Information on EC 3.2.1.44 - fucoidanase

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

EC NUMBER
COMMENTARY hide
3.2.1.44
-
RECOMMENDED NAME
GeneOntology No.
fucoidanase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->2)-alpha-L-fucoside linkages in fucoidan without release of sulfate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
endoglycosidic
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SYSTEMATIC NAME
IUBMB Comments
poly[(1->2)-alpha-L-fucoside-4-sulfate] glycanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-38-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ox
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Gramella sp.
marine bacterium, Flavobacteriaceae, strain KMM6054, associant of the sea urchin Strongylocentrotus intermedius
-
-
Manually annotated by BRENDA team
Haliotis sp.
abalone
-
-
Manually annotated by BRENDA team
Littorina kurila
-
-
-
Manually annotated by BRENDA team
marine bacterium, Flavobacteriaceae, strain KMM6211, associant of the sea urchin Strongylocentrotus intermedius
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-
Manually annotated by BRENDA team
marine bacterium, Flavobacteriaceae, strain KMM3909T, isolated from the green alga Acrosiphonia sonderi
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain KMM 3296
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-
Manually annotated by BRENDA team
strain KMM 3296
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-
Manually annotated by BRENDA team
strain PF-1, growth on minimal medium containing fucoidan as the sole carbon source
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-
Manually annotated by BRENDA team
strain PF-1, growth on minimal medium containing fucoidan as the sole carbon source
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain SW5, member of the family Flavobacteriaceae
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-
Manually annotated by BRENDA team
strain N5
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain N5
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-L-fucoside + H2O
alpha-1,2-fucoside + 4-nitrophenol
show the reaction diagram
4-nitrophenyl-alpha-L-fucopyranoside + H2O
4-nitrophenol + L-fucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-alpha-L-fucoside + H2O
alpha-L-fucopyranose + 4-nitrophenol
show the reaction diagram
alpha-1,2-fucoside 4-sulfate + H2O
alpha-1,2-fucoside 4-sulfate + oligosaccharides
show the reaction diagram
fucoidan + H2O
?
show the reaction diagram
fucoidan + H2O
polysaccharide
show the reaction diagram
Littorina kurila
-
-
the main product is a polysaccharide built up of disaccharide repeating units (-->3)-alpha-L-Fucp-(2,4-di-SO3-)-(1->4)-alpha-L-Fucp-(2SO3-)-(1->)
-
?
p-nitrophenyl alpha-L-fucoside + H2O
alpha-1,2-fucoside + p-nitrophenol
show the reaction diagram
p-nitrophenyl-alpha-L-fucopyranoside + H2O
p-nitrophenol + alpha-L-fucopyranose
show the reaction diagram
Littorina kurila
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-1,2-fucoside 4-sulfate + H2O
alpha-1,2-fucoside 4-sulfate + oligosaccharides
show the reaction diagram
fucoidan + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates, maximal activity above 30 mM
Co2+
-
all three enzymes are slightly activated
Mg2+
Haliotis sp.
-
activating at 0.01 M
NaCl
Littorina kurila
-
at pH 5.4, activity maximum at 0.2 M NaCl, at pH 8.4, 50% inhibition at 0.2 M NaCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
Haliotis sp.
-
inhibitory at high concentrations
Fe3+
-
inhibits all three enzymes
NaCl
Littorina kurila
-
at pH 5.4, activity maximum at 0.2 M NaCl, at pH 8.4, 50% inhibition at 0.2 M NaCl
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose
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induces synthesis of fucoidanases, biosynthesis increases with the cultivation time
D-xylose
N-ethylmaleimide
Haliotis sp.
-
at concentrations above 0.001 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 0.22
p-nitrophenyl alpha-L-fucoside
additional information
fucoidan
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.053
-
isozyme E-2
0.066
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isozyme E-1
0.114
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isozyme E-3
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
Haliotis sp.
-
-
5.5
Littorina kurila
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and second optimum at pH 8.0
5.6
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-
5.8
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-
7.5
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isozyme E-3
8
Littorina kurila
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and second optimum at pH 5.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
Haliotis sp.
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38 - 45
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all three enzymes
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
12.5% of maximum activity
50
Haliotis sp.
-
85% of activity remains
80
-
19% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Littorina kurila
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39500
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E-1, SDS-PAGE
40000 - 68000
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-
64000
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x * 64000, SDS-PAGE
67500
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E-1, gel filtration
68000
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E-2 and E-2, SDS-PAGE
68500
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E-2, gel filtration
84000
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SDS-PAGE
100000 - 200000
Haliotis sp.
-
gel filtration
158000
-
E-1, gel filtration
180000
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x * 180000, SDS-PAGE
200000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
secondary structure analysis FTIR, the second derivative spectra, and the curve-fitting analysis of the amide I bands in their spectra. beta-Sheets are the dominant component with 58%, plus 12% alpha-helices, the content of beta-turns and random coil are 15.39% and 14.5%, respectively
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
4 h, 50% of maximum activity
715321
4 - 9
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all three enzymes
136446
4.5 - 6
5
-
5 h, 50% loss of activity
714918
5 - 9
Haliotis sp.
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highest stability at pH 7.5
136444
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
-
1 h, 50% loss of activity
70
-
all three enzymes were 50% inactivated at this temperature
80
-
complete inactivaion above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, concentrated preparation loses activity after about 3 weeks
0C, concentrated preparation loses activity after about 3 weeks
0C, in 50 mM Tris-HCl buffer, pH 7.5, all three enzymes stable for at least 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
25fold
Haliotis sp.
-
after solid state fermentation of Dendryphiella arenaria TM94
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after solid-state fermentation of Fusarium sp.
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E-1: 29.2fold, E-2: 23.3fold, E-3: 50.5fold
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
additional information