution profile of enzyme from undifferentiated and differentiated HT-29 cells through gel filtration and SDS-PAGE, presence of a 50000 Da protein in both cultures
additional information
-
x * 59000, fase I, x * 56000 + x * 57000, fase II, SDS-PAGE
additional information
-
x * 59000, fase I, x * 56000 + x * 57000, fase II, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
first 25 amino acids near to the N-terminus have characteristics of a signal peptide. If the signal peptide is not removed, it will function as a membrane-anchoring domain
sialoglycoprotein
-
the enzyme occurs in different isoforms depending on the number of terminal sialic acid residues present on the glycoprotein molecules
additional information
-
treatment of enzyme with neuraminidase does not change its isoform profile
glycoprotein
-
contains 0.9% galactose, 1.9% mannose, 1.9% N-acetylglucosamine, 1.9% N-acetylneuraminic acid, w/w
glycoprotein
-
alpha-fucosidase I: sialoglycoprotein, mannose-rich: alpha-fucosidase II
glycoprotein
-
altered carbohydrate composition from enzymes of liver I-cell disease or pseudo-Hurler polydystrophy urine samples
glycoprotein
-
contains 7.4% glucose, 2.2% galactose, 1.8% mannose, 2.2% hexosamine
glycoprotein
-
4.7%, w/w, mannose content for isoform F1, 5%, w/w, mannose content for isoforms F2
glycoprotein
-
residues per tetramer: fucose 3.5, mannose 32, galactose 8: glucose 9, glucosamine 32, sialic acid 8
glycoprotein
-
isoform A derived by sialylation of isoform B near the end of epididymal maturation
glycoprotein
-
N-linked oligosaccharides only for the gonad fluid enzyme, sperm-bound enzyme not N- or O-linked glycosylated
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of mutant D229 soaked with aryl glycoside substrate 4-nitrophenyl alpha-L-fucoside. X-ray data at 1.95 A resolution reveal an unambiguous electron density for the unhydrolysed substrate, which is in the 1C4 conformation. Trapping of fucosyl-enzyme intermediate on the E288Q variant and analysis at 2.1 A. Again, the observed electron density reveals the trapped beta-L-fucosyl enzyme intermediate, here in the 3S1 conformation with the beta-linkage to the nucleophile Asp229
-
in complex with iminocyclitol inhibitors. Compounds show time-dependent, slow-binding inhibition. Inhibitors that have an extra substituent at C1 residing at the beta position adopt a product-like 1C4 chair conformation rather than the transition-state 3H4 half-chair conformation
-
the crystal structure of enzyme is determined at 2.5 A resolution by the MAD method
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D229N
-
inactive, mutation of the catalytic nucleophile. Crystallization data
E288Q
-
acid/base variant, crystallization data in complex with substrate 2-fluoro fucosyl fluoride
D229N
-
inactive, mutation of the catalytic nucleophile. Crystallization data
-
E288Q
-
acid/base variant, crystallization data in complex with substrate 2-fluoro fucosyl fluoride
-
G60D
missense enzyme variant observed in fucosidosis. The variant deviates in secondary structure from the wild-type enzyme. The catalytic activity of the enzyme variant on 4-nitrophenyl alpha-L-fucopyranoside is below the limit of detection for this assay
S150F
enzyme variant observed in fucosidosis. The variant deviates in secondary structure from the wild-type enzyme. The misfolded FucA1 disease variant is stabilized by the iminosugar inhibitor deoxyfuconojirimycin. The variant hydrolyzes 4-nitrophenyl alpha-L-fucopyranoside with similar KM values to the wild-type enzyme and exhibits a 13- to 20fold reduction in kcat
E235Q
decrease of the hydrolytic activity to 0.3% compared to the wild-type activity
H503A
hydrolytic activity of the mutant enzyme dropps to 3.4% compared to wild-type at a substrate concentration saturating the wild-type enzyme. The maximal reaction rate of the mutant enzyme is approximately seven times lower than that of the wild-type and its KM increased approximately 34times, resulting in a 238fold decrease of the catalytic efficiency
W392A
the oligomeric state of the protein is not changed by the mutation. The mutant enzyme is used in crystallization experiments, but it does not produce any crystals. For 4-nitrophenyl-alpha-L-fucoside, the mutation causes an increase in KM, while the maximal rate changed only slightly. When 2'-fucosyllactose is hydrolyzed, KM for the mutant-catalyzed reaction stays about the same, while the maximal rate decreases three times compared to the wild type. The mutation negatively affects the rate of reaction, which results in lower yields. It has no effect on the type of substrate the enzyme can deglycosylate. The mutation does not affect the ability of the enzyme to transfer L-fucose to a specific type of the acceptor molecule
D124G
D146G
D242G
E292G
E58G
H123G
H46G
D2224A
the mutant shows a greatly reduced activity compared with wild-type enzyme
E266A
-
the mutant exhibit very low hydrolytic activity with p-nitrophenyl alpha-L-fucoside
E66A
-
the mutant retains ability to catalyse the hydrolysis of p-nitrophenyl alpha-L-fucoside and fucosyl fluorid, the Km value is increase dramatically
F59A
-
slow tight-binding inhibition, affinity for compound 1 comparable to the wild-type level
G226S/T264A/Y267F/L322P
G226S/Y237H/T264A/L322P
L191A
-
slow tight-binding inhibition, kinetics like wild type, affinity for compound 1 comparable to the wild-type level
M210V/Y237H/T264A
M210V/Y237H/T264A/Y267F
M210V/Y237H/T264A/Y267F/L322P
M225A
-
slow tight-binding inhibition, kinetics like wild type, affinity for compound 1 comparable to the wild-type level
P196L/Y237H/Y267F
R147G/L322P
T264A
T264A/L322P
T264A/Y267F/L322P
Y237H/Y267F/L322P
additional information
D124G
-
kcat/Km at 65°C and pH 6.3 is 3.7fold lower than the wild-type value
D124G
-
kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 3.7fold lower than wild-type value
D146G
-
kcat/Km at 65°C and pH 6.3 is 1.5fold lower than the wild-type value
D146G
-
kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 1.5fold lower than wild-type value
D242G
-
azide activates the mutant, while it does not activate the wild-type enzyme, formate activates mutant higher than wild-type enzyme, the reaction catalysed by the mutant depends less on temperature
D242G
-
inactive, reactivating in the presence of sodium azide or sodium formate, reactivated enzyme maintains its thermophilicity
D242G
-
turnover number on 4-nitrophenyl-alpha-L-fucopyranoside is 0.0012times that of the wild type activity, 40fold reactivation by azide. The fucosyl-azide product obtained by the D242G mutant is in the inverted (beta-L-) configuration when compared with the substrate
E292G
-
kcat/Km at 65°C and pH 6.3 is 310.6fold lower than the wild-type value
E292G
-
kcat/Km at 65°C and pH 6.3 is 310.6fold lower than wild-type value
E292G
-
affects catalysis severely, unchanged affinity for 4-nitrophenyl-alpha-L-fucopyranoside but a 154fold reduction in the turnover number
E292G
-
kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 311fold lower than wild-type value
E58G
-
kcat/Km at 65°C and pH 6.3 is 1897fold lower than the wild-type value
E58G
-
kcat/Km is 10.8-3897fold lower than wild-type value depending on pH-value and buffer
E58G
-
kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 5395fold lower than wild-type value
H123G
-
kcat/Km at 65°C and pH 6.3 is 1719.8fold lower than the wild-type value
H123G
-
affinity for the substrate is remarkably different from that of the wild-type
H123G
-
kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 2929fold lower than wild-type value
H46G
-
kcat/Km at 65°C and pH 6.3 is 410fold lower than the wild-type value
H46G
-
affinity for the substrate is remarkably different from that of the wild-type, 607fold increase in the KM
H46G
-
kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 410fold lower than wild-type value
G226S/T264A/Y267F/L322P
the transferase/hydrolytic kinetic ratio is 22fold higher compared to wild-type ratio
G226S/Y237H/T264A/L322P
no significant modified transglycosylation properties
G226S/Y237H/T264A/L322P
the transferase/hydrolytic kinetic ratio is 34fold higher compared to wild-type ratio
M210V/Y237H/T264A
the transferase/hydrolytic kinetic ratio is 10fold higher compared to wild-type ratio
M210V/Y237H/T264A/Y267F
the transferase/hydrolytic kinetic ratio is 11fold higher compared to wild-type ratio
M210V/Y237H/T264A/Y267F/L322P
no significant modified transglycosylation properties
M210V/Y237H/T264A/Y267F/L322P
the transferase/hydrolytic kinetic ratio is 31.5fold higher compared to wild-type ratio
P196L/Y237H/Y267F
exhibits higher transglycosylation activity than the wild-type
P196L/Y237H/Y267F
the transferase/hydrolytic kinetic ratio is 7.5fold higher compared to wild-type ratio
R147G/L322P
exhibits higher transglycosylation activity than the wild-type
R147G/L322P
the transferase/hydrolytic kinetic ratio is 8.5fold higher compared to wild-type ratio
T264A
exhibits higher transglycosylation activity than the wild-type. Causes a reorientation of the amino acids that are in direct contact with the substrates, resulting in a better docking energy
T264A
the transferase/hydrolytic kinetic ratio is 13fold higher compared to wild-type ratio
T264A/L322P
the transferase/hydrolytic kinetic ratio is 20fold higher compared to wild-type ratio
T264A/Y267F/L322P
causes a reorientation of the amino acids that are in direct contact with the substrates, resulting in a better docking energy
T264A/Y267F/L322P
the transferase/hydrolytic kinetic ratio is 27.5fold higher compared to wild-type ratio
Y237H/Y267F/L322P
the transferase/hydrolytic kinetic ratio is 20.5fold higher compared to wild-type ratio
additional information
-
mutations of the catalytic residues with non-nucleophilic amino acids lead to strong reduction or even abolition of the enzymatic activity. Mutants can be reactivated in the presence of external nucleophiles such as sodium azide
additional information
-
slippery sequence in fucA1 A-AAA-AAT mutated in A-AAG-AAG-T (mutant fucA1B), shows reduced shifting efficiency. Sequence A-AAA-AAT mutated into A-AAG-AAT (single mutant fucA1sm) and C-AAGAAC (triple mutant fucA1tm). Mutant fucA1sm canceles the frameshifting site A and, in the same time, enhances the frameshifting efficiency of site B. In mutant fucA1tm abolished frameshifting
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 5
3 - 7
3.5 - 10
Pedobacter sp. CAU209
A0A7D3USC4
more than 80% of enzyme activity is retained after incubation in buffers from pH 3.5 to 10.0 for 0.5 h
4 - 11
4 - 6
4 - 7
4 - 8
4.5 - 6
5 - 6
5 - 8
additional information
-
comparison of pH stability of enzyme from undifferentiated and differentiated HT-29 cells, enzymes from undifferentiated and differentiated HT-29 cells are very stable at neutral and basic pH values
4
12 h, citrate buffer, enzyme retains 79.71% of its initial activity
4 - 8
-
stable in the presence of 0.05 mg/mg bovine serum albumin, 1 mM 2-mercaptoethanol
7
-
5% CO2 and high humidity or ambient air, 37°C, 24 h, 20-100% loss of activity, depending on conditions
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
45
50
50 - 55
50.15
melting temperature, mutant enzyme S150F, in presence of deoxyfuconojirimycin
51
-
rapid inactivation for alpha-L-fucosidase A, form B more heat-stable, stabilizing effect of bovine serum albumin, addition of 0.5 M potassium thiocyanate leads to more heat sensitivity for both forms
51.53
melting temperature, mutant enzyme G60D, in presence of deoxyfuconojirimycin
55
60
65
69.57
melting temperature, wild-type enzyme, in presence of deoxyfuconojirimycin
70
80
additional information
-
comparison of heat stability of enzyme from undifferentiated and differentiated HT-29 cells
25
QUH15933.1, QUH16573.1, QUH16649.1
48 h, enzyme retains more than 40% of its initial activity
30
QUH15933.1, QUH16573.1, QUH16649.1
48 h, enzyme retains 60% of its initial activity
30
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: above 2 h
30
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 98 min
37
-
gradual loss of activity after 6 min for the purified enzyme, in crude state: stable for 4 h
37
-
5% CO2 and high humidity or ambient air, pH 7.0, 24 h, 20-100% loss of activity, depending on conditions
40
QUH15933.1, QUH16573.1, QUH16649.1
48 h, enzyme retains more than 70% of its initial activity
40
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 56 min
40
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: above 2 h
40
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 28 min
50
-
alpha-fucosidase I: 50% loss of activity in 40 min, alpha-fucosidase II: 20% loss of activity in 40 min
50
-
native enzyme: 80% residual activity after 2 h, deglycosylated enzyme: 38% residual activity after 2 h
50
-
from mouse liver: more labile against inactivation than from human liver or mouse placental enzymes
50
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 14 min
50
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: less than 2 min
50
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: above 2 h
50
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 9 min
50
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 8 min
50
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 67 min
50 - 55
-
triphasic heat inactivation due to 3 different heat sensitive forms, forms I and II: less heat sensitive, form III: most heat sensitive
55
30 min, the enzyme maintains over 75% enzyme activity below 55°C
55
the enzyme maintains over 95% enzyme activity below 55°C
60
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: less than 2 min
60
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
half-life: 4 min
80
-
displays high stability maintaining 60% of the residual activity after 2 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization of the enzyme on Eupergyt CM offers the benefit of stability without compromising the yields of fucosylated compounds
-
In the presence of 0.015% Triton X-100 the frozen enzyme retains 100% activity after 3 months, in absence of 0.015% Triton X-100 the enzyme loses all activity after 2 weeks. In the presence or absence of 0.015% Triton X-100 and 2-4°C retains 100% activity after 2 weeks.
-
increased half-life to 23 h at 37°C and stability to repeated freezing and thawing by addition of 0.5 mg/ml bovine serum albumin
-
stabilizing effect by addition of 0.05 mM/ml bovine serum albumin, 1 mM 2-mercaptoethanol, 1 mM MgSO4, high protein concentrations required
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethyl formamide
dimethyl sulfoxide
dioxane
guanidine-HCl
-
the enzyme unfolds in a broad sigmoidal, cooperative unfolding transition, centered at about 2.2 M guanidinium chloride
guanidinium thiocyanate
-
the enzyme unfolds in a broad sigmoidal, cooperative unfolding transition, centered at about 2.2 M guanidinium thiocyanate
dimethyl formamide
-
more stable than the Aspergillus niger enzyme, no loss of activity up to 10%, v/v
dimethyl sulfoxide
-
more stable than the Aspergillus niger enzyme, no loss of activity up to 20%, v/v
dioxane
-
more stable than the Aspergillus niger enzyme, no loss of activity up to 10%, v/v
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, fully active after 29 days, 0-4°C, 10 mM Na2HPO4, pH 5.5, 0.02% NaN3, w/v, 100 mM L-fucose, 163 days
-
-20°C, in the presence of 1% fucose and presence or absence of 0.015% Triton X-100, 100% activity after 2 weeks
-
2-4°C, in the presence of 1% fucose and 0.015% Triton X-100, 100% activity after 3 months
-
37°C, 5% CO2, ambient air, pH 7.0, 24 h loss of activity and increase of the pH-value, membrane associated enzyme
-
37°C, 5% CO2, high humidity, 24 h, 70% loss of activity, enzyme in semen from storage in liquid nitrogen
-
37°C, 5% CO2, high humidity, 24 h, 90% loss of activity, enzyme in seminal plasma
-
37°C, 5% CO2, high humidity, pH 7.0, 24 h, 20% loss of activity, membrane associated enzyme
-
37°C, 5% CO2, high humidity, pH 7.0, 72 h, 30% loss of activity, membrane associated enzyme
-
4C, 0.2 M sodium citrate, pH 6.0, 20% polyethylene glycol, 2 months
4°C, 24 h, approximate 78% of initial activity is retained
4°C, 3 weeks, enzyme retains 100% of its activity when stored in presence of 20 mM CHAPS
-
4°C, enzyme freeze dried from aqueous solution containing 3 mM DTT and 5-20 mg/ml bovine serum albumin retains full activity for at least one year
-
4°C, in the presencen or absence of 50% glycerol, 0.05mg/ml bovine serum albumine or 2 mM beta-mercaptoethanol, enzyme from epimastigote extracts and from NaCl-solubilized membrane fractions are unstable
-
4C, 0.2 M sodium citrate, pH 6.0, 20% polyethylene glycol, 2 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
near homogeneity
partial
recombinant
to homogeneity, affinity chromatography
to homogeneity, affinity chromatography, isoelectric focusing, 2 forms, alpha-L-fucosidase A and B
-
to homogeneity, chromatography steps
to homogeneity, chromatography techniques
to homogeneity, isoelectric focusing
-
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha-L-fucosidase-encoding gene is identified by functional screening of a soil-derived metagenome library and expressed in Escherichia coli as recombinant 6xHis-tagged protein
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
cloned into pET21a vector, expression in Escherichia coli BL21 (DE3)
KXI90766.1
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli BL21 (DE3)
expression of a His-tagged enzyme in Escherichia coli BL21 (DE3)
into the pET21a vector, transformed into Escherichia coli Novablue cells, into plasmid pBTac2 and expressed in Escherichia coli XL1 blue MRF'
the Tffuc1 gene is cloned into pET22-b(C) vector and expressed in Escherichia coli as a C-terminally His6-tagged protein
through pET21b expression vector
wild-type and mutants as GST fusions expressed in Escherichia coli strain BL21(RB791)
-
expression in Escherichia coli BL21
QUH15933.1, QUH16573.1, QUH16649.1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
anterior midgut is the only midgut fraction that responds to the blood meal in terms of alpha-L-fucosidase production
-
there is a greater than 139fold increase in enzyme mRNA expression in breast tumor samples compared with normal breast tissue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
the enzyme may be used in glycoengineering to remove fucose from core-fucosylated N-glycans of glycoproteins, such as immunoglobulins, that are expressed in both insect and mammalian cells
diagnostics
food industry
A0A068B783, A0A068B2Y3, A0A068B3H5, A0A068B4L8, A0A068B4M2, A0A068B780, A0A068B1E8
the enzyme catalyse the transglycosylation reaction leading to production of fucosylated human milk oligosaccharides
medicine
synthesis
analysis
-
studies of structures and functions of glycoconjugates and oligosaccharides due to unique substrate specificity
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
analysis
-
low cost and accurate method for the detection and analytical determination of the activity of enzyme alpha-L-fucosidase. The method is based upon measuring the fluorescence intensity of the complex ion associate of the ion associate of rhodamine-B and the compound 2-chloro-4-nitrophenol at 580 nm in phosphate buffer, pH 5 against the reagent blank. The correlation between the fluorescence activity of the enzyme by the developed procedures and the standard method is positive and highly significant in patients and controls. The developed method is simple and proceeds without practical artifacts compared to the standard method
analysis
-
the facile recombinant expression procedure and the peculiar substrate specificities make these enzymes attractive candidates for bioanalytical applications
analysis
-
tool for the analysis and modification of human and animal milk oligosaccharides
analysis
-
the facile recombinant expression procedure and the peculiar substrate specificities make the enzyme an attractive candidates for bioanalytical applications
analysis
-
the facile recombinant expression procedure and the peculiar substrate specificities make these enzymes attractive candidates for bioanalytical applications
-
analysis
-
tool for the analysis and modification of human and animal milk oligosaccharides
-
analysis
-
the facile recombinant expression procedure and the peculiar substrate specificities make the enzyme an attractive candidates for bioanalytical applications
-
diagnostics
-
serum alpha-L-fucosidase is a useful marker in the diagnosis of hepatocellular carcinoma. The assay has high sensitivity and specificity. The procedure is simple, rapid, convenient, and can be adapted to automated clinical analyzers for use in large scale screening for early diagnosis of hepatocellular carcinoma
diagnostics
combined detection of the three tumor markers, serum alpha-L-fucosidase, alpha-fetoprotein and thymidine kinase 1 can play a complementary role in the diagnosis of hepatocellular carcinoma, and can significantly improve the sensitivity for the diagnosis of hepatocellular carcinoma
diagnostics
alpha-L-fucosidase is a valuable diagnostic biomarker for hepatocellular carcinoma. An ultrasensitive plasmonic biosensor converts plasmonic absorption to electrical current in order to detect alpha-L-fucosidase and cardiac troponin I using whole human blood in a real-time and parallel fashion. The detection limit is calculated to be 0.016 U/L for alpha-L-fucosidase and 0.015 ng/mL for cardiac troponin I, respectively. The developed biosensor exhibits a promising application for the prediction of cancers and many other diseases
medicine
-
recombinant enzyme will extend the proven efficiacy of enzyme replacement therapy in lysosomal storage disorders e.g. fucosidosis
medicine
-
the differentiation of HT-29 colon cancer cells can be used as a model to study the alteration of the enzyme alpha-L-fucosidase during the progression of the tumoural processs
medicine
-
quality of semen is affected in part by the loss in the activity of alpha-fucosidase, which may be useful in early diagnosis of the loss in reproductive capacity during the course of trypanosomiasis and fertility tests
medicine
-
has a role in the intimate species signature interactions between sperm and oocyte. Relevance for reproductive function in nature or in assisted reproductive technologies
medicine
-
progression-free survival significantly longer in high FUCA activity group than in low FUCA activity group, not correlated to clinical response to trastuzumab but maybe useful as biomarker for predicting progression-free survival for trastuzumab treatment, serum FUCA activity correlates with early detection in hepatocellular carcinoma
medicine
-
may be useful as a biomarker for predicting the progression-free survival of for trastuzumab treatment
medicine
-
gastric cancer cells infected with Helicobacter pylori secrete isoform Fuc2A. Fuc2A is essential for Helicobacter pylori adhesion, in particular to the gastric cancer- and duodenal ulcer-specific strains. FUCA2 significantly enhances the expression of Lewis x antigen in Helicobacter pylori, which is critical for bacterial cell adhesion in the pathogenesis and defense strategy to escape host surveillance
medicine
the enzyme is an indicator of poor prognosis for patients with advanced-stage triple-negative breast cancer
synthesis
-
the transfucosylation ability of one of the fucosidase isoform might be of interest for the synthesis of fucosides
synthesis
Pedobacter sp. CAU209
A0A7D3USC4
the enzyme mediates the fucosylation of lactose and provides an efficient enzymatic strategy to synthesize 2'-fucosyllactose either from artificial pNP-Fuc or natural apple pomace-derived XyG-oligos
synthesis
-
potential synthetic tool for enzymatic synthesis of fucosyl-N-acetylglucosamine disaccharides but also a possibility for the formation of regioisomeric products in glycosidase-catalyzed transglycosylation
synthesis
Pedobacter sp. CAU209
A0A7D3USC4
the enzyme catalyzed the synthesis of 3'-fucosyllactose and 2'-fucosyllactose through a transglycosylation reaction using 4-nitrophenyl alpha-L-fucopyranoside as donor and lactose as acceptor, and total conversion ratio is up to 85% at the optimized reaction conditions
synthesis
the enzyme could be a promising tool to prepare 2'-fucosyllactose and other novel glycosides. The enzyme is capable of transferring the fucosyl residue to other glycosyl receptors with the generation of novel fucosylated compounds
synthesis
-
promising enzyme source for the biosynthesis of 2'-fucosyllactose, an important nutrient in human milk that stimulates beneficial microbiota and prevents infection
synthesis
-
application of the enzyme to synthesize fucosyllactose through transfucosylation reaction, which proved to be an alternative route for the production of fucosyl-oligosaccharide
synthesis
-
application of the enzyme to synthesize fucosyllactose through transfucosylation reaction, which proved to be an alternative route for the production of fucosyl-oligosaccharide
-
synthesis
-
potential synthetic tool for enzymatic synthesis of fucosyl-N-acetylglucosamine disaccharides but also a possibility for the formation of regioisomeric products in glycosidase-catalyzed transglycosylation
-
synthesis
-
the transfucosylation ability of one of the fucosidase isoform might be of interest for the synthesis of fucosides
-
synthesis
Flavobacterium algicola 12076
-
the enzyme could be a promising tool to prepare 2'-fucosyllactose and other novel glycosides. The enzyme is capable of transferring the fucosyl residue to other glycosyl receptors with the generation of novel fucosylated compounds
-
synthesis
-
promising enzyme source for the biosynthesis of 2'-fucosyllactose, an important nutrient in human milk that stimulates beneficial microbiota and prevents infection
-
EXTERNAL LINKS (specific for EC-Number 3.2.1.51)
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Release 2026.1 (March 2026)
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