Information on EC 3.2.1.51 - alpha-L-fucosidase

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

EC NUMBER
COMMENTARY
3.2.1.51
-
RECOMMENDED NAME
GeneOntology No.
alpha-L-fucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an alpha-L-fucoside + H2O = L-fucose + an alcohol
show the reaction diagram
-
-
-
-
an alpha-L-fucoside + H2O = L-fucose + an alcohol
show the reaction diagram
mechanism
-
an alpha-L-fucoside + H2O = L-fucose + an alcohol
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
the enzyme cleaves alpha1-6-, alpha1-3-, alpha1-4- and alpha1-2-O-fucolsyl bonds in fucosylated oligosaccharides
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis
-
-
hydrolysis
-
of glycosidic bond
hydrolysis of O-glycosyl bond
-
-
-
-
transglycosylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
Other glycan degradation
-
SYSTEMATIC NAME
IUBMB Comments
alpha-L-fucoside fucohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acid hydrolase
-
-
alfA
B3W8U6
gene name
alfB
B3WB08
gene name
alfC
B3WBB5
gene name
alpha-fuc
-
encoded by an interrupted gene
alpha-fuc
-
-
alpha-fucosidase
-
-
-
-
alpha-L fucosidase
-
-
alpha-L-fucosidase
-
-
alpha-L-fucosidase
-
ALF
alpha-L-fucosidase
P04066
-
alpha-L-fucosidase
-
-
alpha-L-fucosidase
Q9WYE2
-
alpha-L-fucosidase 2
Q99KR8
-
alpha-L-fucosidase 2
Q6AYS4
-
alpha-L-fucosidase I
P48300
-
alpha-L-fucosidase I
P04066
-
alpha-L-fucosidase I
Q99LJ1
-
alpha-L-fucosidase I
P17164
-
Alpha-L-fucoside fucohydrolase
-
-
-
-
Alpha-L-fucoside fucohydrolase
-
-
Alpha-L-fucoside fucohydrolase
P04066
-
Alpha-L-fucoside fucohydrolase
Q99LJ1
-
alpha-L-fucoside fucohydrolase 2
Q99KR8
-
alpha-L-fucoside fucohydrolase 2
Q6AYS4
-
FucA
Q9VTJ4
gene name
FucA
-
-
Fuca1
P04066
-
Fuca1
Q99LJ1
-
Fuca1
P17164
-
Fuca2
-
-
Fuca2
Q99KR8
-
Fuca2
Q6AYS4
-
fucosidase, alpha-L-1, tissue
Q5EAL9
-
h-Fuc
P04066
-
serum AFU
-
-
serum alpha-L-fucosidase
-
-
TMalphafuc
Q9WYE2
-
CAS REGISTRY NUMBER
COMMENTARY
9037-65-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
Bacillus fulminans
-
-
-
Manually annotated by BRENDA team
probable alpha-L-fucosidase; YCH46, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
putative alpha-L-fucosidase protein; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
putative alpha-L-fucosidase; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
putative exported alpha-L-fucosidase protein; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
putative exported hydrolase; NCTC 9343, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
YCH46, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
VPI5482, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Bacteroides thetaiotaomicron Bt2970
strain Bt2970
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
putative alpha-L-fucosidase, precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
putative uncharacterized protein; CB15, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
probable glycosyl hydrolase; strain 13, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Clostridium perfringens 13
probable glycosyl hydrolase; strain 13, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Chinese hamster ovary cells
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SWissProt
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
isoform FucA2
-
-
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
tissue alpha-L-fucosidase precursor
SwissProt
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes; putative uncharacterized protein; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
Syrian hamster
-
-
Manually annotated by BRENDA team
Microscilla sp.
MS119, putative fucosidase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Microscilla sp.
MS120, putative fucosidase; RE1, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
MS119, putative fucosidase; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
MS120, putative fucosidase; RE1, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
no activity in Trichomonas foetus
-
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
marine mollusk
-
-
Manually annotated by BRENDA team
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
alpha-L-fucosidase, putative; W83, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
glycosyl hydrolase, putative alpha-L-fucosidase; KPA171202, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
KPA171202, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
precursor; comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
SH1, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
-
Q86FH9
SwissProt
Manually annotated by BRENDA team
clone ZZZ276 mRNA sequence; comparative and phylogenetic analysis of alpha-L-fucosidase genes
Q86FH9
SwissProt
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
strain R6, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
strain TIGR4 comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
putative glycosyl hydrolase; strain A3(2), comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
OH11242
-
-
Manually annotated by BRENDA team
strain 142, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Streptomyces sp. 142
strain 142, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Streptomyces sp. OH11242
OH11242
-
-
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
; comparative and phylogenetic analysis of alpha-L-fucosidase genes
-
-
Manually annotated by BRENDA team
alpha-L-fucosidase, putative
GenBank
Manually annotated by BRENDA team
alpha-L-fucosidase, putative; comparative and phylogenetic analysis of alpha-L-fucosidase genes
GenBank
Manually annotated by BRENDA team
strain Y5
-
-
Manually annotated by BRENDA team
strain Y5
-
-
Manually annotated by BRENDA team
alpha-L-fucosidase family protein; ATCC35405, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
Venus mercenaria
-
-
-
Manually annotated by BRENDA team
strain pv. Citri str.306, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
pv. campestris str. 8004, comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
comparative and phylogenetic analysis of alpha-L-fucosidase genes
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
-
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
low activity
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
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
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
alpha-fucosidase II highly active
-
?
2-chloro-4-nitrophenyl alpha-L-fucopyranoside + H2O
2-chloro-4-nitrophenol + L-fucose
show the reaction diagram
-
pH 6.8, 37C
-
-
?
2-deoxy-2-fluoro-alpha-L-fucosyl fluoride + H2O
fluoride + 2-deoxy-2-fluoro-alpha-L-fucose
show the reaction diagram
Q9WYE2, -
-
-
-
-
2-fluoro-4-nitrophenyl alpha-L-fucopyranoside + H2O
2-fluoro-4-nitrophenol + L-fucose
show the reaction diagram
-
pH 6.8, 37C
-
-
?
2-methyl-4-nitrophenyl alpha-L-fucopyranoside + H2O
2-methyl-4-nitrophenol + L-fucose
show the reaction diagram
-
pH 6.8, 37C
-
-
?
2-nitrophenyl alpha-L-fucopyranoside + H2O
2-nitrophenol + alpha-L-fucopyranose
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
2alpha-fucosyl-lactitol + H2O
?
show the reaction diagram
-
-
-
-
-
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
very low activity
-
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
low activity
-
?
4-methylumbelliferyl alpha-L-fucopyranoside
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
P04066
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
induces acrosome reaction of guinea pig spermatozoa
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
responsible for the intralysosomal hydrolysis of fucose-containing glypeptide and glycolipids
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
4-methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
involved in sperm-egg interactions
-
-
?
4-methylumbelliferyl-alpha-L-fucopyranoside + H2O
methylumbelliferone + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-fucoside
?
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
show the reaction diagram
-
sodium acetate buffer 50 mM, pH 5.0, 37C
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside
?
show the reaction diagram
-
assay at pH 4.5, 37C for 3 h, reaction stopped by addition of borate buffer
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
Venus mercenaria
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
Q9WYE2
-
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
can cleave alpha-(1-2)-, alpha-(1-3)- and alpha-(1-4)- fucosyl linkages
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
can cleave alpha-(1-2)-, alpha-(1-3)- and alpha-(1-4)- fucosyl linkages
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
can cleave alpha-(1-2)-, alpha-(1-3)- and alpha-(1-4)- fucosyl linkages
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
show the reaction diagram
-
-, substrate incubated with plasma sample of breast cancer patients treated with anti-cancer monoclonal antibody trastuzumbal
-
-
?
4-nitrophenyl-alpha-L-fucopyranoside + N-acetyl-D-glucosamine + H2O
4-nitrophenol + alpha-L-Fuc-(1-3)-D-GlcNAc
show the reaction diagram
-
transglycosylation activity
no other isomer
?
4-nitrophenyl-alpha-L-fucopyranoside + N-acetyl-D-glucosamine + H2O
4-nitrophenol + alpha-L-fucose-(1-3)-D-GlcNAc
show the reaction diagram
-
catalytic residues Asp242, Glu58, and Glu292
-
-
?
4-nitrophenyl-alpha-L-fucoside + H2O
4-nitrophenol + alpha-L-fucose
show the reaction diagram
-
activity measured in whole fly homogenates, substrate concentration of 6 mM in citrate buffer
-
-
?
4-nitrophenyl-alpha-L-fucoside + H2O
alpha-L-fucopyranose + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
6-O-alpha-L-fucopyranosyl-N-acetylglucosamine + H2O
alpha-L-fucopyranose + N-acetyl-glucosamine
show the reaction diagram
-
Fuc-alpha-1,6-GlcNAc-linkage most susceptible
-
?
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-3)-D-GalNAc + H2O
alpha-L-fucose + beta-D-Gal-(1-3)-D-GalNAc
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
alpha-L-Fuc-(1-2)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
show the reaction diagram
-
same yield of transglycosylation and hydrolysis products
-
?
alpha-L-Fuc-(1-3)-a-L-Fuc-O-4-NP + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-L-Fuc-(1-3)-alpha-L-Fuc-O-4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-L-Fuc-(1-3)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
show the reaction diagram
-
slower hydrolysis than for the alpha-(1-6)- or alpha-(1-2)-isomers, transglycosylation activity
-
?
alpha-L-Fuc-(1-3)-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
alpha-L-Fuc-(1-4)-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
alpha-L-Fuc-(1-6)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-6)-D-GlcNAc + D-galactose
show the reaction diagram
-
same yield of transglycosylation and hydrolysis products
-
?
alpha-L-Fuc-(1-6)-D-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
34% yield based on the donor substrate
-
?
alpha-L-fucosyl fluoride + H2O
alpha-L-fucose + fluoride
show the reaction diagram
Q9WYE2, -
-
-
-
-
alpha-L-fucosyl fluoride + H2O
alpha-L-fucose + fluoride
show the reaction diagram
-
-
-
-
?
alpha-L-fucosyl fluoride + H2O
fluoride + alpha-L-fucose
show the reaction diagram
Q9WYE2, -
-
-
-
?
antigen H disaccharide + H2O
?
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
antigen H type II trisaccharide + H2O
?
show the reaction diagram
B3W8U6, B3WB08, B3WBB5
-
-
-
?
beta-D-GlcNAc-(1-4)-(alpha-L-Fuc-(1-6))-D-GlcNAc + H2O
alpha-L-fucose + beta-D-GlcNAc-(1-4)-D-GlcNAc
show the reaction diagram
-
-
-
-
?
Fuc-alpha-(1-2)-Fuc-beta-4-nitrophenol + H2O
alpha-L-fucose + Fuc-beta-4-nitrophenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-3)-GalNAc-alpha-phenol + H2O
alpha-L-fucose + Gal-beta-(1-3)-N-acetyl-galactosaminyl-phenol
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
low activity
-
?
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
show the reaction diagram
Venus mercenaria
-
low activity
-
?
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
show the reaction diagram
-
alpha-fucosidase I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
Bacillus fulminans
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
Venus mercenaria
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
only hydrolysed by alpha-L-fucosidase II, lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-difucohexaitol I, NaBH4-reduced oligosaccharide
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
only hydrolysed by alpha-fucosidase II
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
Bacillus fulminans
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-sorbitol + H2O
alpha-L-fucose + Gal-beta-(1-4)-sorbitol
show the reaction diagram
-
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, 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
-
?
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
show the reaction diagram
-
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, 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
-
?
Fuc-alpha-(1-2)-Gal-beta-4-nitrophenol + H2O
alpha-L-fucose + beta-galactosyl-4-nitrophenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Glc + H2O
alpha-L-fucose + D-glucose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Xyl + H2O
alpha-L-fucose + D-xylose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-[Gal-alpha-(1-3)]-Gal-beta-phenol + H2O
alpha-L-fucose + Gal-alpha-(1-3)-Gal-beta-phenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
low activity, 3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
show the reaction diagram
-
low activity, 3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
show the reaction diagram
-
3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
show the reaction diagram
-
3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Glc + H2O
alpha-L-fucose + D-glucose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
slow hydrolysis rate
-
?
Fuc-alpha-(1-3)-GlcNAc-beta-O(CH2)6NHCOCF3 + H2O
alpha-L-fucose + GlcNAc-beta-O(CH2)6NHCOCF3
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-GlcNAc-beta-phenol + H2O
alpha-L-fucose + N-acetyl-glucosaminyl-beta-phenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-4)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-4)-GlcNAc-beta-phenol + H2O
alpha-L-fucose + beta-N-acetyl-glucosaminyl-phenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-4)-[Gal-beta-(1-3)]-GlcNAc-beta-phenol + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-phenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc-4-nitrophenol + H2O
alpha-L-fucose + GlcNAc-4-nitrophenol
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc-beta-Asn + H2O
alpha-L-fucose + N-acetyl-D-glucosaminyl-Asn
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-[Gal-beta-(1-3)]-GlcNAc-beta-OCH3 + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-OCH3
show the reaction diagram
-
-
-
?
fucoidan + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
fucose residues from fucose-containing oligosaccharide chains on porcine gastric mucin + H2O
?
show the reaction diagram
Streptomyces sp., Streptomyces sp. OH11242
-
fase I, not: fase II
-
-
?
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
show the reaction diagram
-
low activity for alpha-L-fucosidase II
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose III
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose III
-
?
Gal-beta-(1-4)[Fuc-alpha-(1-3)]-Glc + H2O
Gal-beta-(1-4)-Glc + alpha-L-fucose
show the reaction diagram
-
NaBH4-reduced oligosaccharide, very slow hydrolysis, very slow hydrolysis, NaBH4-reduced oligosaccharide
-
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
show the reaction diagram
-
-
-
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
show the reaction diagram
-
low activity
-
?
gastric mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
porcine
-
?
gastric mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
porcine
-
?
gastric mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
porcine
-
?
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
show the reaction diagram
-
not completely hydrolysed due to steric hinderance by beta-(1-2)-GlcNAc residues
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
not active on native glycoproteins
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
from meconium H-1, H-2 and X-1, desialyzed porcine submaxillry mucin
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
cellular source of substrate
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
desialyzed porcine submaxillary mucin, meconium H-1, H-2 and X-1
-
?
glycoprotein + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
specifically hydrolyses terminal alpha-(1-2)-fucosidic bonds of glycoproteins, glycopeptides and oligosaccharides
-
?
glycoprotein + H2O
alpha-L-fucose + ?
show the reaction diagram
Venus mercenaria
-
salivary human type H
-
?
glycosphingolipid + H2O
alpha-L-fucose + ?
show the reaction diagram
Venus mercenaria
-
blood-group active types B and H
-
?
gp120 oligosaccharides + H2O
alpha-L-fucose + ?
show the reaction diagram
-
released from recombinant CHO cell-produced gp120, glycoproteins containing fucose in alpha-1,3- and alpha-1,6-linkages are no substrates
-
?
IgG Fc peptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
from human, rabbit, horse, human, rabbit, horse
-
?
IgG L peptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
lacto-N-difucohexaitol I + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity
-
?
lacto-N-difucohexaose I + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity for alpha-L-fucosidase II
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
Venus mercenaria
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
low activity
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
alpha-fucosidase II
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
alpha-fucosidase II
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
preferentially hydrolysed by alpha-fucosidase II
-
?
lactoferrin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity
-
?
LH-beta peptic glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
m-nitrophenyl alpha-L-fucopyranoside + H2O
m-nitrophenol + L-fucose
show the reaction diagram
-
pH 6.8, 37C
-
-
?
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
show the reaction diagram
-
-
-
?
meconium H-1 + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
meconium H-2 + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
meconium X-1 + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
low activity
-
?
methyl alpha-L-fucopyranoside + H2O
methanol + alpha-L-fucose
show the reaction diagram
-
or methanol or ethanol as acceptor
-
-
?
oligosaccharide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
-
?
oligosaccharide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
-
-
?
oligosaccharides + H2O
alpha-L-fucose + ?
show the reaction diagram
-
di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
-
?
oligosaccharides + H2O
alpha-L-fucose + ?
show the reaction diagram
-
di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
-
-
?
orosomucoid + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity, higher activity if desialyzed
-
?
p-cyanophenyl alpha-L-fucopyranoside + H2O
p-cyanophenol + L-fucose
show the reaction diagram
-
pH 6.8, 37C
-
-
?
p-nitrophenyl alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucopyranose
show the reaction diagram
-
-
anomeric configuration of the produced fucopyranse
-
?
p-nitrophenyl alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucopyranose
show the reaction diagram
-
or methanol or ethanol as acceptor
-
-
?
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
25% yield based on the donor substrate
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
-
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
Q9WYE2, -
-
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
fase II, not: fase I
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
fase II, not: fase I
-
-
?
p-nitrophenyl alpha-L-fucoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
Streptomyces sp. OH11242
-
fase II, not: fase I
-
-
?
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucose
show the reaction diagram
P04066
-
-
-
?
p-nitrophenyl-alpha-L-fucoside + H2O
L-fucose + p-nitrophenol
show the reaction diagram
Q9WYE2
the enzyme has low transglycosylation properties
-
-
?
phenyl alpha-L-fucopyranoside + H2O
phenol + L-fucose
show the reaction diagram
-
pH 6.8, 37C
-
-
?
saliva + H2O
alpha-L-fucose + ?
show the reaction diagram
-
human
-
?
saliva + H2O
alpha-L-fucose + ?
show the reaction diagram
-
Ulex europaeus
-
?
stomach + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
submaxilary mucin trisaccharide + H2O
alpha-L-fucose + disaccharide
show the reaction diagram
-
-
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
desialyzed and not, desialyzed mucine best substrate tested
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
one form, optimally active at pH 5, not able to hydrolyse p-nitrophenyl-alpha-L-fucopyranoside
-
-
-
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
A-minus type and desialyzed, porcine
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
A-minus type and desialyzed, porcine
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
A-minus type and desialyzed, porcine
-
-
-
submaxillary porcine trisaccharide + H2O
alpha-L-fucose + disaccharide
show the reaction diagram
-
-
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
Venus mercenaria
-
bovine, from bovine
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
hydrolysis only after pronase or neuraminidase treatment
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
[Man-beta-(1-6)-Man-alpha-(1-3)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAcOT-[Fuc-alpha-(1-6)] + H2O
[Man-beta-(1-6)-Man-alpha-(1-3)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAcOT + alpha-L-fucose
show the reaction diagram
-
-, subscript OT is used to indicate NaBH4-reduced oligosaccharide
-
?
milk + H2O
alpha-L-fucose + ?
show the reaction diagram
-
human
-
?
additional information
?
-
-
the enzyme is able to catalyse the hydrolysis of fucosyl units of Ascophyllum nodosum fucoidan
-
-
-
additional information
?
-
-
not: p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-fucopyranoside, p-nitrophenyl N-acetyl-beta-D-glucosaminide, p-nitrophenyl alpha-mannopyranoside
-
-
-
additional information
?
-
-
not: p-nitrophenyl-alpha-L-fucoside
-
-
-
additional information
?
-
-
Two specific mutations, designed on the basis of the programmed -1 frameshifting mechanism, promotes transfucosylation reactions by following a retaining reaction mechanism.
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
all eukaryotic alpha-L-fucosidases contain a catalytic N-terminal domain with a (beta/alpha)8-TIM barrel structure and a C-terminal domain
-
-
-
additional information
?
-
-
behaviour of the catalytic residues is different from that of Sulfolobus solfataricus alpha-fuc
-
-
-
additional information
?
-
Q9WYE2
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%)
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
B3W8U6, B3WB08, B3WBB5
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
-
-
-
additional information
?
-
Bacteroides thetaiotaomicron Bt2970
-
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
-
-
-
additional information
?
-
-
not: p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-fucopyranoside, p-nitrophenyl N-acetyl-beta-D-glucosaminide, p-nitrophenyl alpha-mannopyranoside
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
-
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
low activity
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
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
-
?
2'-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
alpha-fucosidase II highly active
-
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
very low activity
-
?
3-fucosyllactitol + H2O
alpha-L-fucose + lactitol
show the reaction diagram
-
low activity
-
?
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
show the reaction diagram
-
-
-
-
?
6-O-alpha-L-fucopyranosyl-N-acetylglucosamine + H2O
alpha-L-fucopyranose + N-acetyl-glucosamine
show the reaction diagram
-
Fuc-alpha-1,6-GlcNAc-linkage most susceptible
-
?
alpha-L-Fuc-(1-2)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
show the reaction diagram
-
same yield of transglycosylation and hydrolysis products
-
?
alpha-L-Fuc-(1-3)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-3)-D-GlcNAc + D-galactose
show the reaction diagram
-
slower hydrolysis than for the alpha-(1-6)- or alpha-(1-2)-isomers, transglycosylation activity
-
?
alpha-L-Fuc-(1-6)-D-Gal + N-acetyl-D-glucosamine
alpha-L-Fuc-(1-6)-D-GlcNAc + D-galactose
show the reaction diagram
-
same yield of transglycosylation and hydrolysis products
-
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
low activity
-
?
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
show the reaction diagram
Venus mercenaria
-
low activity
-
?
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
show the reaction diagram
-
alpha-fucosidase I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
Bacillus fulminans
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
Venus mercenaria
-
lacto-N-fucopentaose I
-
?
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
show the reaction diagram
-
only hydrolysed by alpha-L-fucosidase II, lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol I, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-difucohexaitol I, NaBH4-reduced oligosaccharide
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
only hydrolysed by alpha-fucosidase II
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
Bacillus fulminans
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc + H2O
alpha-L-fucose + lactose
show the reaction diagram
-
2'-fucosyllactose
-
?
Fuc-alpha-(1-2)-Gal-beta-(1-4)-sorbitol + H2O
alpha-L-fucose + Gal-beta-(1-4)-sorbitol
show the reaction diagram
-
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
-
?
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
show the reaction diagram
-
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
-
?
Fuc-alpha-(1-2)-Glc + H2O
alpha-L-fucose + D-glucose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-2)-Xyl + H2O
alpha-L-fucose + D-xylose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
show the reaction diagram
-
low activity, 3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
show the reaction diagram
-
3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Gal-beta-(1-4)-Glc + H2O
alpha-D-fucose + lactose
show the reaction diagram
-
3-fucosyllactose
-
?
Fuc-alpha-(1-3)-Glc + H2O
alpha-L-fucose + D-glucose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-3)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
slow hydrolysis rate
-
?
Fuc-alpha-(1-4)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-Gal + H2O
alpha-L-fucose + D-galactose
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc + H2O
alpha-L-fucose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Fuc-alpha-(1-6)-GlcNAc-beta-Asn + H2O
alpha-L-fucose + N-acetyl-D-glucosaminyl-Asn
show the reaction diagram
-
-
-
?
fucoidan + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
low activity for alpha-L-fucosidase II
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaitol II, NaBH4-reduced oligosaccharide
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose III
-
?
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
show the reaction diagram
-
lacto-N-fucopentaose III
-
?
Gal-beta-(1-4)[Fuc-alpha-(1-3)]-Glc + H2O
Gal-beta-(1-4)-Glc + alpha-L-fucose
show the reaction diagram
-
very slow hydrolysis, NaBH4-reduced oligosaccharide
-
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
show the reaction diagram
-
-
-
?
GalNAc-alpha-(1-3)-Gal-[Fuc-alpha-(1-2)] + H2O
alpha-L-fucose + GalNAc-alpha-(1-3)-Gal
show the reaction diagram
-
low activity
-
?
gastric mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
porcine
-
?
gastric mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
porcine
-
?
gastric mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
porcine
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
not active on native glycoproteins
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
cellular source of substrate
-
?
glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
desialyzed porcine submaxillary mucin, meconium H-1, H-2 and X-1
-
?
glycoprotein + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
specifically hydrolyses terminal alpha-(1-2)-fucosidic bonds of glycoproteins, glycopeptides and oligosaccharides
-
?
glycoprotein + H2O
alpha-L-fucose + ?
show the reaction diagram
Venus mercenaria
-
salivary human type H
-
?
glycosphingolipid + H2O
alpha-L-fucose + ?
show the reaction diagram
Venus mercenaria
-
blood-group active types B and H
-
?
gp120 oligosaccharides + H2O
alpha-L-fucose + ?
show the reaction diagram
-
released from recombinant CHO cell-produced gp120, glycoproteins containing fucose in alpha-1,3- and alpha-1,6-linkages are no substrates
-
?
IgG Fc peptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
human, rabbit, horse
-
?
IgG L peptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
lacto-N-difucohexaitol I + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity
-
?
lacto-N-difucohexaose I + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
lacto-N-fucopentaitol III + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity for alpha-L-fucosidase II
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
Venus mercenaria
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
-
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
low activity
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
alpha-fucosidase II
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
alpha-fucosidase II
-
?
lacto-N-fucopentaose II + H2O
alpha-L-fucose + Gal-beta-(1-3)-GlcNAc-beta-(1-3)-Gal-beta-(1-4)-Glc
show the reaction diagram
-
preferentially hydrolysed by alpha-fucosidase II
-
?
lactoferrin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity
-
?
LH-beta peptic glycopeptide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
meconium H-1 + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
meconium H-2 + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
-
-
?
meconium X-1 + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
low activity
-
?
oligosaccharide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
-
?
oligosaccharide + H2O
alpha-L-fucose + ?
show the reaction diagram
-
di-, tri- and pentasaacharides having alpha-1-2, alpha-1-3, and alpha-1-4 bonds
-
-
?
orosomucoid + H2O
alpha-L-fucose + ?
show the reaction diagram
-
low activity, higher activity if desialyzed
-
?
saliva + H2O
alpha-L-fucose + ?
show the reaction diagram
-
human
-
?
saliva + H2O
alpha-L-fucose + ?
show the reaction diagram
-
Ulex europaeus
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
Bacillus fulminans
-
desialyzed and not, desialyzed mucine best substrate tested
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
one form, optimally active at pH 5, not able to hydrolyse p-nitrophenyl-alpha-L-fucopyranoside
-
-
-
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
A-minus type and desialyzed, porcine
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
A-minus type and desialyzed, porcine
-
?
submaxillary mucin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
A-minus type and desialyzed, porcine
-
-
-
submaxillary porcine trisaccharide + H2O
alpha-L-fucose + disaccharide
show the reaction diagram
-
-
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
-
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
Venus mercenaria
-
bovine
-
?
thyroglobulin + H2O
alpha-L-fucose + ?
show the reaction diagram
-
hydrolysis only after pronase or neuraminidase treatment
-
?
[Man-beta-(1-6)-Man-alpha-(1-3)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAcOT-[Fuc-alpha-(1-6)] + H2O
[Man-beta-(1-6)-Man-alpha-(1-3)]-Man-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAcOT + alpha-L-fucose
show the reaction diagram
-
-
-
?
milk + H2O
alpha-L-fucose + ?
show the reaction diagram
-
human
-
?
additional information
?
-
-
the enzyme is able to catalyse the hydrolysis of fucosyl units of Ascophyllum nodosum fucoidan
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
-
5 mM, complete inhibition
Ca2+
-
alpha-fucosidase II, 21% activation at 10 mM
Ca2+
-
10% activation at 10 mM
Cd2+
-
5 mM, about 5% inhibition
Co2+
-
5 mM, about 5% inhibition
Cu2+
-
5 mM, about 5% inhibition
Fe2+
-
12% activation at 2 mM
Fe2+
-
5 mM, 76% inhibition
Zn2+
-
10% activation at 10 mM
Zn2+
-
150% activity at 1 mM
Zn2+
-
5 mM, 10% inhibition
Mn2+
-
22% stimulation at 5 mM
additional information
-
the addition of calcium, magnesium, cobalt, manganese, nickel, and zinc at 10 mM concentrations does not increase enzymatic rates
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
-
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
-
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
-
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
(2S,3R,4R,5R)-5-(3-aminopropoxy)-2-methylpiperidine-3,4-diol
-
-
(2S,3R,4R,5R,6S)-2-(hydroxymethyl)-6-methylpiperidine-3,4,5-triol
-
-
(2S,3R,4S,5R)-1-(3-aminopropyl)-2-methylpiperidine-3,4,5-triol
-
-
(2S,3R,4S,5R)-2-(propan-2-yl)piperidine-3,4,5-triol
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
(2S,3R,4S,5R)-2-benzylpiperidine-3,4,5-triol
-
-
(2S,3R,4S,5R)-2-benzylpiperidine-3,4,5-triol
-
fuconojirimycin derivative, time dependent, slow-binding inhibition
(2S,3R,4S,5R)-2-isopropylpiperidine-3,4,5-triol
-
-
(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-[2-(1,1'-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
1-deoxyfuconojirimycin
-
-
1-deoxygalactonojirimycin
-
-
1-deoxymannojirimycin
-
-
1-deoxynojirimycin
-
-
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-methyltetrahydro-2H-pyran-3,4-diol
-
uncompetitive inhibition, Ki: 23 mM
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-aminophenyl 1-thio alpha-L-fucoside
-
weak competitive inhibition, Ki: 1.25 mM
4-chloromercuribenzoate
-
71% inhibition at 1 mM
4-chloromercuribenzoate
-
50% inhibition at 0.0015 mM, totally reversal by addition of 4 mM DTT
4-chloromercuribenzoate
-
92% inhibition at 0.1 mM
4-chloromercuriphenylsulfonic acid
-
complete inhibition at 0.002 mM
4-chloromercuriphenylsulfonic acid
-
slight inhibition at 1 mM
4-hydroxy-2-methyltetrahydro-2H-pyran-3-yl acetate
-
competitive inhibition, Ki: 0.09 mM
-
4-mercuribenzoate
-
complete inhibition at 0.25 mM
5-(hydroxymethyl)pyrrolidine-2,3,4-triol
-
competitive inhibition, Ki: 0.91 mM
5-amino-5-deoxy-L-fucose
-
-
5-fluoro-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)-1H-indole-2-carboxamide
-
-
6-N-acetylamino-deoxymannojirimycin
-
-
Ag+
-
complete inactivation at 0.1 mM, complete reversal by addition of 1.1 mM DTT
Ag+
-
59% inhibition at 3 mM
Ag+
-
effective inhibition at 5 mM
Ag2+
-
complete inactivation at 1 mM
alpha-L-fuco-N-benzyl aminocyclopentitol
-
-
alpha-L-fucose
-
competitive inhibition, Ki: 0.065 mM
alpha-L-fucose
-
competitive inhibition, Ki: 0.3 mM
alpha-L-fucose
-
90% competitive inhibition at 5 mM, Ki: 0.12 mM
alpha-L-fucose
-
85% inhibition at 2.5 mM
alpha-L-fucose
-
competitive inhibition, Ki: 0.13 mM
alpha-L-fucose
-
competitive inhibition at 50 mM
alpha-L-fucose
-
competitive inhibition, Ki: 0.275 mM
alpha-L-fucose
-
competitive inhibition, Ki: 0.285 mM
alpha-L-fucose
-
competitive inhibition, Ki: 1.6 mM
alpha-L-fucose
-
competitive inhibition at 50 mM
alpha-L-fucose
-
competivite inhibition of p-nitrophenyl alpha-L-fucopyranoside hydrolysis
Ca2+
-
alpha-fucosidase I, slight inhibition at 10 mM
Cd2+
-
effective inhibition at 5 mM
Cu2+
-
complete inactivation at 1 mM
Cu2+
-
88% inhibition at 2 mM
Cu2+
-
effective inhibition at 5 mM
D-1-deoxymannojirimycin
-
competitive inhibition, Ki: 0.03 mM
D-1-deoxyrhamnojirimycin
-
competitive inhibition, Ki: 0.011 mM
D-1-deoxytalonojirimycin
-
competitive inhibition, Ki: 0.053 mM
D-arabinose
-
95% inhibition at 2.5 mM
D-arabinose
-
competitive inhibition, Ki: 50 mM
D-fucal
-
uncompetitive inhibition, Ki: 35 mM
D-fucose
-
15% inhibition at 50 mM
D-Galactono-1,4-lactone
-
15% inhibition at 50 mM
D-galactose
-
competitive inhibition, Ki: 1.7 mM
D-galactose
-
15% inhibition at 50 mM
D-glucono-1,5-lactone
-
30% inhibition at 50 mM
D-glucose
-
15% inhibition at 50 mM
D-glucose
-
21% inhibition at 6 mM
deoxycholate
Bacillus fulminans
-
34% inhibition at 0.2%, w/v
deoxycholate
-
36% inhibition at 0.012%, w/v
deoxyfuconojirimycin
-
competitive inhibition, Ki: 0.000024 mM
deoxyfuconojirimycin
-
inhibits by 94-100% at 1 mM
ethanolamine
-
strong inhibition
ethylenediaminetetraacetic acid
Bacillus fulminans
-
68% inhibition at 0.1 mM
Fe3+
-
40% inhibition at 2 mM
-
formaldehyde
-
57% inhibition at 160 mM
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
fucosylamine
-
competitive inhibition, Ki: 0.014 mM
Hg2+
Bacillus fulminans
-
marked inhibition at 0.1 mM
Hg2+
-
potent inhibitor at 1 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
marked inhibition at 20 mM
Hg2+
-
effective non-competitive inhibition at 2 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
effective non-competitive inhibition at 2 mM
Hg2+
-
complete inactivation at 0.1 mM, complete reversal by addition of 1.1 mM DTT
Hg2+
-
92% inhibition at 0.1 mM
Hg2+
-
effective inhibition at 5 mM
iodoacetamide
-
30% inhibition at 1 mM
L-1-deoxyfuconojirimycin
-
competitive inhibition, Ki: 0.00003 mM
-
L-1-deoxymannojirimycin
-
competitive inhibition, Ki: 90 mM
-
L-1-deoxyrhamnojirimycin
-
competitive inhibition, Ki: 1 mM
-
L-cysteine
-
alpha-fucosidase I, slight inhibition at 10 mM
L-cysteine
-
20% inhibition at 30 mM
L-fucal
-
competitive inhibition, best inhibitor of glycal compounds tested, Ki: 0.05 mM
-
L-fuco-nojirimycin
-
very potent, competitive inhibitor
L-fucosamine
-
-
L-galactono-1,4-lactone
-
30% inhibition at 50 mM
L-rhamnose
-
competitive inhibition, Ki: 140 mM
Mg2+
-
slight inhibition at 10 mM
Mn2+
Bacillus fulminans
-
slight inhibition at 0.1 mM
N-ethylmaleimide
-
30% inhibition at 1 mM
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
-
-
Ni2+
-
effective inhibition at 5 mM
p-nitrophenyl alpha-L-fucoside
-
; substrate inhibition at high concentration
Pb2+
-
effective inhibition at 5 mM
Phenol
-
noncompetitive inhibition, Ki: 112 mM
SDS
Bacillus fulminans
-
42% inhibition at 0.02%, w/v
Sn2+
-
24% inhibition at 2 mM
Zn-acetate
-
more than 90% inhibition at 5 mM
Mn2+
-
26% inhibition at 2 mM
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
azide
-
increases the rate of substrate cleavage in depending of azide concentration
Bovine serum albumin
-
increases acitivity up to 100%
-
Bovine serum albumin
-
increases acitivity up to 100%
-
chemokine CCL1
-
1.8-fold increase of ALP-expression after 24-h stimulation
-
chemokine CCL5
-
2.2-fold increase of ALP-expression after 24-h stimulation
-
CN-
-
30% activation at 10 mM
dithiothreitol
-
13% activation at 0.2 mM
ethylenediaminetetraacetic acid
-
5% activation at 10 mM
formate
-
increases the rate of substrate cleavage in depending of azide concentration
KCl
-
17% activation at 300 mM
NaCl
-
small positive effect
Sodium azide
-
1M, enhanced enzyme activity, only in mutants
methanol
-
linear increase in enzyme-catalyzed cleavage of p-nitrophenyl alpha-L-fucoside and fucosyl fluoride
additional information
-
the enzyme activity is increases with the ionic strength from 10 mM to 200 mM
-
additional information
-
cell-bound enzyme activity increases sharply following permeabilization of intact sperm
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.67
-
2'-fucosyllactitol
-
alpha-fucosidase II
-
1.18
-
2'-fucosyllactitol
-
-
-
0.63
-
2'-fucosyllactose
-
-
1.79
-
2'-fucosyllactose
-
at pH 5.0
2.5
-
2'-fucosyllactose
Bacillus fulminans
-
-
10.6
-
2'-fucosyllactose
-
at pH 7.0
0.063
-
2-chloro-4-nitrophenyl alpha-L-fucopyranoside
-
mutant E289G
2.1
-
2-deoxy-2-fluoro-alpha-L-fucosyl fluoride
-
pH 5.0, 60C
0.27
-
2-nitrophenyl alpha-L-fucopyranoside
B3W8U6, B3WB08, B3WBB5
pH 7.0, 37C
2.9
-
2-nitrophenyl alpha-L-fucopyranoside
B3W8U6, B3WB08, B3WBB5
pH 7.0, 37C
5.2
-
2-nitrophenyl alpha-L-fucopyranoside
B3W8U6, B3WB08, B3WBB5
pH 7.0, 37C
1.25
-
3'-fucosyllactose
-
-
1.9
-
3'-fucosyllactose
-
at pH 5.0
0.06
-
4-methylumbelliferyl alpha-L-fucopyranoside
-
pH 5.0, 37C, undifferentiated HT-29 cells
0.06
-
4-methylumbelliferyl alpha-L-fucopyranoside
-
pH 7.0, 37C
0.07
-
4-methylumbelliferyl alpha-L-fucopyranoside
-
pH 5.0, 37C, differentiated HT-29 cells
0.08
-
4-methylumbelliferyl alpha-L-fucopyranoside
-
pH 7.0, 37C
0.022
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.031
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
at pH 7.0
0.05
0.06
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.05
0.06
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.05
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.07
0.08
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.07
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.072
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
at pH 5.0
0.08
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.083
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.12
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.125
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
alpha-fucosidase I
0.125
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.14
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.14
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
4-5fold increase in fucosidosis patients
0.22
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.3
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.4
-
4-methylumbelliferyl-alpha-L-fucopyranoside
-
-
0.00325
-
4-methylumbelliferyl-beta-fucoside
-
control semen
0.01825
-
4-methylumbelliferyl-beta-fucoside
-
infected semen
0.02
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, wild-type enzyme
0.028
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, wild-type enzyme
0.028
-
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 6.3, in the presence of sodium phosphate; wild-type enzyme
0.033
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme D146G
0.033
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant D146G; mutant enzyme D146G
0.056
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme E292G
0.06
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme T264A/Y267F/L322P; 70C, mutant enzyme M210V/Y237H/T264A
0.06
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E292G, at pH 6.3, in the presence of sodium phosphate; mutant enzyme E292G
0.065
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme T264A
0.07
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.07
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme T264A
0.079
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, wild-type enzyme
0.08
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme G226S/Y237H/T264A/L322P
0.088
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme D124G
0.09
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme G226S/T264A/Y267F/L322P; 40C, mutant enzyme M210V/Y237H/T264A/Y267F; 40C, mutant enzyme P196L/Y237H/Y267F
0.09
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant D124G; mutant E292G, at pH 4.6, in the presence of sodium acetate; mutant enzyme D124G
0.1
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme M210V/Y237H/T264A; 70C, mutant enzyme G226S/Y237H/T264A/L322P4; 70C, mutant enzyme P196L/Y237H/Y267F
0.13
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme R147G/L322P
0.14
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.14
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P; 70C, mutant enzyme M210V/Y237H/T264A/Y267F
0.168
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.18
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.19
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.19
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme T264A/L322P
0.21
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.22
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.22
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.23
-
4-nitrophenyl-alpha-L-fucopyranoside
-
isoform F2
0.23
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme Y237H/Y267F/L322P
0.242
-
4-nitrophenyl-alpha-L-fucopyranoside
-
isoform F1
0.25
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P; 70C, mutant enzyme T264A/L322P
0.26
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.26
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65C, wild-type enzyme
0.26
-
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 5.0, in the presence of sodium citrate
0.277
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.28
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme R147G/L322P
0.29
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme Y237H/Y267F/L322P
0.3
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.3
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.3
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme G226S/T264A/Y267F/L322P
0.31
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme T264A/Y267F/L322P
0.358
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.38
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.43
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.45
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.48
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.6
-
4-nitrophenyl-alpha-L-fucopyranoside
Venus mercenaria
-
-
0.6
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium acetate
0.71
-
4-nitrophenyl-alpha-L-fucopyranoside
-
sperm-bound enzyme
0.87
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
0.91
-
4-nitrophenyl-alpha-L-fucopyranoside
-
gonad fluid enzyme
1.1
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant E58G, at pH 4.6, in the presence of sodium formate
1.2
-
4-nitrophenyl-alpha-L-fucopyranoside
-
-
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, 65C, mutant enzyme H46G
17
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme H46G
17
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant enzyme H46G; mutant H46G
0.0287
-
4-nitrophenyl-alpha-L-fucoside
-
wild-type and mutant fucA1B
3
-
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-3)-D-GalNAc
-
pH 6.5, 37C
7
-
alpha-L-Fuc-(1-2)-beta-D-Gal-(1-4)-beta-D-GlcNAc-1-Me
-
pH 6.5, 37C
0.075
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C, mutant E266A
0.15
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C, wild-type enzyme
0.23
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C
2.5
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C, mutant E66A
9
-
beta-D-GlcNAc-(1-4)-(alpha-L-Fuc-(1-6))-D-GlcNAc
-
pH 6.5, 37C
2.9
-
Fuc-alpha-(1-2)-Gal
-
-
1.56
-
Fuc-alpha-(1-2)-Gal-beta-(1-4)-Glc
-
-
0.52
-
Fuc-alpha-(1-2)-Gal-beta-4-nitrophenol
-
-
1.63
-
Fuc-alpha-(1-3)-GlcNAc-phenol
-
-
2.01
-
Fuc-alpha-(1-4)-GlcNAc-beta-phenol
-
-
1.75
-
Fuc-alpha-(1-6)-GlcNAc
-
at pH 5.0
0.88
-
gastric mucin
-
-
-
1.6
-
glycopeptide from desialyzed porcine submaxillary mucin
Bacillus fulminans
-
-
-
1.02
-
gp120 oligosaccharide
-
at pH 5.0
-
0.1
-
lacto-N-fucopentaitol II
-
alpha-fucosidase I
0.095
-
lacto-N-fucopentaitol III
-
alpha-fucosidase I
2
-
lacto-N-fucopentaose
Bacillus fulminans
-
-
-
16
-
methyl alpha-L-fucopyranoside
-
pH 6.5, 37C
0.11
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E289Q, 50 mM sodium phosphate buffer, pH 6.8, 37C, loss of catalytic activity
0.12
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E289G, 50 mM sodium phosphate buffer, pH 6.8, 37C, loss of catalytic activity
0.2
-
p-nitrophenyl alpha-L-fucopyranoside
-
pH 6.5, 37C
0.27
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D258G, 50 mM sodium phosphate buffer, pH 6.8, 37C
0.28
-
p-nitrophenyl alpha-L-fucopyranoside
-
50 mM sodium phosphate buffer, pH 6.8, 37C; mutant D158G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant D276G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant E135G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant E275G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant E70G, 50 mM sodium phosphate buffer, pH 6.8, 37C
0.3
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E79G, 50 mM sodium phosphate buffer, pH 6.8, 37C
0.65
-
p-nitrophenyl alpha-L-fucopyranoside
-
pH 4, 60C
1.04
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D225G, 50 mM sodium phosphate buffer, pH 6.8, 37C, loss of catalytic activity
1.06
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D225N, 50 mM sodium phosphate buffer, pH 6.8, 37C
0.028
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.3, 65C
0.032
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 60C
0.034
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 37C
0.05
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 37C, wild-type enzyme
0.25
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.8, 25C
0.33
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.8, 25C, epididymis
0.75
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.8, 25C, kidney
0.75
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.8, 25C
2.1
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 37C, mutant E66A
0.02
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
wild-type, at 40C
0.06
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A, at 70C. Mutant T264A/Y267F/L322P, at 40C
0.065
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A, at 40C
0.07
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A, at 70C
0.079
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
wild-type, at 70C
0.08
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/Y237H/T264A/L322P, at 40C
0.09
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/T264A/Y267F/L322P, at 40C; mutant M210V/Y237H/T264A/Y267F, at 40C; mutant P196L/Y237H/Y267F, at 40C
0.1
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant P196L/Y237H/Y267F and mutant G226S/Y237H/T264A/L322P, at 70C. Mutant M210V/Y237H/T264A, at 40C
0.13
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant R147G/L322P, at 40C
0.14
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A/Y267F, at 70C; mutant M210V/Y237H/T264A/Y267F/L322P, at 40C
0.19
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/L322P, at 40C
0.23
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant Y237H/Y267F/L322P, at 70C
0.25
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/L322P7 and mutant M210V/Y237H/T264A/Y267F/L322P, at 70C
0.28
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant R147G/L322P, at 70C
0.29
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant Y237H/Y267F/L322P, at 40C
0.3
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/T264A/Y267F/L322P, at 70C
0.31
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/Y267F/L322P, at 70C
0.33
-
porcine submaxillary mucine, desialyzed
Bacillus fulminans
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.047
-
2-deoxy-2-fluoro-alpha-L-fucosyl fluoride
-
pH 5.0, 60C
0.24
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant D242G; mutant enzyme D242G
0.48
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme G226S/T264A/Y267F/L322P
0.5
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme T264A/Y267F/L322P
0.73
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, 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; mutant enzyme E292G
1.96
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme E292G
2.7
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme G226S/Y237H/T264A/L322P
3.6
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme T264A/L322P
4.3
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme M210V/Y237H/T264A/Y267F
5.1
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, wild-type enzyme
6.4
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme G226S/T264A/Y267F/L322P
8.2
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, 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
Q9WYE2
40C, mutant enzyme Y237H/Y267F/L322P
15
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme P196L/Y237H/Y267F; 40C, mutant enzyme R147G/L322P; 40C, mutant enzyme T264A
20
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
40C, mutant enzyme M210V/Y237H/T264A; 70C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P
35
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, wild-type enzyme
39
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme G226S/Y237H/T264A/L322P4
50
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme T264A/L322P
56
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme M210V/Y237H/T264A/Y267F
65
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme M210V/Y237H/T264A
96
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, 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
Q9WYE2
70C, mutant enzyme P196L/Y237H/Y267F
169
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme T264A
198
-
4-nitrophenyl-alpha-L-fucopyranoside
Q9WYE2
70C, mutant enzyme R147G/L322P
224
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme D146G
224
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant D146G; mutant enzyme D146G
240
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme D124G
240
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant D124G; mutant enzyme D124G
287
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, wild-type enzyme
287
-
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 6.3, in the presence of sodium phosphate; wild-type enzyme
419
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH 6.3, 65C, mutant enzyme E292G; pH 6.3, 65C, mutant enzyme H46G
419
-
4-nitrophenyl-alpha-L-fucopyranoside
-
mutant enzyme H46G; mutant H46G
430
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65C, wild-type enzyme
430
-
4-nitrophenyl-alpha-L-fucopyranoside
-
wild-type, at pH 5.0
495
-
4-nitrophenyl-alpha-L-fucopyranoside
-
pH5.0, 65C, 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
137
-
4-nitrophenyl-alpha-L-fucoside
-
mutant fucA1B
287
-
4-nitrophenyl-alpha-L-fucoside
-
wild-type
0.13
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C, mutant E266A
1.4
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C, mutant E66A
2.9
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C
7.6
-
alpha-L-fucosyl fluoride
-
pH 5.0, 25C, wild-type enzyme
0.003
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D225G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant D225N, 50 mM sodium phosphate buffer, pH 6.8, 37C
0.039
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E289Q, 50 mM sodium phosphate buffer, pH 6.8, 37C
0.048
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E289G, 50 mM sodium phosphate buffer, pH 6.8, 37C
12.5
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D258G, 50 mM sodium phosphate buffer, pH 6.8, 37C
16
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E135G, 50 mM sodium phosphate buffer, pH 6.8, 37C
16.3
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant E79G, 50 mM sodium phosphate buffer, pH 6.8, 37C
16.7
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D276G, 50 mM sodium phosphate buffer, pH 6.8, 37C
16.9
-
p-nitrophenyl alpha-L-fucopyranoside
-
mutant D158G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant E275G, 50 mM sodium phosphate buffer, pH 6.8, 37C; mutant E70G, 50 mM sodium phosphate buffer, pH 6.8, 37C
17.1
-
p-nitrophenyl alpha-L-fucopyranoside
-
50 mM sodium phosphate buffer, pH 6.8, 37C
0.24
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.5, 65C, D242G mutant
1.3
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 37C, mutant E66A
5.4
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 37C
9.1
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 60C
14.3
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 37C, wild-type enzyme
245
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.5, 65C, wild-type enzyme
287
-
p-nitrophenyl alpha-L-fucoside
-
pH 6.3, 65C
0.48
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/T264A/Y267F/L322P, at 40C
0.5
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/Y267F/L322P, at 40C
0.73
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A/Y267F/L322P, at 40C
2.7
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/Y237H/T264A/L322P, at 40C
3.6
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/L322P, at 40C
4.3
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A/Y267F, at 40C
5.1
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
wild-type, at 40C
6.4
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/T264A/Y267F/L322P, at 70C
8.2
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/Y267F/L322P, at 70C
14.8
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant Y237H/Y267F/L322P, at 40C
15
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant R147G/L322P, mutant P196L/Y237H/Y267F and mutant T264A, at 40C
20
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A, at 40C; mutant M210V/Y237H/T264A/Y267F/L322P, at 70C
35
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
wild-type, at 70C
39
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant G226S/Y237H/T264A/L322P, at 70C
50
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A/L322P7, at 70C
56
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A/Y267F, at 70C
65
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant M210V/Y237H/T264A, at 70C
96
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant Y237H/Y267F/L322P, at 70C
164
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant P196L/Y237H/Y267F, at 70C
169
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant T264A, at 70C
198
-
p-nitrophenyl-alpha-L-fucose
Q9WYE2
mutant R147G/L322P, at 70C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
12
-
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C, epididymis
14
-
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C
15
-
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C, kidney
125
-
(1R,2R,3R,4R,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C
22
-
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C
28
-
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C, kidney
58
-
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C
188
-
(1R,2R,3R,4S,5R)-4-amino-5-methylcyclopentane-1,2,3-triol
-
pH 6.8, 25C, epididymis
1.52e-05
-
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
-
1.63e-05
-
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
-
0.006
-
(2S,3R,4S,5R)-2-(propan-2-yl)piperidine-3,4,5-triol
-
-
0.005
-
(2S,3R,4S,5R)-2-benzylpiperidine-3,4,5-triol
-
-
0.000237
-
(2S,3R,4S,5S)-2-methyl-5-(phenylamino)pyrrolidine-3,4-diol
-
-
-
8e-05
-
(2S,3S,4R,5S)-2-(1H-benzimidazol-2-yl)-5-methylpyrrolidine-3,4-diol
-
-
-
4e-05
-
(2S,3S,4R,5S)-2-[2-(1,1'-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
-
-
200
-
(R)-2-aminobutanol
-
pH 6.8, 25C
400
-
(R)-2-aminobutanol
-
pH 6.8, 25C, kidney
1100
-
(R)-2-aminobutanol
-
pH 6.8, 25C
350
-
(R)-2-aminobuthanol
-
pH 6.8, 25C, epididymis
100
-
(S)-2-aminobutanol
-
pH 6.8, 25C
200
-
(S)-2-aminobutanol
-
pH 6.8, 25C, kidney
1300
-
(S)-2-aminobutanol
-
pH 6.8, 25C
125
-
(S)-2-aminobuthanol
-
pH 6.8, 25C, epididymis
2.6e-05
-
1-deoxyfuconojirimycin
-
pH 4, 60C
1
-
1-deoxygalactonojirimycin
-
pH 4, 60C
0.034
-
1-deoxymannojirimycin
-
pH 4, 60C
1
-
1-deoxynojirimycin
-
pH 4, 60C
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
1.8e-05
-
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
-
-
-
23
-
2-methyltetrahydro-2H-pyran-3,4-diol
-
uncompetitive inhibition
1.17e-05
-
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
5.6e-06
-
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
-
-
-
1.25
-
4-aminophenyl 1-thio alpha-L-fucoside
-
weak competitive inhibition
0.09
-
4-hydroxy-2-methyltetrahydro-2H-pyran-3-yl acetate
-
competitive inhibition
-
0.91
-
5-(hydroxymethyl)pyrrolidine-2,3,4-triol
-
competitive inhibition
1e-06
-
5-amino-5-deoxy-L-fucose
-
-
9.7e-06
-
5-fluoro-N-(((2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methylpiperidin-2-yl)methyl)-1H-indole-2-carboxamide
-
-
0.055
-
6-N-acetylamino-deoxymannojirimycin
-
pH 4, 60C
0.57
-
alpha-L-fuco N-benzyl aminocyclopentitol
-
pH 6.8, 25C, epididymis
28
-
alpha-L-fuco N-benzyl aminocyclopentitol
-
pH 6.8, 25C, epididymis
0.3
-
alpha-L-fuco-N-benzyl aminocyclopentitol
-
pH 6.8, 25C
0.68
-
alpha-L-fuco-N-benzyl aminocyclopentitol
-
pH 6.8, 25C, kidney
6
-
alpha-L-fuco-N-benzyl aminocyclopentitol
-
pH 6.8, 25C
18
-
alpha-L-fuco-N-benzyl aminocyclopentitol
-
pH 6.8, 25C
110
-
alpha-L-fuco-N-benzyl aminocyclopentitol
-
pH 6.8, 25C, kidney
180
-
alpha-L-fuco-N-benzyl aminocyclopentitol
-
pH 6.8, 25C
0.03
-
D-1-deoxymannojirimycin
-
competitive inhibition
0.011
-
D-1-deoxyrhamnojirimycin
-
competitive inhibition
0.053
-
D-1-deoxytalonojirimycin
-
competitive inhibition
35
-
D-fucal
-
uncompetitive inhibition
2.4e-05
-
deoxyfuconojirimycin
-
competitive inhibition
0.15
-
fucose
-
pH 6.5, 37C
0.014
-
fucosylamine
-
competitive inhibition
3e-05
-
L-1-deoxyfuconojirimycin
-
competitive inhibition
-
90
-
L-1-deoxymannojirimycin
-
competitive inhibition
-
1
-
L-1-deoxyrhamnojirimycin
-
competitive inhibition
-
0.05
-
L-fucal
-
competitive inhibition, best inhibitor of glycal compounds tested
-
1e-06
-
L-fuco-nojirimycin
-
-
0.316
-
L-fucosamine
-
pH 4, 60C
0.24
-
L-fucose
-
pH 4, 60C
140
-
L-rhamnose
-
competitive inhibition
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
-
-
0.64
-
p-nitrophenyl alpha-L-fucoside
-
pH 5.0, 60C
112
-
Phenol
-
noncompetitive inhibition
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.4e-05
-
(2R,3R,4R,5R,6S)-2-(aminomethyl)-6-methylpiperidine-3,4,5-triol
-
-
0.000267
-
(2S,3R,4R,5R)-5-(3-aminopropoxy)-2-methylpiperidine-3,4-diol
-
-
5.2e-05
-
(2S,3R,4R,5R,6S)-2-(hydroxymethyl)-6-methylpiperidine-3,4,5-triol
-
-
7e-05
-
(2S,3R,4S,5R)-1-(3-aminopropyl)-2-methylpiperidine-3,4,5-triol
-
-
0.007
-
(2S,3R,4S,5R)-2-benzylpiperidine-3,4,5-triol
-
-
0.006
-
(2S,3R,4S,5R)-2-isopropylpiperidine-3,4,5-triol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0004
-
B3W8U6, B3WB08, B3WBB5
substrate alpha-L-Fuc-(1-3)-D-GlcNAc, pH 7.0, 37C
0.0012
-
-
HT-29 cells, plasma membrane
0.002
-
-
trypomastigote extracts
0.002
-
B3W8U6, B3WB08, B3WBB5
substrate antigen H disaccharide, pH 7.0, 37C
0.003
-
-
non-differentiated HT-29 cells
0.0043
-
-
HT-29 cells, crude extract
0.0057
-
-
colonic mucosa, crude extract
0.0068
-
-
colonic mucosa, plasma membrane
0.008
-
B3W8U6, B3WB08, B3WBB5
substrate alpha-L-Fuc-(1-4)-D-GlcNAc, pH 7.0, 37C
0.009
-
-
differentiated HT-29 cells
0.01
-
-
in corpus epididymidis
0.013
-
-
in spermatozoa
0.015
-
-
in caput epididymidis
0.018
-
-
in cauda epididymidis
0.03
-
-
epimastigote extracts, comparison of fractions
0.032
-
B3W8U6, B3WB08, B3WBB5
substrate alpha-L-Fuc-(1-4)-D-GlcNAc, pH 7.0, 37C
0.033
-
B3W8U6, B3WB08, B3WBB5
substrate antigen H type II trisaccharide, pH 7.0, 37C
0.072
-
B3W8U6, B3WB08, B3WBB5
substrate 2'-fucosyllactitol, pH 7.0, 37C
0.09
-
-
at pI 5.9
0.12
-
Bacillus fulminans
-
-
0.132
-
B3W8U6, B3WB08, B3WBB5
substrate antigen H disaccharide, pH 7.0, 37C
0.19
-
-
alpha-L-fucosidase II
0.37
-
-
-
0.44
-
B3W8U6, B3WB08, B3WBB5
substrate alpha-L-Fuc-(1-6)-D-GlcNAc, pH 7.0, 37C
1.46
-
-
alpha-L-fucosidase I
1.69
-
-
at pI 6.3
1.8
-
-
alpha-L-fucosidase B
1.93
-
-
-
2.17
-
-
at pI 8.2
3.81
-
-
alpha-L-fucosidase A
4.76
-
-
-
5.69
-
-
isoform F2
5.84
-
-
-
5.89
-
-
isoform F1
7.8
-
-
-
10.66
-
-
-
12.8
-
-
-
13.62
-
B3W8U6, B3WB08, B3WBB5
substrate alpha-L-Fuc-(1-6)-D-GlcNAc, pH 7.0, 37C
14.9
17.1
-
recombinant enzyme, value depending on expression systems and buffer
15.6
-
-
-
24.2
-
-
-
27.5
-
B3W8U6, B3WB08, B3WBB5
substrate alpha-L-Fuc-(1-3)-D-GlcNAc, pH 7.0, 37C
32.1
-
-
recombinant enzyme
35
-
-
-
39.7
-
-
-
83
-
-
-
31250
-
-
-
additional information
-
-
variation of activity during differentiation
additional information
-
-
-
additional information
-
-
-
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
additional information
-
-
0.08 U/ml, incubation at 37C for 1 h, decreased migratory process of immune cells and less lectin-binding; 0.08 U/ml, incubation for 8 h; 0.5 U/ml - 0.4 U/ml, incubation for 1-24 h
additional information
-
-
5.5 micromol/min/l, progressive disease group; 5.9 micromol/min/l, nonresponders to trastuzumab; 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; 6.3 micromol/min/l, non-progressive disease group; 7.2 micromol/min/l, responders to trastuzumab; average activity 6.1 U/l
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
form S3
2.5
-
-
two pH-optima
3
-
-
one of two pH-optima
3.5
5.5
-
isoforms F1
3.9
4
-
major pH-optimum
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
6
-
isoforms F2
4.3
-
-
one of two pH-optima
4.5
-
-
assay at
4.6
-
-
one of two pH-optima
4.7
-
-
fase II, two activity maxima are found at pH 4.7 and 6.5
5
6.5
-
alpha-fucosidase II
5
-
-
gonad fluid enzyme sharper pH dependence curve than the sperm-bound enzyme
5
-
-
optimal hydrolysis rate for 2'-fucosyllactose and Fuc-alpha-(1-6)-GlcNAc
5
-
-
two pH-optima
5
-
-
alpha-fucosidase II
5
-
-
slight different pH-optima for monomeric, dimeric and tetrameric forms
5
-
-
form S1
5.1
-
-
-
5.3
5.5
-
isoform GF-2
5.3
-
-
isoform GF-1
5.3
-
-
alpha-fucosidase I
5.4
5.6
-
-
5.4
-
-
deglycosylated enzyme
5.5
5.8
-
-
5.5
6
-
fase I
5.5
-
-
in citrate buffer
5.5
-
-
-
5.5
-
-
alpha-fucosidase I
5.5
-
-
one of two pH-optima
5.5
-
Venus mercenaria
-
-
5.5
-
-
alpha-fucosidase I
5.5
-
-
for 4-nitrophenyl-alpha-L-fucopyranoside
5.7
5.9
-
-
5.7
-
-
assay at, pH-optimum estimated for
5.8
-
-
broad optimum
6
6.5
-
in potassium phosphate buffer
6
6.5
-
-
6
-
-
extremely broad optimum
6
-
-
-
6
-
-
for 4-methylumbelliferyl-alpha-L-fucopyranoside
6.1
-
-
neutral alpha-fucosidase form
6.3
-
-
second pH-optimum for native and deglycosylated enzymes
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
-
-
second pH-optimum
6.5
-
-
fase II, two activity maxima are found at pH 4.7 and 6.5
6.8
7.3
-
-
6.8
-
-
one of two pH-optima
6.9
7.1
-
-
6.9
-
-
-
6.9
-
-
second minor pH-optimum
7
-
-
fluorogenic substrate, natural substrates, isolated from dog brain, more readily digested at acidic pH
7
-
-
-
7
-
-
optimal hydrolysis rate for 4-methylumbelliferyl-alpha-L-fucopyranoside
7
-
B3W8U6, B3WB08, B3WBB5
;
7.5
-
B3W8U6, B3WB08, B3WBB5
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
5
-
low activity between
3
5
-
low activity between
3
5
-
high activity between
3
5
-
low activity between
3
5
-
appreciable activity between; low activity between
3.5
6.3
-
pH 3.5: about 55% of maximal activity, pH 6.25: 50% of maximal activity
3.7
5.5
-
less than 50% of maximal activity above and below
4.5
6
-
optimal activity within
4.8
5.2
-
recombinant enzyme
5.5
7.5
-
high activity between
6
6.5
-
enzyme in active form
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
39
-
B3W8U6, B3WB08, B3WBB5
-
41
-
B3W8U6, B3WB08, B3WBB5
;
45
-
-
-
50
-
-
optimal temperatures for hydrolysis
55
-
-
form S1
55
-
-
-
95
-
-
the activity increases sharply up to the optimal temperature of 95C, the highest temperature tested
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
comparison of temperature range depending of wild-type and mutant enzyme, the reaction catalyzed by the mutant D242G depends less on temperature
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
-
-
acidic form
6
-
-
isoelectric focusing, possible minor isoform
6
-
-
isoelectric focusing
6.2
-
-
neutral form
6.5
-
-
isoelectric focusing, isoform I
6.9
-
-
isoelectric focusing
7.1
-
-
isoelectric focusing, isoform II
additional information
-
-
isoelectric focusing indicates that the purified enzyme consists of multiple isoforms
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
activities below and above pI 7.0
Manually annotated by BRENDA team
-
gastric cancer cell. Cells infected with Helicobacter pylori secrete isoform Fuc2A
Manually annotated by BRENDA team
Bacillus fulminans
-
-
Manually annotated by BRENDA team
Streptomyces sp. OH11242
-
-
-
Manually annotated by BRENDA team
-
two forms, alpha-fucosidase I and II
Manually annotated by BRENDA team
-
partly secretory and partly non-secretory bound form
Manually annotated by BRENDA team
-
not detected in adjacent tissue
Manually annotated by BRENDA team
Venus mercenaria
-
-
Manually annotated by BRENDA team
-
cell colorectal cancer cells
Manually annotated by BRENDA team
-
no activity above pI 7.0
Manually annotated by BRENDA team
-
activities below and above pI 7.0
Manually annotated by BRENDA team
-
no activity above pI 7.0
Manually annotated by BRENDA team
-
characterization of alpha-fucosidase from fucosidosis patients
Manually annotated by BRENDA team
-
normal and I-cell disease samples
Manually annotated by BRENDA team
-
two forms: S1 and S3
Manually annotated by BRENDA team
-
two isoforms: A, B, characterized during epididymal maturation
Manually annotated by BRENDA team
-
one form tightly bound to the sperm plasma membrane, one form present in the gonad fluid
Manually annotated by BRENDA team
-
plasma membrane associated
Manually annotated by BRENDA team
-
; 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
Manually annotated by BRENDA team
-
activities below and above pI 7.0
Manually annotated by BRENDA team
-
samples from pseudo-Hurler polydystrophy
Manually annotated by BRENDA team
-
whole fly homogenates
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of liver cancer cell, not detected in adjacent tissue
-
Manually annotated by BRENDA team
-
normally a lysosomal glycoprotein, released by secretion and/or cell lysis
-
Manually annotated by BRENDA team
-
increasing activity up to aggregation stage, not detectable in the growth phase
-
Manually annotated by BRENDA team
-
maximal enzyme synthesis by growth on porcine gastric mucin containing media
-
Manually annotated by BRENDA team
-
induction of enzyme synthesis by addition of L-fucose to the medium
-
Manually annotated by BRENDA team
-
partly secretory from cauda epididymidis
-
Manually annotated by BRENDA team
-
most induction of enzyme synthesis if cells grown in 2% active sludge hydrolyzate medium
-
Manually annotated by BRENDA team
-
gastric cancer cells infected with Helicobacter pylori secrete isoform Fuc2A
-
Manually annotated by BRENDA team
Bacillus fulminans
-
-
Manually annotated by BRENDA team
-
fucosidase is broadly distributed over the membrane systems of human sperm, but is relatively enriched within the equatorial segment; 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
Manually annotated by BRENDA team
-
bound in membrane of monocytes
Manually annotated by BRENDA team
-
specifically localized to the convex region of the prinicipal segment of testicular and cauda epididymal sperm heads
Manually annotated by BRENDA team
-
10-20% of the total cellular enzyme
Manually annotated by BRENDA team
-
overlying the acrosome, integral membrane protein terminally mannosylated, with the catalytic site oriented towards the extracellular space
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
38100
-
-
originates from the translational termination of the ribosome at the OCH codon of the fucA1 N-terminal ORF, Western blot analysis
50000
-
-
alpha-fucosidase II, gel filtration
50000
-
-
SDS-PAGE
51000
-
-
SDS-PAGE
55970
-
-
gonad fluid enzyme, mass spectrometry
62000
-
-
gel filtration
67850
-
-
sperm-bound enzyme, mass spectrometry
68000
-
-
gel filtration, two acid forms
70000
75000
-
gel filtration
70000
80000
Bacillus fulminans
-
gel filtration
75000
-
-
gel filtration
78700
-
-
originates from frameshifting in either site A or B of fucA1, Western blot analysis
80000
-
-
gel filtration
85000
-
-
gel filtration, neutral form
86000
-
-
major form
93800
-
-
membrane-bound form
97000
-
-
Western blot analysis
100000
-
-
gel filtration, alpha-fucosidase I
109000
116000
-
gel filtration, soluble form
156000
-
-
gel filtration
180000
-
-
gel filtration
192000
-
-
gel filtration
200000
-
-
isoform GF-2, gel filtration
200000
-
-
gel filtration
200000
-
-
gel filtration
200000
-
-
gel filtration
200000
-
-
gel filtration
200000
-
-
gel filtration
210000
220000
-
sedimentation equilibrium centrifugation
217000
-
-
sedimentation equilibrium centrifugation
220000
-
-
gel filtration
230000
-
-
sedimentation equilibrium centrifugation
230000
-
-
sedimentation equilibrium centrifugation
230000
-
-
minor form
233000
-
-
gel filtration
236000
-
-
gel filtration
240000
-
-
gel filtration
256000
-
-
gel filtration
260000
-
-
gel filtration
270000
-
-
gel filtration at pH 7.0
285000
-
-
gel filtration
285000
-
-
gel filtration
300000
-
-
gel filtration
305000
-
-
gel filtration at pH 5.0 or 6.0, molecular weight depends on pH-value
330000
-
-
isoform GF-1, gel filtration
390000
-
-
gel filtration at pH 5.0
473000
-
-
gel filtration
508000
-
-
gel filtration, recombinant enzyme
508000
-
-
mutant fucA1B, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 51000, SDS-PAGE
?
-
x * 47000-49000 Da, SDS-PAGE
?
-
x * 37000, SDS-PAGE
?
-
x * 48000 + x * 55000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 57700, calculated, x * 80000, recombinant GFP fusion protein including His-tag, SDS-PAGE
decamer
-
10 * 57000, recombinant enzyme
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 135000, SDS-PAGE
dimer
-
alpha-fucosidase I, 2 * 50000, SDS-PAGE, can aggregate to tetra- and hexamers
hexamer
-
hexamer of two trimers
monomer
-
1 * 55971, gonad fluid enzyme, 1 * 67847, sperm-bound enzyme, mass spectrometry
monomer
-
1 * 51000, SDS-PAGE
monomer
-
1 * 62000, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
nonamer
-
9 * 57400, calculated from sequence
nonamer
-
9 * 57000
oligomer
-
contains subunits of 55 kDa and 52 kDa, SDS-PAGE
oligomer
-
contains subunits of 63 kDa, SDS-PAGE
oligomer
-
subunits of 50.1 kDa each, SDS-PAGE
tetramer
-
4 * 54000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 63000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 73500, SDS-PAGE, monomers and dimers also active
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 50000, gel filtration
tetramer
-
2 * 60000 + 2 * 2 * 47000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 61000, SDS-PAGE
tetramer
-
4 * 56000-57000, SDS-PAGE
tetramer
-
4 * 61000, SDS-PAGE
-
monomer
-
alpha-fucosidase II, 1 * 50000, SDS-PAGE, less-biologically active form, can aggregate to tetra- and hexamers
additional information
-
x * 59000, fase I, x * 56000 + x * 57000, fase II, SDS-PAGE
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
Streptomyces sp. OH11242
-
x * 59000, fase I, x * 56000 + x * 57000, fase II, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
10%, w/w, carbohydrate content
glycoprotein
-
-
glycoprotein
-
-
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
glycoprotein
-
-
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 0.9% galactose, 1.9% mannose, 1.9% N-acetylglucosamine, 1.9% N-acetylneuraminic acid, w/w
glycoprotein
-
1% carbohydrate content per molecule
sialoglycoprotein
-
the enzyme occurs in different isoforms depending on the number of terminal sialic acid residues present on the glycoprotein molecules
glycoprotein
-
contains 7.4% glucose, 2.2% galactose, 1.8% mannose, 2.2% hexosamine
glycoprotein
-
sialylated
glycoprotein
-
sialylated
glycoprotein
-
-
glycoprotein
-
4.7%, w/w, mannose content for isoform F1, 5%, w/w, mannose content for isoforms F2
glycoprotein
-
isoform A derived by sialylation of isoform B near the end of epididymal maturation
glycoprotein
-
-
glycoprotein
-
residues per tetramer: fucose 3.5, mannose 32, galactose 8: glucose 9, glucosamine 32, sialic acid 8
glycoprotein
-
0.6% carbohydrate per native molecule
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
N-linked oligosaccharides only for the gonad fluid enzyme, sperm-bound enzyme not N- or O-linked glycosylated
additional information
-
treatment of enzyme with neuraminidase does not change its isoform profile
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
recombinant enzyme, vapor diffusion method
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
8
-
4 h, above and below decrease in enzyme activity
3
5
-
form S1, most stable between
3
5.5
-
at pH 3.0 and pH 5.5: more than 50% of the fucosidase activity
3
7
-
stable within
3
-
-
rapid inactivation
4
10
-
fairly stable within
4
6
-
stable between
4
7
-
isoform F1: stable within
4
8
-
stable within
4
8
-
stable in the presence of 0.05 mg/mg bovine serum albumin, 1 mM 2-mercaptoethanol
4.5
6
-
stable within
4.5
7
-
isoform F2: stable within
4.5
9
-
stable within, kept at 4C
5
6
-
most stable within, form S3
5
8
-
stable between
5.5
10
-
stable within
5.5
7.5
-
the enzyme is stable overnight at 37C
5.5
-
-
instability below
7
-
-
55C, 4 h
7
-
-
5% CO2 and high humidity or ambient air, 37C, 24 h, 20-100% loss of activity, depending on conditions
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
loss of activity within 1 week
4
55
-
highly stable
25
-
-
50% remaining activity after 2 h
30
-
-
30 min, stable
37
-
-
half-life: 1 h
37
-
-
gradual loss of activity after 6 min for the purified enzyme, in crude state: stable for 4 h
37
-
-
50% activity after 2 h, complete loss of activity after 4 h
37
-
-
the enzyme is stable overnight in the pH range from 5.5 to 7.5
37
-
-
100% activity after 6 h
37
-
-
5% CO2 and high humidity or ambient air, pH 7.0, 24 h, 20-100% loss of activity, depending on conditions
45
-
-
stable up to
45
-
-
stable below
45
-
-
stable up to
45
-
-
thermal inactivation at temperatures above 45C
45
-
-
30 min, 40% loss of activity
50
55
-
greatly decreased thermostability in fucosidosis patients
50
55
-
triphasic heat inactivation due to 3 different heat sensitive forms, forms I and II: less heat sensitive, form III: most heat sensitive
50
-
Bacillus fulminans
-
7% loss of activity after 5 min
50
-
-
isoform A: 50% inactivation in 1 h, isoform B: 50% inactivation in 10 min
50
-
-
native enzyme: 80% residual activity after 2 h, deglycosylated enzyme: 38% residual activity after 2 h
50
-
-
inactivation above, isoform GF-1 more heat stable than GF-2
50
-
-
-
50
-
-
from mouse liver: more labile against inactivation than from human liver or mouse placental enzymes
50
-
-
30% loss of activity after 3 h
50
-
-
alpha-fucosidase I: 50% loss of activity in 40 min, alpha-fucosidase II: 20% loss of activity in 40 min
50
-
-
30 min, complete loss of activity
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
55
-
-
pH 7.0, 4 h
60
65
-
isoform F2: stable up to
60
-
-
40% of activity remains after 1 day
60
-
-
the activity decreases rapidly at temperatures above 60C
60
-
-
the enzyme shows no loss of activity after 24 h
65
-
-
fairly stable up to
65
-
-
isoform F1: stable up to
65
-
-
completely abolished
65
-
-
stable for 10 min
65
-
-
fully active after 5 min
70
-
Bacillus fulminans
-
77% loss of activity after 5 min
70
-
-
50% loss of activity after 5 min
70
-
-
60% loss of activity
75
-
-
high stability
80
-
-
60% residual activity after 2 h
80
-
-
2 h, 40% loss of activity; displays high stability maintaining 60% of the residual activity after 2 h
100
-
-
denatured by heating over 100C for 5 min
additional information
-
-
comparison of heat stability of enzyme from undifferentiated and differentiated HT-29 cells
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sensitive to repeated freezing and thawing
-
increased half-life to 23 h at 37C and stability to repeated freezing and thawing by addition of 0.5 mg/ml bovine serum albumin
-
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 2-4C retains 100% activity after 2 weeks.
-
60% loss of activity after lyophilization
-
stabilizing effect by addition of 0.05 mM/ml bovine serum albumin, 1 mM 2-mercaptoethanol, 1 mM MgSO4, high protein concentrations required
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimethyl formamide
-
-
dimethyl formamide
-
more stable than the Aspergillus niger enzyme, no loss of activity up to 10%, v/v
dimethyl sulfoxide
-
-
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
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
frozen, 1 year
-
4C, 0.2 M sodium citrate, pH 6.0, 20% polyethylene glycol, 2 months
-
-20C, 0.5 mg/ml bovine serum albumin, 6 months
-
4C, 3 weeks, enzyme retains 100% of its activity when stored in presence of 20 mM CHAPS
-
-10C, 3-6% loss of activity after 3 days
-
-20C, fully active after 29 days, 0-4C, 10 mM Na2HPO4, pH 5.5, 0.02% NaN3, w/v, 100 mM L-fucose, 163 days
-
-20C, in the presence of 1% fucose and presence or absence of 0.015% Triton X-100, 100% activity after 2 weeks
-
-20C, pH 5.5 in presence of 1% L-fucose, 100% activity after 6 weeks
-
2-4C, in the presence of 1% fucose and 0.015% Triton X-100, 100% activity after 3 months
-
2-4C, pH 5.5 in presence of 1% L-fucose, 77% activity after 6 weeks
-
21C, pH 5.5 in presence of 1% L-fucose, 100% activity after 3 days
-
37C, 5% CO2, ambient air, pH 7.0, 24 h loss of activity and increase of the pH-value, membrane associated enzyme
-
37C, 5% CO2, high humidity, 24 h, 70% loss of activity, enzyme in semen from storage in liquid nitrogen
-
37C, 5% CO2, high humidity, 24 h, 90% loss of activity, enzyme in seminal plasma
-
37C, 5% CO2, high humidity, 72 h, no activity, enzyme in seminal plasma
-
37C, 5% CO2, high humidity, pH 7.0, 24 h, 20% loss of activity, membrane associated enzyme
-
37C, 5% CO2, high humidity, pH 7.0, 72 h, 30% loss of activity, membrane associated enzyme
-
55C, LB medium, 4 h
-
4C, 0.2 M sodium citrate, pH 6.0, 20% polyethylene glycol, 2 months
-
2-4C, 29 days
-
30C, 30% loss of activity after 40 days
-
60C, 40% loss of activity after 1 day
-
frozen, more than 90% of its initial activity after 3 months
-
-20C, acetate buffer, pH 6.0, 100 mM L-fucose, several months
-
2-4C, stable for one month
-
4C, 0.2 M sodium citrate, pH 6.0, 20% polyethylene glycol, 2 months
-
4C, 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
-
4C, 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, 10 mM sodium phosphate, pH 5.5, 1 mM EDTA, 1 mM PMSF, one month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity, chromatography techniques
-
near homogeneity, chromatography techniques
Bacillus fulminans
-
partial, three forms at different pI-values
-
homogeneous, chromatography techniques
-
to homogeneity, recombinant enzyme
-
to homogeneity, isoelectric focusing
-
to homogeneity, affinity chromatography
-
to homogeneity, affinity chromatography
-
to homogeneity, affinity chromatography
-
homogeneous, chromatography steps
-
33fold
-
by ion-exchange chromatography, more than 95% homogeneity
-
near homogeneity, 1step affinity chromatography
-
to homogeneity, 2step affinity chromatography
-
to homogeneity, affinity chromatography
-
to homogeneity, affinity chromatography, isoelectric focusing, 2 forms, alpha-L-fucosidase A and B
-
to homogeneity, two forms: alpha-fucosidase I and II, affinity chromatography
-
to homogeneity, affinity chromatography
-
to homogeneity, isoelectric focusing
-
to homogeneity, chromatography steps
-
near homogeneity
-
near homogeneity, antibody affinity chromatography
-
to homogeneity, affinity chromatography
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography techniques, two isoforms: F1, F2
-
partial, two forms
-
to homogeneity, affinity chromatography, alpha-fucosidase I
-
near homogeneity
-
to homogeneity, affinity chromatography
-
two fractions, fase I and II
-
by GST purification system, mutant fucA1B purified up to 95%
-
to homogeneity, affinity chromatography
-
by Ni2+-affinity chromatography; recombinant
Q9WYE2
partially purified
-
to homogeneity, two forms, affinity chromatography
-
to homogeneity, isoelectric focusing
-
to homogeneity, affinity chromatography, two isoforms
Venus mercenaria
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Pichia pastoris
-
expression in CHO cells; expression in MDCK cells
-
expression in Trichoplusia ni cells
-
expression in Escherichia coli stream BL21(DE3)
-
through pET21b expression vector
-
expressed in Escherichia coli; expression in Escherichia coli
-
expression in Escherichia coli
-
wild-type and mutants as GST fusions expressed in Escherichia coli strain BL21(RB791)
-
expression in Escherichia coli; into the pET21a vector, transformed into Escherichia coli Novablue cells, into plasmid pBTac2 and expressed in Escherichia coli XL1 blue MRF'
Q9WYE2
through pET21b expression vector
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
Bacteroides thetaiotaomicron Bt2970
-
inactive, mutation of the catalytic nucleophile. Crystallization data
-
E288Q
Bacteroides thetaiotaomicron Bt2970
-
acid/base variant, crystallization data in complex with substrate 2-fluoro fucosyl fluoride
-
D124G
-
kcat/Km at 65C and pH 6.3 is 3.7fold lower than the wild-type value
D124G
-
activity is not significantly affected; kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 3.7fold lower than wild-type value
D146G
-
kcat/Km at 65C and pH 6.3 is 1.5fold lower than the wild-type value
D146G
-
activity is not significantly affected; 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; 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 65C and pH 6.3 is 310.6fold lower than the wild-type value; kcat/Km at 65C 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; kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 311fold lower than wild-type value
E58G
-
kcat/Km at 65C and pH 6.3 is 1897fold lower than the wild-type value; kcat/Km is 10.8-3897fold lower than wild-type value depending on pH-value and buffer
E58G
-
affects catalysis severely; kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 5395fold lower than wild-type value
H123G
-
kcat/Km at 65C 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; kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 2929fold lower than wild-type value
H46G
-
kcat/Km at 65C and pH 6.3 is 410fold lower than the wild-type value
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
Q9WYE2
exhibits a higher kcat than the wild-type; the transferase/hydrolytic kinetic ratio is 22fold higher compared to wild-type ratio
G226S/Y237H/T264A/L322P
Q9WYE2
no significant modified transglycosylation properties; the transferase/hydrolytic kinetic ratio is 34fold higher compared to wild-type ratio
L191A
-
slow tight-binding inhibition, kinetics like wild type, affinity for compound 1 comparable to the wild-type level
M210V/Y237H/T264A
Q9WYE2
exhibits a higher kcat than the wild-type; the transferase/hydrolytic kinetic ratio is 10fold higher compared to wild-type ratio
M210V/Y237H/T264A/Y267F
Q9WYE2
exhibits a lower kcat than the wild-type; the transferase/hydrolytic kinetic ratio is 11fold higher compared to wild-type ratio
M210V/Y237H/T264A/Y267F/L322P
Q9WYE2
no significant modified transglycosylation properties; the transferase/hydrolytic kinetic ratio is 31.5fold higher compared to wild-type ratio
M225A
-
slow tight-binding inhibition, kinetics like wild type, affinity for compound 1 comparable to the wild-type level
P196L/Y237H/Y267F
Q9WYE2
exhibits higher transglycosylation activity than the wild-type; the transferase/hydrolytic kinetic ratio is 7.5fold higher compared to wild-type ratio
R147G/L322P
Q9WYE2
exhibits higher transglycosylation activity than the wild-type; the transferase/hydrolytic kinetic ratio is 8.5fold higher compared to wild-type ratio
T264A
Q9WYE2
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; the transferase/hydrolytic kinetic ratio is 13fold higher compared to wild-type ratio
T264A/L322P
Q9WYE2
exhibits a higher kcat than the wild-type; the transferase/hydrolytic kinetic ratio is 20fold higher compared to wild-type ratio
T264A/Y267F/L322P
Q9WYE2
causes a reorientation of the amino acids that are in direct contact with the substrates, resulting in a better docking energy; the transferase/hydrolytic kinetic ratio is 27.5fold higher compared to wild-type ratio
W58A
-
instabile
Y237H/Y267F/L322P
Q9WYE2
exhibits a higher kcat than the wild-type; the transferase/hydrolytic kinetic ratio is 20.5fold higher compared to wild-type ratio
Y267A
-
affinity for compound 1 comparable to the wild-type level
Y64A
-
affinity for compound 1 comparable to the wild-type level
H46G
-
affinity for the substrate is remarkably different from that of the wild-type, 607fold increase in the KM; kcat/KM for 4-nitrophenyl-alpha-L-fucopyranoside is 410fold lower than wild-type value
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
medicine
-
recombinant enzyme will extend the proven efficiacy of enzyme replacement therapy in lysosomal storage disorders e.g. fucosidosis
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
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
-
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
-
may be useful as a biomarker for predicting the progression-free survival of for trastuzumab treatment; 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
-
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
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
-
studies of structures and functions of glycoconjugates and oligosaccharides due to unique substrate specificity
medicine
-
deficiency in enzyme activity is associated with fucosidosis
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