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Information on EC 3.2.1.63 - 1,2-alpha-L-fucosidase for references in articles please use BRENDA:EC3.2.1.63Word Map on EC 3.2.1.63
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H2O = L-fucose + methyl beta-D-galactoside
; high specificity for non-reducing terminal L-fucose residues alpha 1,2-linked to D-galactose residues
-
-
-
hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
stepwise reaction mechanism, the first step is the proton transfer from N423 to D766, and the second step involves the hydrolysis reaction via the inversion mechanism catalyzed by the amide group of N423. Assisted by D766, N423 serves as the general base to activate the water molecule to attack the anomeric carbon center. E566 is the general acid to facilitate the cleavage of glycosidic bond between L-fucose and galactose units. The intrinsic resonance structure for the side chain amide group of the asparagine residue is the origin to the catalytic activity
-
hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
-
-
-
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hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
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-
-
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hydrolysis of O-glycosyl bond
-
-
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2-alpha-L-fucopyranosyl-beta-D-galactoside fucohydrolase
Highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by a 1,2-alpha-linkage. Not identical with EC 3.2.1.111 1,3-alpha-L-fucosidase.
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alpha-(1--> 2)-L-fucosidase
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-
-
-
alpha-L-fucosidase II
-
-
-
-
fucosidase, 1,2-alpha-L-
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-
-
-
additional information
-
AfcA, an inverting glycosidase, belongs to the glycoside hydrolase family GH95
1,2-alpha-L-fucosidase
-
-
-
-
1,2-alpha-L-fucosidase
-
-
AfcA
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AfcA
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from glycoside hydrolase family 95
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brenda
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brenda
Bacillus fulminans
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-
brenda
strain: VIII-210
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-
brenda
strain: VIII-240
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-
brenda
strain: VIII-240
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brenda
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brenda
-
J9UN47
UniProt
brenda
no activity in Bifidobacterium longum
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-
-
brenda
almond
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-
brenda
i.e. Ruminococcus AB strain VI-268, ATCC35913
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-
brenda
strains: VIII-239 and IX-70
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brenda
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GenBank
brenda
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SwissProt
brenda
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brenda
strain JCM1254
SwissProt
brenda
strain JCM1254, gene afcA
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-
brenda
strain: VIII-210
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-
brenda
strains D119 and L22
B2C4H2
UniProt
brenda
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physiological function
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AfcA plays essential role in degrading alpha1,2-fucosylated milk oligosaccharides and also glycoconjugates, in the gastrointestinal tracts of the host
evolution
J9UN47
the enzyme belongs to the glycosyl hydrolase family 29, GH29, of retaining fucosidases
evolution
-
the enzyme belongs to the glycosyl hydrolase family 29, GH29, of retaining fucosidases
additional information
J9UN47
the enzyme shows active-site conformational flexibility, structure-function analysis, overview
additional information
-
the side chain amide group of the asparagine residue, N423, is proposed to act as the general base to activate this water nucleophile, with assistance provided by a nearby D766. In the crystal structure, the D766 is hydrogen bonds with the N423
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2'-fucosyllactose + H2O
?
-
hydrolysis by the Fuc domain of AfcA. N423 and D766 are critical for activating an attacking water molecule and N421 is critical for maintaining the water molecule and the side-chain of E566 (a general acid) in their proper orientations
-
-
?
2'-fucosyllactose + H2O
fucose + lactose
2'-fucosyllactose + H2O
L-fucose + lactose
2'-L-fucosyllactose + H2O
L-fucose + lactose
2-fucosyllactitol + H2O
fucose + lactitol
-
-
-
-
-
2-O-alpha-L-fucopyranosyl-D-galactose + H2O
L-fucose + galactose
4-nitrophenyl-alpha-L-fucoside + H2O
4-nitrophenol + L-fucose
J9UN47
-
-
-
?
alpha-Fuc-(1-2)-beta-Gal-(1-3)-beta-GlcNAc-(1-3)-beta-Gal-(1-4)-beta-Glu + H2O
alpha-L-fucose + beta-Gal-(1-3)-beta-GlcNAc-(1-3)-beta-Gal-(1-4)-beta-Glu
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i.e. lacto-N-fucopentaose I
-
?
beta-L-fucosyl fluoride + lactose + H2O
?
-
Hehre resynthesis-hydrolysis is catalyzed by the wild-type Fuc domain of AfcA. Conversion of the inverting alpha-glycosidase to a glycosynthase
-
-
?
blood group substance H + H2O
?
Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc + H2O
L-fucose + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
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i.e. lacto-N-fucopentaose I, at 29% of the activity with 2'-fucosyllactose
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-
?
Fucalpha(1-2)Galbeta(1-4)Glc + H2O
L-fucose + Galbeta(1-4)Glc
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i.e. 2'-fucosyllactose
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-
?
Galbeta(1-4)(Fucalpha(1-3))Glc + H2O
?
-
i.e. 3-fucosyllactose, at 0.85% of the activity with 2'-fucosyllactose
-
-
?
lacto-N-fucopentaose I
?
Bacillus fulminans
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-
-
-
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lacto-N-fucopentaose I + H2O
?
methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H2O
L-fucose + methyl beta-D-galactoside
mucin + H2O
?
B2C4H2
-
-
-
?
O-alpha-L-fucose-(1-2)-O-beta-D-galactose-(1-4)-D-glucose + H2O
L-fucose + lactose
porcine gastric mucin + H2O
?
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at 33% of the activity with 2'-fucosyllactose
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-
?
submaxillary glycoprotein + H2O
L-fucose + ?
-
degradation of blood group substances
-
?
additional information
?
-
2'-fucosyllactose + H2O
fucose + lactose
Bacillus fulminans
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-
-
-
-
2'-fucosyllactose + H2O
fucose + lactose
-
-
-
-
?
2'-fucosyllactose + H2O
fucose + lactose
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-
-
-
2'-fucosyllactose + H2O
L-fucose + lactose
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-
-
?
2'-fucosyllactose + H2O
L-fucose + lactose
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simulation of the reaction by the combined quantum mechanical and molecular mechanical approach. Molecular dynamics simulations and free energy profiles support that the overall reaction is a stepwise mechanism
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-
?
2'-fucosyllactose + H2O
L-fucose + lactose
J9UN47
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-
-
?
2'-L-fucosyllactose + H2O
L-fucose + lactose
reaction with recombinant Fuc domain
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-
?
2'-L-fucosyllactose + H2O
L-fucose + lactose
reaction with recombinant Fuc domain
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-
?
2-O-alpha-L-fucopyranosyl-D-galactose + H2O
L-fucose + galactose
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-
-
?
2-O-alpha-L-fucopyranosyl-D-galactose + H2O
L-fucose + galactose
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-
-
?
blood group substance H + H2O
?
74% of the activity with 2'-fucosyllactose, reaction with recombinant Fuc domain
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?
blood group substance H + H2O
?
74% of the activity with 2'-fucosyllactose, reaction with recombinant Fuc domain
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-
?
lacto-N-fucopentaose I + H2O
?
61% of the activity with 2'-fucosyllactose, reaction with recombinant Fuc domain
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-
?
lacto-N-fucopentaose I + H2O
?
61% of the activity with 2'-fucosyllactose, reaction with recombinant Fuc domain
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-
?
methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H2O
L-fucose + methyl beta-D-galactoside
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-
-
?
methyl-2-alpha-L-fucopyranosyl-beta-D-galactoside + H2O
L-fucose + methyl beta-D-galactoside
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-
-
-
?
mucin + H2O
L-fucose + ?
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porcine and canine, submaxillary
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mucin + H2O
L-fucose + ?
Bacillus fulminans
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porcine submaxillary and glycopeptide of desialyzed mucin
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O-alpha-L-fucose-(1-2)-O-beta-D-galactose-(1-4)-D-glucose + H2O
L-fucose + lactose
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i.e. 2-O-alpha-L-fucosyllactose
-
?
O-alpha-L-fucose-(1-2)-O-beta-D-galactose-(1-4)-D-glucose + H2O
L-fucose + lactose
Bacillus fulminans
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i.e. 2-O-alpha-L-fucosyllactose
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O-alpha-L-fucose-(1-2)-O-beta-D-galactose-(1-4)-D-glucose + H2O
L-fucose + lactose
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i.e. 2-O-alpha-L-fucosyllactose
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?
additional information
?
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highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by 1,2-alpha linkage
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additional information
?
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inductively produced in culture medium containing porcine gastric mucin, weakly induced by L-fucose and D-arabinose, but not by other sugars including D-glucose
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additional information
?
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the recombinant Fuc domain shows no activity with 3-fucosyllactose, lacto-N-fucopentaose II, lacto-N-fucopentaose V and blood group substance B
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additional information
?
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the recombinant Fuc domain shows no activity with 3-fucosyllactose, lacto-N-fucopentaose II, lacto-N-fucopentaose V and blood group substance B
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additional information
?
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the recombinant Fuc domain shows no activity with 3-fucosyllactose, lacto-N-fucopentaose II, lacto-N-fucopentaose V and blood group substance B
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-
additional information
?
-
the recombinant Fuc domain shows no activity with 3-fucosyllactose, lacto-N-fucopentaose II, lacto-N-fucopentaose V and blood group substance B
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-
additional information
?
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not: p-nitrophenyl-alpha-L-fucoside, 2-O-, 3-O- and 4-O-alpha-L-fucopyranosylfucoses, 3-O- and 4-O-alpha-L-fucopyranosyl-D-galactoses, action on oligosaccharides and glycoproteins, not: simple methyl nitrophenyl fucosides
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additional information
?
-
J9UN47
substrate specificity, overview. No activity with 3-fucosyllactose. The nezyme is also active on xyloglucan
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-
-
additional information
?
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highly specific for non-reducing terminal L-fucose residues linked to D-galactose residues by 1,2-alpha linkage
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-
-
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2'-fucosyllactose + H2O
L-fucose + lactose
-
-
-
-
?
submaxillary glycoprotein + H2O
L-fucose + ?
-
degradation of blood group substances
-
?
additional information
?
-
-
inductively produced in culture medium containing porcine gastric mucin, weakly induced by L-fucose and D-arabinose, but not by other sugars including D-glucose
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-
-
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CaCl2
-
slight activation
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(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
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(2R,3S,4S,5R,6S)-2-benzyl-6-methylpiperidine-3,4,5-triol
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(2S,3R,4S,5S,6R)-2-methyl-6-(propan-2-yl)piperidine-3,4,5-triol
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2-(1H-indol-3-yl)-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
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2-cyclopentyl-2-phenyl-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
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3-(1H-indol-3-yl)-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]propanamide
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9-oxo-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-9H-fluorene-1-carboxamide
-
BaCl2
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1 mM, 63% inhibition
CaCl2
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1 mM, 60% inhibition
CoCl2
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1 mM, 38% inhibition
CuSO4
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1 mM, 86% inhibition
cysteine
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1 mM, 27% inhibition
D-mannose
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10 mM, 22% inhibition
deoxycholate
Bacillus fulminans
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-
dithiothreitol
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1 mM, 22% inhibition
FeSO4
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1 mM, complete inhibition
glutathione
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1 mM, 21% inhibition
L-fucose
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10 mM, 91% inhibition
lactose
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10 mM, 27% inhibition
Mn2+
Bacillus fulminans
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-
N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1-benzofuran-2-carboxamide
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N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1H-indole-2-carboxamide
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N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
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NEM
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0.1 mM, 24% inhibition
NiSO4
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1 mM, 59% inhibition
p-chloromercuribenzoate
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p-Chloromercuriphenylsulfonate
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1 mM, 12% inhibition
p-mercuribenzoate
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1 mM, 23% inhibition
SDS
Bacillus fulminans
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-
ZnCl2
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1 mM, 43% inhibition
EDTA
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1 mM, 23% inhibition
EDTA
Bacillus fulminans
-
-
Hg2+
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0.1 mM, complete inhibition
Hg2+
Bacillus fulminans
-
-
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maltose
-
10 mM, 10% activation
NEM
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1 mM, 20% activation
Sodium azide
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for D766A mutant only
additional information
B2C4H2
mucin highly induces gene expression
-
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0.53 - 2.5
2'-fucosyllactose
0.675
2-fucosyllactitol
-
-
0.035 - 17
2-fucosyllactose
2
alpha-Fuc-(1-2)-beta-Gal-(1-3)-beta-GlcNAc-(1-3)-beta-Gal-(1-4-)-beta-Glc
Bacillus fulminans
-
-
-
1.6
glycopeptide desialyzed porcine submaxillary mucin
Bacillus fulminans
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-
-
0.175
glycoprotein
Bacillus fulminans
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hog, submaxillary
0.083
methyl 2-O-alpha-L-fucopyranosyl-beta-D-galactoside
-
-
0.33
porcine submaxillary mucin
Bacillus fulminans
-
-
-
additional information
additional information
J9UN47
steady-state kinetics of deglycosylated and glycosylated enzyme, overview
-
0.53
2'-fucosyllactose
Fuc domain
2.5
2'-fucosyllactose
Bacillus fulminans
-
-
0.035
2-fucosyllactose
-
N421A mutant
0.056
2-fucosyllactose
-
N421G mutant
0.075
2-fucosyllactose
-
N423G mutant
0.089
2-fucosyllactose
-
D766A mutant
0.091
2-fucosyllactose
-
wild type
0.16
2-fucosyllactose
-
E566A mutant
0.19
2-fucosyllactose
-
D766E mutant
0.32
2-fucosyllactose
-
N423D mutant
17
2-fucosyllactose
-
E485A mutant
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0.0000163
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
pH and temperature not specified in the publication
0.005
(2R,3S,4S,5R,6S)-2-benzyl-6-methylpiperidine-3,4,5-triol
pH and temperature not specified in the publication
0.006
(2S,3R,4S,5S,6R)-2-methyl-6-(propan-2-yl)piperidine-3,4,5-triol
pH and temperature not specified in the publication
0.000000475
2-(1H-indol-3-yl)-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
pH and temperature not specified in the publication
0.001005
2-cyclopentyl-2-phenyl-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
pH and temperature not specified in the publication
0.000000105
3-(1H-indol-3-yl)-N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]propanamide
pH and temperature not specified in the publication
0.000000441
N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1-benzofuran-2-carboxamide
pH and temperature not specified in the publication
0.000000427
N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]-1H-indole-2-carboxamide
pH and temperature not specified in the publication
0.00000447
N-[[(2R,3S,4S,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl]methyl]acetamide
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.12
Bacillus fulminans
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 8
-
pH 5.0: about 60% of maximal activity, pH 8.0: about 35% of maximal activity
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37
-
assay at
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20 - 60
-
20°C: about 45% of maximal activity, 60°C: about 45% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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inductively produced in culture medium containing porcine gastric mucin, weakly induced by L-fucose and D-arabinose, but not by other sugars including glucose
brenda
-
-
brenda
additional information
-
commercial preparation
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70000 - 80000
Bacillus fulminans
-
gel filtration
81000
-
2 * 81000, SDS-PAGE
200000
-
value greater than, multiple isozymic forms
205000
x * 205000, calculated from sequence
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?
-
x * 205000, calculated from sequence
dimer
-
2 * 81000, SDS-PAGE
monomer
J9UN47
crystal structure analysis, solution small angle x-ray scattering
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glycoprotein
J9UN47
prediction of three N-glycosylation sites on Asn187, Asn280, and Asn401 (residues numbered for the protein without signal peptide). Deglycosylation of the recombinant enzyme expressed from Pichia pastoris by treatment with Endo H or peptide N-glycosidase F. The N-glycans on Asn-280 of the TIM barrel domain retained a chitobiose core and high mannose type substitutions, GlcNAc-beta1-4GlcNAc-beta1-4(Man-alpha1-6)Man-alpha1-3Man-alpha1-2Man-alpha1-2Man, possibly protected from EndoH by the beta,gamma-crystallin domain. The other two N-glycosylation sites Asn187 and Asn401 are each attached to one GlcNAc residue, indicative of Endo H cleavage. No effect of Endo H deglycosylation on the catalytic efficiency with small fucosylated substrates or on thermal stability, but higher solubility of the glycosylated than the deglycosylated enzyme
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of the AfcA catalytic domain in unliganded and complexed forms with the inhibitor deoxyfuconojirimycin, the substrate 2-fucosyllactose, and the products L-fucose and lactose at 1.12-2.10 A resolution
-
purified deglycosylated recombinant enzyme in open or closed form or complexed with L-fucose, sitting-drop vapor diffusion method or batch method, several different crystal forms, mixing 0.001 ml of 14-16 mg/ml Endo H-treated fucosidase in 25 mM Tris, pH 7.5, with 0.001 ml of precipitant solution containing 0.1 M Tris, pH 8.0, and either 30% or 40% w/v PEG MME 2000, 20°C, 2-3 days, X-ray diffraction structure determination and analysis at 1.38-156 A resolution, molecular replacement method
J9UN47
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5 - 9
-
37°C, 6 h, stable
665770
6.5 - 7.5
-
Fuc domain is stable for 12 h
665375, 665768
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35
30 min, Fuc domain is stable below
70
Bacillus fulminans
-
5 min, 77% loss of activity
80
Bacillus fulminans
-
5 min, complete loss of activity
50
-
pH 7.0, 10 min, stable up to
50
Bacillus fulminans
-
5 min, no loss of activity
60
-
pH 7.0, 10 min, about 80% loss of activity
60
Bacillus fulminans
-
5 min, 7% loss of activity
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dialysis, water: rapid loss of activity, buffers: precipitation with considerable inactivation below pH 5.5
-
lyophilization causes inactivation
-
repeated freezing and thawing causes inactivation
-
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of the recombinant protein by saturated ammonium sulfate precipitation and Q sepharose fast flow, CHT ceramic hydroxyapatite and gel filtration column chromatography
-
recombinant enzyme from Pichia pastoris by gel filtration and anion exchange chromatography, recombinant His6-tagged and MBP-fused crystallin domain from Escherichia coli by nickel affinity chromatography
J9UN47
wild-type and mutant derivatives of the catalytic domain of AfcA (Fuc domain)
-
-
-
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expression of 1,2-alpha-L-fucosidase in Escherichia coli, expression of the Fuc domain (responsible for fucosidase activity) as a hexahistidine-tagged protein in Escherichia coli
gene afcA, expression in Escherichia coli and in enzyme-deficient Bifidobacterium longum strain 105-A which renders the transformant able to utilize 2'-fucosyllactose as the sole carbon source
-
overexpression in Escherichia coli, selenomethionine-substituted protein
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sequence comparisons, recombinant enzyme expression of the enzyme including its native signal peptide from pPICZAalpha without the C-terminal Myc/His6 tags in Pichia pastoris, expression of the His6-tagged crystallin domain, residues 501-585, of the enzyme fused to maltose-binding protein at the N-terminus in Escherichia coli
J9UN47
wild-type and mutant derivatives of the catalytic domain of AfcA (Fuc domain)
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D766A
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site directed mutagenesis
D766E
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site directed mutagenesis
D766G
-
most effectively synthesizes 2'-fucosyllactose
E485A
-
site directed mutagenesis
E566A
-
site directed mutagenesis
N421A
-
site directed mutagenesis
N421G/N423G
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site directed mutagenesis
N423D
-
site directed mutagenesis
N421G
-
site directed mutagenesis
N421G
-
synthesizes 2'-fucosyllactose
N423G
-
site directed mutagenesis
N423G
-
synthesizes 2'-fucosyllactose
N423G
-
mutagenesis simulation, the mutant still has significant activity
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medicine
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1,2-alpha-L-fucosynthase, derived from an inverting alpha-glycosidase (AfcA) and from a glycosidase with an unusual reaction mechanism, may serve as a promising tool to create biologically active compounds that can be used not only for prebiotics but also for clinical treatments aimed to regulate various cellular processes and infectious diseases
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A9WRZ2_RENSM
Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
302
32506
TrEMBL
L7VK99_CLOSH
Clostridium stercorarium subsp. stercorarium (strain ATCC 35414 / DSM 8532 / NCIMB 11754)
761
86415
TrEMBL
A0A1U7CSZ3_9BACT
823
89968
TrEMBL
A9WRZ1_RENSM
Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
283
32161
TrEMBL
A9WRZ0_RENSM
Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
187
19611
TrEMBL
Q9WYE2_THEMA
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
449
52205
TrEMBL
Q6JV24_BIFBI
1959
205511
TrEMBL
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Bahl, O.P.
Glycosidases of Aspergillus niger. II. Purification and general properties of 1,2-alpha-L-fucosidase
J. Biol. Chem.
245
299-304
1970
Aspergillus niger
brenda
Larson, G.; Falk, P.; Hoskin, L.C.
Degradation of human intestinal glycosphingolipids by extracellular glycosidases from mucin-degrading bacteria of the human fecal flora
J. Biol. Chem.
263
10790-10798
1988
Bifidobacterium bifidum, Bifidobacterium bifidum VIII-210, Bifidobacterium longum subsp. infantis, Bifidobacterium longum subsp. infantis VIII-240, Ruminococcus gnavus, Ruminococcus torques
brenda
Aminoff, D.; Frurukawa, K.
Enzymes that destroy blood group specificity. I. Purification and properties of alpha-L-fucosidase from Clostridium perfringens
J. Biol. Chem.
245
1659-1669
1970
Clostridium perfringens
brenda
Kochibe, N.
Purification and properties of alpha-L-fucosidase from Bacillus fulminans
J. Biochem.
74
1141-1149
1973
Bacillus fulminans
brenda
Ogata-Arakawa, M.; Muramatsu, T.; Kobata, A.
alpha-L-Fucosidases from almond emulsin: characterization of the two enzymes with different specificities
Arch. Biochem. Biophys.
181
353-358
1977
Prunus dulcis
brenda
Katayama, T.; Sakuma, A.; Kimura, T.; Makimura, Y.; Hiratake, J.; Sakata, K.; Yamanoi, T.; Kumagai, H.; Yamamoto, K.
Molecular cloning and characterization of Bifidobacterium bifidum 1,2-alpha-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95)
J. Bacteriol.
186
4885-4893
2004
Bifidobacterium bifidum, Bifidobacterium bifidum (Q6JV24)
brenda
Katayama, T.; Fujita, K.; Yamamoto, K.
Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins
J. Biosci. Bioeng.
99
457-465
2005
Bifidobacterium bifidum, Bifidobacterium bifidum (Q6JV24)
brenda
Miura, T.; Okamoto, K.; Yanase, H.
Purification and characterization of extracellular 1,2-alpha-L-fucosidase from Bacillus cereus
J. Biosci. Bioeng.
99
629-635
2005
Bacillus cereus
brenda
Ruas-Madiedo, P.; Gueimonde, M.; Fernandez-Garcia, M.; de los Reyes-Gavilan, C.G.; Margolles, A.
Mucin degradation by Bifidobacterium strains isolated from the human intestinal microbiota
Appl. Environ. Microbiol.
74
1936-1940
2008
Bifidobacterium bifidum (B2C4H2)
brenda
Nagae, M.; Tsuchiya, A.; Katayama, T.; Yamamoto, K.; Wakatsuki, S.; Kato, R.
Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum
J. Biol. Chem.
282
18497-18509
2007
Bifidobacterium bifidum
brenda
Wada, J.; Honda, Y.; Nagae, M.; Kato, R.; Wakatsuki, S.; Katayama, T.; Taniguchi, H.; Kumagai, H.; Kitaoka, M.; Yamamoto, K.
1,2-alpha-l-Fucosynthase: a glycosynthase derived from an inverting alpha-glycosidase with an unusual reaction mechanism
FEBS Lett.
582
3739-3743
2008
Bifidobacterium bifidum
brenda
Ashida, H.; Miyake, A.; Kiyohara, M.; Wada, J.; Yoshida, E.; Kumagai, H.; Katayama, T.; Yamamoto, K.
Two distinct alpha-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates
Glycobiology
19
1010-1017
2009
Bifidobacterium bifidum, no activity in Bifidobacterium longum
brenda
Wu, H.; Ho, C.; Ko, T.; Popat, S.; Lin, C.; Wang, A.
Structural basis of alpha-fucosidase inhibition by iminocyclitols with Ki values in the micro- to picomolar range
Angew. Chem.
49
337-340
2010
Thermotoga maritima (Q9WYE2)
brenda
Cao, H.; Walton, J.D.; Brumm, P.; Phillips, G.N.
Structure and substrate specificity of a eukaryotic fucosidase from Fusarium graminearum
J. Biol. Chem.
289
25624-25638
2014
Fusarium graminearum, Fusarium graminearum (J9UN47)
brenda
Liu, J.; Zheng, M.; Zhang, C.; Xu, D.
Amide resonance in the catalysis of 1,2-alpha-L-fucosidase from Bifidobacterium bifidum
J. Phys. Chem. B
117
10080-10092
2013
Bifidobacterium bifidum
brenda
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