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D-Allose
D-Psicose
16%, relative activity compared to activity with D-galactose
-
-
?
D-fucose
D-fuculose
221% activity compared to D-galactose
-
-
r
D-Galactose
?
Lactobacillus gayonii
-
weak activity
-
-
-
D-gulose
D-sorbose
1.3%, relative activity compared to activity with D-galactose
-
-
?
D-rhamnose
?
28% activity compared to D-galactose
-
-
?
D-ribulose
?
12%, relative activity compared to activity with D-galactose
-
-
?
D-sorbose
?
31% activity compared to D-galactose
-
-
?
D-tagatose
D-galactose
-
-
-
-
r
D-Xylose
D-Xylulose
7.0%, relative activity compared to activity with D-galactose
-
-
?
L-Fucose
L-Fuculose
only F279 mutant
-
-
?
L-ribulose
L-arabinose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
-
-
r
additional information
?
-
D-Allose

?
about 10% activity compared to D-galactose
-
-
?
D-Allose
?
about 10% activity compared to D-galactose
-
-
?
D-Allose
?
9% activity compared to D-galactose
-
-
?
D-Allose
?
9% activity compared to D-galactose
-
-
?
D-Fucose

?
-
slightly less than 10% of the activity on L-arabinose
-
-
-
D-Fucose
?
-
slightly less than 10% of the activity on L-arabinose
-
-
-
D-Fucose
?
9.3%, relative activity compared to activity with D-galactose
-
-
?
D-galactose

D-tagatose
conversion yield over 50% after 12 h under optimal conditions
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
the enzyme has high preference for D-galactose (100% activity)
-
-
?
D-galactose
D-tagatose
the enzyme has high preference for D-galactose (100% activity)
-
-
?
D-galactose
D-tagatose
-
30% yield after 36 h at 50°C
-
?
D-galactose
D-tagatose
-
30% yield after 36 h at 50°C
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
at elevated temperatures, not dependent on divalent metal ions
-
-
?
D-galactose
D-tagatose
-
2% of the activity with L-arabinose
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
36% yield after 6 days of incubation at 35°C
-
?
D-galactose
D-tagatose
-
36% yield after 6 days of incubation at 35°C
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
r
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
at elevated temperatures in the presence of divalent metal ions
-
-
?
D-galactose
D-tagatose
-
the bioconversion yield of D-galactose to D-tagatose by the purified enzyme after 12 h at 65°C reaches 36%
-
-
?
D-galactose
D-tagatose
-
the bioconversion yield of D-galactose to D-tagatose by the purified enzyme after 12 h at 65°C reaches 36%
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
100% activity
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
39% conversion after 48 h at pH 6.0 and 65°C
-
?
D-galactose
D-tagatose
100% activity, conversion rate of 55% with 1mM Mn2+ after 12 h at 65°C
-
-
?
D-galactose
D-tagatose
100% activity, conversion rate of 55% with 1mM Mn2+ after 12 h at 65°C
-
-
?
D-galactose
D-tagatose
-
39% conversion after 48 h at pH 6.0 and 65°C
-
?
D-galactose
D-tagatose
Lactobacillus gayonii
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
36% conversion after 7 h at 40°C
-
-
?
D-galactose
D-tagatose
-
36% conversion after 7 h at 40°C
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
45.6% conversion at 40°C
-
?
D-galactose
D-tagatose
-
45.6% conversion at 40°C
-
?
D-galactose
D-tagatose
100% activity
conversion of 52% after 24 h at 50°C
-
?
D-galactose
D-tagatose
100% activity
conversion of 52% after 24 h at 50°C
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
43.9% yield with immobilized enzyme
-
?
D-galactose
D-tagatose
100% activity
-
-
r
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-galactose
D-tagatose
-
56% conversion after 6 h at 80°C
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
the conversion equilibrium shifts to more ketone sugar from aldose sugar as the isomerization reaction temperature raises. 68% conversion of D-galactose to D-tagatose at 80°C
-
r
D-galactose
D-tagatose
-
the conversion equilibrium shifts to more ketone sugar from aldose sugar as the isomerization reaction temperature raises. 68% conversion of D-galactose to D-tagatose at 80°C
-
r
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
-
?
D-galactose
D-tagatose
-
-
-
?
D-glucose

?
less than 40% activity compared to D-galactose
-
-
?
D-glucose
?
less than 40% activity compared to D-galactose
-
-
?
D-Ribose

?
7% activity compared to D-galactose
-
-
?
D-Ribose
?
7% activity compared to D-galactose
-
-
?
D-xylose

-
32.3% activity compared to D-galactose
-
-
?
D-xylose
-
32.3% activity compared to D-galactose
-
-
?
D-Xylose

?
-
slightly less than 10% of the activity on L-arabinose
-
-
-
D-Xylose
?
-
slightly less than 10% of the activity on L-arabinose
-
-
-
D-Xylose
?
about 70% activity compared to D-galactose
-
-
?
D-Xylose
?
about 70% activity compared to D-galactose
-
-
?
D-Xylose
?
14% activity compared to D-galactose
-
-
?
D-Xylose
?
14% activity compared to D-galactose
-
-
?
L-Arabinose

?
-
enzyme of pentose pathway
-
-
-
L-Arabinose
?
-
catalyzes the first step in catabolism of L-arabinose
-
-
-
L-Arabinose

L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
r
L-Arabinose
L-Ribulose
-
-
-
r
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
40% activity compared to D-galactose
-
-
?
L-Arabinose
L-Ribulose
40% activity compared to D-galactose
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
substrate conversion of 19.4% within 1.5 h
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
r
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
the Bacillus licheniformis L-arabinose isomerase shows a high degree of substrate specificity for L-arabinose. The conserved amino acid Y333 in the substrate binding pocket of the wild-type L-AI is important for the catalytic efficiency, other putative catalytic residues are E306, E333, H350, and H450
-
-
?
L-Arabinose
L-Ribulose
the enzyme has a high preference only for L-arabinose
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
-
-
r
L-Arabinose
L-Ribulose
the enzyme shows high substrate specificity
-
-
r
L-Arabinose
L-Ribulose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
-
-
r
L-Arabinose
L-Ribulose
-
11% yield after 2 h of incubation at 35°C
-
?
L-Arabinose
L-Ribulose
-
11% yield after 2 h of incubation at 35°C
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
other aldoses like D-fucose, D-ribose, D-allose, D-mannose and D-xylose are poor substrates for the wild type and the mutated enzymes
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
other aldoses like D-fucose, D-ribose, D-allose, D-mannose and D-xylose are poor substrates for the wild type and the mutated enzymes
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
33% conversion yield within 720 h at pH 7.5 and 60°C
-
?
L-Arabinose
L-Ribulose
1482%, relative activity compared to activity with D-galactose
-
-
?
L-Arabinose
L-Ribulose
-
equilibrium ratio of L-arabinose to L-ribulose is 88.8:11.2 at 25°C, 80.0:19.0 at 55°C, and 78.0:22.0 at 75°C
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
high preference for L-arabinose (220% compared to D-galactose)
-
-
r
L-Arabinose
L-Ribulose
high preference for L-arabinose (220% compared to D-galactose)
-
-
r
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
Lactobacillus gayonii
-
-
-
-
L-Arabinose
L-Ribulose
Lactobacillus gayonii
-
r
-
-
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
r
-
-
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
-
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
244% activity compared to D-galactose
-
-
r
L-Arabinose
L-Ribulose
244% activity compared to D-galactose
-
-
r
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
70% conversion to L-ribulose in 6 h at 80°C
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
-
?
L-Arabinose
L-Ribulose
-
-
-
?
L-Fucose

?
-
slightly less than 10% of the activity on L-arabinose
-
-
-
L-Fucose
?
-
slightly less than 10% of the activity on L-arabinose
-
-
-
additional information

?
-
-
D-glucose and D-allose do not serve as substrate
-
-
-
additional information
?
-
D-glucose and D-allose do not serve as substrate
-
-
-
additional information
?
-
D-glucose and D-allose do not serve as substrate
-
-
-
additional information
?
-
-
no substrate: L-ribose, L-xylose, D-glucose, D-mannose, D-xylose, and D-allose
-
-
-
additional information
?
-
-
other aldoses than L-arabinose including D-galactose are ineffective as substrate (1% or less, compared with L-arabinose)
-
-
-
additional information
?
-
other aldoses than L-arabinose including D-galactose are ineffective as substrate (1% or less, compared with L-arabinose)
-
-
-
additional information
?
-
-
no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview
-
-
-
additional information
?
-
no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview
-
-
-
additional information
?
-
D-xylose (2.7%), D-mannose (2.5%), L-xylose (1.9%), D-glucose (1.7%), and L-ribose (0.7%) do not serve as substrates in the presence of Mn2+ or Co2+
-
-
-
additional information
?
-
D-xylose (2.7%), D-mannose (2.5%), L-xylose (1.9%), D-glucose (1.7%), and L-ribose (0.7%) do not serve as substrates in the presence of Mn2+ or Co2+
-
-
-
additional information
?
-
no activity with L-arabinose
-
-
-
additional information
?
-
-
no activity with L-arabinose
-
-
-
additional information
?
-
no activity with L-arabinose
-
-
-
additional information
?
-
-
no activity with L-arabinose
-
-
-
additional information
?
-
-
no substrate: D-galactose
-
-
-
additional information
?
-
no substrate: D-galactose
-
-
-
additional information
?
-
-
no substrate: D-galactose
-
-
-
additional information
?
-
no substrate: D-galactose
-
-
-
additional information
?
-
no activity with D-glucose, D-mannose, and L-fucose
-
-
-
additional information
?
-
no activity with D-glucose, D-mannose, and L-fucose
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K+
Lactobacillus gayonii
-
slight activation
Sr2+
Lactobacillus gayonii
-
slight activation
Ba2+

activating
Ba2+
inhibits galactose isomerization, remaining activity 94%
Ba2+
120% activity at 1 mM
Ca2+

-
poor activator
Ca2+
the addition of Ca2+ has slightly positive but no significant effect on the enzyme activity
Ca2+
serves as catalyst; serves as catalyst
Ca2+
serves as catalyst; serves as catalyst; serves as catalyst
Ca2+
106% of the activity with Mn2+
Ca2+
-
serves as catalyst
Ca2+
enhances galactose isomerization by 12%
Ca2+
-
the most effective enzyme activator with the reaction rate by 150%
Ca2+
-
serves as catalyst
Ca2+
Lactobacillus gayonii
-
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
-
serves as catalyst
Ca2+
-
serves as catalyst
Co2+

activates and increase thermostability of the enzyme
Co2+
1 mM required for activity
Co2+
3fold increase in activity, assay in presence of 0.5 mM
Co2+
-
the enzyme activity is significantly increased by adding 1 mM Co2+ (2.9fold)
Co2+
0.5 mM, 190% of the activity of EDTA-treated enzyme
Co2+
-
or Mn2+, required. 443% of initial activity at 1 mM
Co2+
1 mM, 110% of initial activity
Co2+
-
does not restore activity after dialysis with EDTA
Co2+
-
60% activation compared to Mn2+
Co2+
increase in activity at 80°C only, no effect at 65°C
Co2+
activating, highest activity of the mutated enzyme at 1.0 mM
Co2+
enhances galactose isomerization by 11%, maximum activity occurs at 3 mM Mn2+
Co2+
201% activity at 1 mM, Co2+ is required for enzymatic activity and thermostability
Co2+
Lactobacillus gayonii
-
slight activation
Co2+
Lactobacillus gayonii
-
activates to about half the extent of Mn2+
Co2+
required for maximal activity and stability
Co2+
-
Mn2+, Mg2+ or Co2+ required
Co2+
this enzyme exhibits a weak requirement for metal ions for its maximal activity evaluated at 0.6 mM Mn2+ and 0.8 mM Co2+ (115.38% activity in the presence of Mn2+ and Co2+)
Co2+
1 mM, 4.2fold activation
Co2+
-
restores activity after dialysis against EDTA
Co2+
addition of CoSO4 reactivates the enzyme to 45% after inactivation with EDTA
Co2+
-
improves the enzymatic activity to 121% at 5 mM
Co2+
0.05 mM Co2+, can improve both catalytic activity and thermostability at higher temperatures
Co2+
-
Mn2+ or Co2+ required, about 1 mM Co2+ restores activity of dialyzed enzyme
Co2+
-
preferred cofactor
Co2+
-
divalent cation, maximal activity in presence of both Mn2+ and Co2+
Co2+
-
1mM for the free enzyme and for the immobilized enzyme in Escherichis coli cells
Cu2+

inhibitory
Cu2+
inhibits galactose isomerization remaining activity 42%
Fe2+

activating
Fe2+
-
106% relative activity at 1 mM
Fe2+
inhibits galactose isomerization remaining activity 98%
Fe2+
addition of FeSO4 reactivates the enzyme to 76% after inactivation with EDTA
Mg2+

1 mM required for activity
Mg2+
-
240% of initial activity at 1 mM
Mg2+
the addition of Mg2+ has slightly positive but no significant effect on the enzyme activity
Mg2+
1 mM, 120% of initial activity
Mg2+
117% of the activity with Mn2+
Mg2+
-
50% activation compared to Mn2+
Mg2+
enhances galactose isomerization by 9%
Mg2+
-
the enzyme has low metal requirement of only 0.8 mM Mg2+ for its maximal activity and thermostability. At 35°C, the addition of 1 mM Mg2+ to the EDTA-treated enzyme increases the specific activity from 65 to 201 units/mg
Mg2+
-
the enzyme activity is increased nearly 1.8fold after addition of 0.8 mM Mg2+
Mg2+
-
Mg2+, Mn2+ or Co2+ required
Mn2+

activates and increase thermostability of the enzyme
Mn2+
1 mM required for activity
Mn2+
3fold increase in activity, assay in presence of 1 mM
Mn2+
-
best activator for enzymatic activity and thermostability. The enzyme activity is significantly increased by adding 1 mM Mn2+ (4.3fold)
Mn2+
0.5 mM, 270% of the activity of EDTA-treated enzyme
Mn2+
-
approximately 0.06 eqiuvalents of Mn2+/subunit
Mn2+
-
or Co2+, required. 497% of initial activity at 1 mM
Mn2+
required, 42% activation at 1 mM
Mn2+
1 mM, 111% of initial activity
Mn2+
-
restores activity after dialysis against EDTA
Mn2+
-
essential for catalysis, but also competitive inhibitor for L-arabinose
Mn2+
activates the enzyme; activates the enzyme; activates the enzyme
Mn2+
-
used in assay conditions
Mn2+
-
required for activity
Mn2+
presence of Mn2+ stabilizes protein 1.9- and 9fold at 60°C and 70°C, respectively
Mn2+
-
strong activator, approximately 0.06 eqiuvalents of Mn2+/subunit
Mn2+
increase in activity at 80°C only, no effect at 65°C
Mn2+
activating, highest activity of the wild type enzyme at 1.0 mM
Mn2+
is closely bound to the protein even after treatment with EDTA
Mn2+
-
404% relative activity at 1 mM, the enzyme has an absolute requirement for the divalent metal ion Mn2+ for both catalytic activity and thermostability
Mn2+
-
about 2fold increase in activity at 1 mM Mn2+
Mn2+
-
the enzyme is not metal-dependent for catalytic activity but Mn2+ significantly enhances the activity of its apo enzyme and increases thermostability
Mn2+
required to achieve maximum activity, competitive activator, increases thermal stability of AI, enhances galactose isomerization by 34%, maximum activity occurs at 5 mM Mn2+
Mn2+
-
activates the enzyme
Mn2+
298% activity at 1 mM, Mn2+ is required for enzymatic activity and thermostability
Mn2+
Lactobacillus gayonii
-
required, Km: 0.00525 mM
Mn2+
Lactobacillus gayonii
-
required
Mn2+
Lactobacillus gayonii
-
activates the enzyme
Mn2+
required for maximal activity and stability
Mn2+
-
the enzyme has low metal requirement of only 0.8 mM Mn2+ for its maximal activity and thermostability (above 35°C). At 35°C, the addition of 1 mM Mn2+ to the EDTA-treated enzyme increases the specific activity from 65 to 204 units/mg
Mn2+
-
the enzyme activity is increased nearly 1.8fold after addition of 0.8 mM Mn2+
Mn2+
-
Mn2+, Mg2+ or Co2+ required
Mn2+
activates 2.5fold at 1 mM
Mn2+
this enzyme exhibits a weak requirement for metall ions for its maximal activity evaluated at 0.6 mM Mn2+ and 0.8 mM Co2+ (115.38% activity in the presence of Mn2+ and Co2+)
Mn2+
1 mM, 3.4fold activation
Mn2+
-
restores activity after dialysis against EDTA
Mn2+
addition of MnCl2 reactivates the enzyme to 100% after inactivation with EDTA
Mn2+
-
highest activity with Mn2+. The optimum Mn2+ concentration for the free and calcium alginate-immobilized enzyme is 5 mM (132% activity)
Mn2+
0.1 mM Mn2+,increases activity to 167.3% and can improve both catalytic activity and thermostability at higher temperatures
Mn2+
-
Mn2+ or Co2+ required, about 5 mM Mn2+ restores activity of dialyzed enzyme
Mn2+
-
the enzyme is not metal-dependent for catalytic activity but Mn2+ significantly (3fold) enhances the activity of its apo enzyme and increases thermostability
Mn2+
-
divalent cation, maximal activity in presence of both Mn2+ and Co2+
Mn2+
-
1mM for the free enzyme, 10 mM for the immobilized enzyme in Escherichis coli cells
Ni2+

about 135% activity at 1 mM
Zn2+

-
307% of initial activity at 1 mM
Zn2+
129% activity at 1 mM
Zn2+
-
improves the enzymatic activity to 115% at 5 mM
additional information

metal ions are essential for catalytic activity, but metal ions, such as Mg2+, Ni2+, and Ba2+, are poor activators, while Fe2+, Ca2+, and Zn2+ have no effect on the activity
additional information
-
metal ions are essential for catalytic activity, but metal ions, such as Mg2+, Ni2+, and Ba2+, are poor activators, while Fe2+, Ca2+, and Zn2+ have no effect on the activity
additional information
-
the enzyme is not dependent on divalent metal ions, since it is only marginally activated by Mg2+, Mn2+ or Ca2+
additional information
the enzyme is not dependent on divalent metal ions, since it is only marginally activated by Mg2+, Mn2+ or Ca2+
additional information
-
the conversion of D-galactose into D-tagatose is not dependent on divalent metal ions
additional information
-
no stimulation by Ca2+, Ba2+, Fe2+, Hg2+, or Cu2+ at 1 mM each
additional information
-
the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM
additional information
the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM
additional information
-
the enzyme has very low requirement for metal ions for catalytic activity, but it is stabilized by divalent metal ions (Mg2+, Mn2+)
additional information
the enzyme has very low requirement for metal ions for catalytic activity, but it is stabilized by divalent metal ions (Mg2+, Mn2+)
additional information
-
activity and thermostability are totally independent of metallic ions up to 65°C, above 65°C, the enzyme's activity is also independent of metallic ions of its activity, but its thermostability is improved in the presence of only 0.2 mM Co2+ and 1 mM Mn2+; Ca2+, Ni2+, Zn2+, Mg2+, Fe2+, Cu2+ show no effect
additional information
activity and thermostability are totally independent of metallic ions up to 65°C, above 65°C, the enzyme's activity is also independent of metallic ions of its activity, but its thermostability is improved in the presence of only 0.2 mM Co2+ and 1 mM Mn2+; Ca2+, Ni2+, Zn2+, Mg2+, Fe2+, Cu2+ show no effect
additional information
-
not significantly stimulated by Mg2+
additional information
-
the enzyme has no activity in the absence of metal ions
additional information
the enzyme has no activity in the absence of metal ions
additional information
not influenced by Ca2+ and Ni2+
additional information
-
the enzyme is not affected by Zn2+, Ca2+, Co2+, Fe2+, and Ba2+
additional information
-
not influenced by Mg2+ and Ca2+
additional information
not influenced by Mg2+ and Ca2+
additional information
-
not activated by Mg2+, Fe2+, and Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Li+
about 90% residual activity at 1 mM
Na+
about 90% residual activity at 1 mM
Ba2+

-
6% residual activity at 1 mM
Ba2+
33.08% residual activity at 1 mM
Ca2+

-
complete inhibition at 1 mM
Ca2+
33.61% residual activity at 1 mM
Co2+

about 85% residual activity at 1 mM
Co2+
82% residual activity at 10 mM
Co2+
moderate inhibitory effect at 1 mM
Co2+
58% of the activity with Mn2+
Co2+
-
90% residual activity at 1 mM
Co2+
strong inhibition at 1 mM
Cu2+

30% inhibition at 1 mM
Cu2+
about 25% residual activity at 1 mM
Cu2+
-
about 5% residual activity at 1 mM Mg2+
Cu2+
-
significant inhibition
Cu2+
-
53% residual activity at 1 mM
Cu2+
20% residual activity at 1 mM
Cu2+
Lactobacillus gayonii
-
-
Cu2+
-
about 30% residual activity at 1 mM
Cu2+
3.31% residual activity at 1 mM
Cu2+
-
23% residual activity at 1 mM
Dulcitol

weak inhibitor
Dulcitol
remaining activity 72.9%
Dulcitol
90% residual activity at 10 mM
EDTA

1 mM inhibits activity completely
EDTA
60% loss of activity
EDTA
30% inhibition at 1 mM
EDTA
1 mM, complete loss of activity
EDTA
1 mM, 25% of the activity in presence of 1 mM Mn2+
EDTA
-
22% residual activity at 1 mM
EDTA
complete inhibition at 1 mM
EDTA
-
54% inhibition at 1 mM EDTA assayed at 35°C
EDTA
complete inhibition at 1 mM
erythritol

weak inhibitor
erythritol
remaining activity 50.0%
erythritol
weak inhibitor
erythritol
42% residual activity at 10 mM
Fe2+

strong inhibitory effect, over 70% of the activity is lost already at 0.5 mM Fe2+
Fe2+
Lactobacillus gayonii
-
-
Fe2+
strong inhibition at 1 mM
Fe3+

about 35% residual activity at 1 mM
Fe3+
strong inhibitory effect, over 70% of the activity is lost already at 0.5 mM Fe3+
Fe3+
27.52% residual activity at 1 mM
Hg2+

-
significant inhibition
Hg2+
Lactobacillus gayonii
-
-
L-arabitol

-
competitive inhibitor
L-arabitol
strong inhibitory
L-arabitol
remaining activity 11.2%
L-arabitol
Lactobacillus gayonii
-
-
L-arabitol
strong inhibitor
L-arabitol
11% residual activity at 10 mM
Mg2+

about 90% residual activity at 1 mM
Mg2+
-
about 80% residual activity at 1 mM Mg2+
Mg2+
-
90% residual activity at 1 mM
Mg2+
45.12% residual activity at 1 mM
Mn2+

about 70% residual activity at 1 mM
Mn2+
moderate inhibitory effect at 1 mM
Mn2+
-
essential for catalysis, but also competitive inhibitor for L-arabinose
Mn2+
31.14% residual activity at 1 mM; 60.81% residual activity at 1 mM
Ni2+

70% residual activity at 10 mM
Ni2+
-
about 60% residual activity at 1 mM Mg2+
Ni2+
39.71% residual activity at 1 mM
Ni2+
-
85% residual activity at 1 mM
ribitol

-
-
ribitol
strong inhibitory
ribitol
strongest competitive inhibitor, no detectable activity left
ribitol
Lactobacillus gayonii
-
-
ribitol
22% residual activity at 10 mM
xylitol

weak inhibitor
xylitol
remaining activity 50.0%
xylitol
Lactobacillus gayonii
-
-
xylitol
46% residual activity at 10 mM
Zn2+

about 65% residual activity at 1 mM
Zn2+
-
about 10% residual activity at 1 mM Mg2+
Zn2+
-
61% residual activity at 1 mM
Zn2+
Lactobacillus gayonii
-
-
Zn2+
strong inhibition at 1 mM
Zn2+
12.89% residual activity at 1 mM
additional information

-
no activity loss is observed after treatment with EDTA for 12 h
-
additional information
no activity loss is observed after treatment with EDTA for 12 h
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
173.6
L-fucose
F279Q mutant
1.328
D-galactose

mutant F280N/C450S/N475K, pH 8, 55°C
3 - 5
D-galactose
-
at pH 7.0 and 50°C
7.7
D-galactose
pH 7.5, 35°C
25.19
D-galactose
without borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
26.81
D-galactose
with 10 mM borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
41.4
D-galactose
mutant D478Q, pH 7.0, 65°C
45
D-galactose
N475K mutant
46
D-galactose
mutant enzyme D268K/D269K/D299K, at pH 5.0 and 65°C
51
D-galactose
mutant enzyme D268K/D269K/D299K, at pH 4.0 and 65°C
54.7
D-galactose
wild-type, pH 7.0, 65°C
55
D-galactose
mutant enzyme D269K/D299K, at pH 5.0 and 65°C
56
D-galactose
mutant enzyme D268K/D269K/D299K, at pH 6.0 and 65°C; mutant enzyme D269K/D299K, at pH 6.0 and 65°C
59
D-galactose
-
with 0.8 mM MgCl2 and 0.8 mM MnCl2, in 100 mM sodium acetate buffer (pH 5.0), at 35°C
60
D-galactose
-
pH 7.5, 90°C
60.2
D-galactose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C
60.7
D-galactose
mutant D478R, pH 7.0, 65°C
61
D-galactose
mutant enzyme D269K/D299K, at pH 4.0 and 65°C
63
D-galactose
wild type enzyme, at pH 6.0 and 65°C
66
D-galactose
at 50°C and pH 6.0
66
D-galactose
mutant D478N, pH 7.0, 65°C
67
D-galactose
C450S mutant
71
D-galactose
-
at pH 7.0 and 40°C
74
D-galactose
mutant enzyme D299K, at pH 5.0 and 65°C
75
D-galactose
C450S /N475K mutant
75.4
D-galactose
mutant D478K, pH 7.0, 65°C
78
D-galactose
mutant enzyme D299K, at pH 6.0 and 65°C
82
D-galactose
mutant enzyme D299R, at pH 5.0 and 65°C
83.2
D-galactose
mutant D478A, pH 7.0, 65°C
84
D-galactose
mutant enzyme D299K, at pH 4.0 and 65°C; mutant enzyme D299R, at pH 6.0 and 65°C
86.1
D-galactose
pH 7.5, 22°C
90
D-galactose
K428N mutant
93
D-galactose
mutant enzyme D299R, at pH 4.0 and 65°C
94
D-galactose
mutant enzyme D268K, at pH 6.0 and 65°C; mutant enzyme D269K, at pH 6.0 and 65°C
96
D-galactose
mutant enzyme D269K, at pH 5.0 and 65°C
97
D-galactose
V408A mutant
101
D-galactose
Y164F mutant
101
D-galactose
-
at pH 7.0 and 30°C
103
D-galactose
K320R/N475K mutant
105
D-galactose
N475Q mutant
108
D-galactose
mutant enzyme D269K, at pH 4.0 and 65°C
116
D-galactose
wild type enzyme, at pH 5.0 and 65°C
117
D-galactose
mutant enzyme D268K/D269K, at pH 5.0 and 65°C
119
D-galactose
at pH 7.0 and 50°C
122
D-galactose
in 25 mM Tris-HCl buffer (pH 7.5), at 60°C
125
D-galactose
mutant enzyme D268K, at pH 5.0 and 65°C
129
D-galactose
wild-type at pH 6 and 65°C
129
D-galactose
mutant enzyme D268K/D269K, at pH 6.0 and 65°C
130
D-galactose
Y164H mutant
137
D-galactose
mutant enzyme D268K/D269K, at pH 4.0 and 65°C
144
D-galactose
wild type
145
D-galactose
wild type enzyme
148
D-galactose
K320R mutant
149
D-galactose
K428N /N475K mutant
161
D-galactose
N228D mutant
166
D-galactose
mutant enzyme D268K, at pH 4.0 and 65°C
173
D-galactose
N475R mutant
175
D-galactose
at pH 7.0 and 40°C
201
D-galactose
S393T mutant
201
D-galactose
mutant enzyme D268K/D299K, at pH 6.0 and 65°C
227
D-galactose
in the presence of 10 mM Mn2+, enzyme treated with EDTA
246
D-galactose
mutant enzyme D268K/D299K, at pH 5.0 and 65°C
250
D-galactose
-
pH 7.0, 85°C
252
D-galactose
N-His-tagged recombinant protein, Michaelis-Menten kinetics, pH 5.6, 50°C
256
D-galactose
-
pH 7.0, 37°C, whole cells
257
D-galactose
V408A /N475K mutant
279
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis
280
D-galactose
M322V mutant
287
D-galactose
mutant enzyme D268K/D299K, at pH 4.0 and 65°C
339
D-galactose
mutant C450S/N475K, pH 8, 55°C
355.1
D-galactose
pH 7.5, 60°C
365
D-galactose
-
pH 7.0, 37°C, purified enzyme
426
D-galactose
C-His-tagged recombinant protein, K0.5 value, cooperative interaction model, pH 5.6, 50°C
578
D-galactose
mutated enzyme
578
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
590
D-galactose
at pH 6.5 and 45°C
713
D-galactose
G384D mutant
1105
D-galactose
W164G mutant; Y164G mutant
2564
D-galactose
in the presence of 1 mM Mn2+, enzyme treated with EDTA
11
D-tagatose

-
pH 7.0, 37°C, purified enzyme
114
D-tagatose
-
pH 7.0, 37°C, whole cells
5.2
L-arabinose

-
in the presence of 0.8 mM Mn2+, at pH 7.5 and 60°C
8 - 16
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333V
10.4
L-arabinose
-
in the presence of 0.6 mM Mn2+, at pH 7.5 and 60°C
11
L-arabinose
-
in the presence of 0.2 mM Mn2+, at pH 7.5 and 60°C
11.3
L-arabinose
pH 7.5, 22°C
15
L-arabinose
M322V mutant
15.4
L-arabinose
-
in the presence of 0.4 mM Mn2+, at pH 7.5 and 60°C
18.6
L-arabinose
-
in the presence of 0.8 mM Mn2+, at pH 7.5 and 60°C
22.6
L-arabinose
-
in the presence of 0.6 mM Mn2+, at pH 7.5 and 60°C
25.8
L-arabinose
-
in the presence of 0.1 mM Mn2+, at pH 7.5 and 60°C
27
L-arabinose
-
D-galactose induced enzyme
28
L-arabinose
-
in the presence of 0.4 mM Mn2+, at pH 7.5 and 60°C
28.42
L-arabinose
wild type
29.3
L-arabinose
D308A mutant
29.9
L-arabinose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C
30.1
L-arabinose
E351A mutant
30.4
L-arabinose
H446A mutant
30.6
L-arabinose
F329A mutant
31
L-arabinose
-
pH 7.5, 90°C
31.6
L-arabinose
-
with 0.8 mM MgCl2 and 0.8 mM MnCl2, in 100 mM sodium acetate buffer (pH 5.0), at 35°C
33.3
L-arabinose
-
L-arabinose induced enzyme
34.2
L-arabinose
mutant D478A, pH 7.0, 65°C
36
L-arabinose
W164G mutant; Y164G mutant
38.2
L-arabinose
-
wild-type at pH 6 and 50°C
39
L-arabinose
-
in the presence of 0.2 mM Mn2+, at pH 7.5 and 60°C
39.7
L-arabinose
-
wild-type at pH 7 and 50°C
42
L-arabinose
-
at pH 7.0 and 50°C
42.7
L-arabinose
-
mutant enzyme D118V, at pH 7.5 and 70°C
43.4
L-arabinose
at 60°C, pH 7.5
43.7
L-arabinose
-
mutant E268K at pH 7 and 50°C
43.8
L-arabinose
-
wild-type at pH 8 and 50°C
46
L-arabinose
-
mutant E268K at pH 8 and 50°C
46.2
L-arabinose
wild-type at pH 7 and 65°C
47.5
L-arabinose
wild-type at pH 8 and 65°C
48
L-arabinose
wild-type at pH 6 and 65°C
51
L-arabinose
C450S mutant
52.5
L-arabinose
mutant K269E at pH 8 and 65°C
53.8
L-arabinose
mutant K269E at pH 7 and 65°C
55
L-arabinose
Lactobacillus gayonii
-
-
55
L-arabinose
mutant D478K, pH 7.0, 65°C
56
L-arabinose
K320R mutant
56
L-arabinose
mutant D478R, pH 7.0, 65°C
56.1
L-arabinose
-
mutant E268K at pH 6 and 50°C
56.3
L-arabinose
mutant D478N, pH 7.0, 65°C
57.9
L-arabinose
mutant K269E at pH 6 and 65°C
57.9
L-arabinose
-
wild type enzyme, at pH 7.5 and 70°C
58
L-arabinose
K320R/N475K mutant
59
L-arabinose
K428N mutant
61
L-arabinose
-
in the presence of 0.1 mM Mn2+, at pH 7.5 and 60°C
66
L-arabinose
V408A /N475K mutant
67
L-arabinose
wild type enzyme
69
L-arabinose
N475K mutant
71
L-arabinose
C450S /N475K mutant
76
L-arabinose
V408A mutant
77
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis
78.5
L-arabinose
in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
79.7
L-arabinose
F279Q mutant
80
L-arabinose
-
mutant enzyme N460L, at pH 7.5 and 70°C
82
L-arabinose
N475R mutant
90
L-arabinose
Y164H mutant
94
L-arabinose
N475Q mutant
94.2
L-arabinose
mutant D478Q, pH 7.0, 65°C
97
L-arabinose
wild type; Y164F mutant
100
L-arabinose
mutated enzyme
100
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
100
L-arabinose
-
mutant enzyme D333V, at pH 7.5 and 70°C
105.2
L-arabinose
wild-type, pH 7.0, 65°C
106
L-arabinose
-
at pH 7.0 and 70°C
106
L-arabinose
mutant C450S/N475K, pH 8, 55°C
111.7
L-arabinose
pH 7.0, 40°C
116
L-arabinose
-
pH 7.0, 85°C
119.3
L-arabinose
-
mutant enzyme D195V, at pH 7.5 and 70°C
120
L-arabinose
at pH 6.5 and 45°C
123
L-arabinose
N228D mutant
147.1
L-arabinose
-
mutant enzyme E261L, at pH 7.5 and 70°C
163
L-arabinose
G384D mutant
168
L-arabinose
K428N /N475K mutant
188
L-arabinose
S393T mutant
269.8
L-arabinose
pH 7.5, 60°C
334
L-arabinose
mutant F280N/C450S/N475K, pH 8, 55°C
352
L-arabinose
-
immobilized enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C
369
L-arabinose
-
pH 7.5, 50°C
369
L-arabinose
pH 7.5, 50°C, recombinant wild-type enzyme
369
L-arabinose
-
pH 7.5, 50°C, free recombinant enzyme
369
L-arabinose
-
free enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C
492
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333F
620
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333W
750
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333I
770
L-arabinose
-
pH 7.5, 50°C, immobilized recombinant enzyme
5
L-ribulose

Lactobacillus gayonii
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
241.7
L-aldose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
241.7
L-ribulose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
0.98
D-galactose

mutant D478Q, pH 7.0, 65°C
1.02
D-galactose
-
pH 7.0, 37°C, purified enzyme
1.13
D-galactose
wild-type, pH 7.0, 65°C
1.26
D-galactose
mutant D478R, pH 7.0, 65°C
1.36
D-galactose
mutant D478K, pH 7.0, 65°C
1.58
D-galactose
mutant D478A, pH 7.0, 65°C
1.65
D-galactose
mutant D478N, pH 7.0, 65°C
2.2
D-galactose
without borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
4.21
D-galactose
-
pH 7.0, 37°C, whole cells
4.9
D-galactose
in 25 mM Tris-HCl buffer (pH 7.5), at 60°C
17.4
D-galactose
mutant C450S/N475K, pH 8, 55°C
20.18
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
28.4
D-galactose
pH 7.5, 35°C
53.08
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis
78.5
D-galactose
with 10 mM borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
104.1
D-galactose
mutant F280N/C450S/N475K, pH 8, 55°C
0.06
D-tagatose

-
pH 7.0, 37°C, purified enzyme
0.82
D-tagatose
-
pH 7.0, 37°C, whole cells
0.9
L-arabinose

in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
11.2
L-arabinose
-
mutant enzyme E261L, at pH 7.5 and 70°C
11.9
L-arabinose
-
mutant enzyme D118V, at pH 7.5 and 70°C
12.8
L-arabinose
mutant F280N/C450S/N475K, pH 8, 55°C
12.9
L-arabinose
pH 7.0, 40°C
14.2
L-arabinose
-
mutant enzyme D195V, at pH 7.5 and 70°C
14.9
L-arabinose
-
mutant enzyme D333V, at pH 7.5 and 70°C
15.88
L-arabinose
-
wild-type at pH 6 and 50°C
19.62
L-arabinose
mutant K269E at pH 6 and 65°C
23.65
L-arabinose
-
wild-type at pH 7 and 50°C
24.11
L-arabinose
-
mutant E268K at pH 6 and 50°C
24.97
L-arabinose
wild-type at pH 8 and 65°C
25.8
L-arabinose
mutant K269E at pH 8 and 65°C
27.8
L-arabinose
-
mutant enzyme N460L, at pH 7.5 and 70°C
28.55
L-arabinose
wild-type at pH 7 and 65°C
29.63
L-arabinose
-
mutant E268K at pH 8 and 50°C
31.03
L-arabinose
-
wild-type at pH 8 and 50°C
32.93
L-arabinose
-
mutant E268K at pH 7 and 50°C
33.15
L-arabinose
wild-type at pH 6 and 65°C
33.8
L-arabinose
-
wild type enzyme, at pH 7.5 and 70°C
37.2
L-arabinose
mutant K269E at pH 7 and 65°C
38.9
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333V
50.3
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333I
71.8
L-arabinose
wild-type, pH 7.0, 65°C
72.9
L-arabinose
mutant D478R, pH 7.0, 65°C
75.25
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis
85
L-arabinose
mutant D478A, pH 7.0, 65°C
99.6
L-arabinose
mutant D478K, pH 7.0, 65°C
105
L-arabinose
mutant D478Q, pH 7.0, 65°C
107.9
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
110
L-arabinose
mutant D478N, pH 7.0, 65°C
148.8
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333W
188.2
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333F
207
L-arabinose
-
pH 7.5, 50°C
207.5
L-arabinose
pH 7.5, 50°C, recombinant wild-type enzyme
207.6
L-arabinose
pH and temperature not specified in the publication
240.6
L-arabinose
mutant C450S/N475K, pH 8, 55°C
3657
L-arabinose
-
at pH 7.0 and 70°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0023 - 0.173
D-galactose
2.02
L-aldose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
2.02
L-ribulose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
0.0023
D-galactose

at pH 7.0 and 50°C
0.012
D-galactose
at pH 6.5 and 45°C
0.017
D-galactose
pH 7.5, 60°C
0.018
D-galactose
mutant D478K, pH 7.0, 65°C
0.019
D-galactose
mutant D478A, pH 7.0, 65°C
0.02
D-galactose
wild type enzyme, at pH 5.0 and 65°C
0.02
D-galactose
wild-type, pH 7.0, 65°C
0.021
D-galactose
mutant D478R, pH 7.0, 65°C
0.024
D-galactose
mutant D478Q, pH 7.0, 65°C
0.025
D-galactose
mutant D478N, pH 7.0, 65°C
0.035
D-galactose
mutant enzyme D268K/D299K, at pH 4.0 and 65°C
0.04
D-galactose
in 25 mM Tris-HCl buffer (pH 7.5), at 60°C
0.047
D-galactose
at pH 7.0 and 40°C
0.048
D-galactose
at 50°C and pH 6.0
0.05
D-galactose
mutant enzyme D268K, at pH 6.0 and 65°C
0.05
D-galactose
mutant C450S/N475K, pH 8, 55°C
0.055
D-galactose
mutant enzyme D268K/D299K, at pH 5.0 and 65°C
0.057
D-galactose
mutant enzyme D268K/D269K, at pH 4.0 and 65°C
0.065
D-galactose
mutant enzyme D268K/D299K, at pH 6.0 and 65°C
0.067
D-galactose
mutant enzyme D268K/D269K, at pH 6.0 and 65°C
0.07
D-galactose
mutant enzyme D268K, at pH 4.0 and 65°C
0.078
D-galactose
mutant enzyme D268K/D269K, at pH 5.0 and 65°C
0.08
D-galactose
mutant F280N/C450S/N475K, pH 8, 55°C
0.09
D-galactose
without borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
0.09
D-galactose
mutant enzyme D268K, at pH 5.0 and 65°C
0.1
D-galactose
mutant enzyme D299K, at pH 4.0 and 65°C
0.103
D-galactose
mutant enzyme D299K, at pH 6.0 and 65°C
0.105
D-galactose
mutant enzyme D269K, at pH 4.0 and 65°C
0.108
D-galactose
mutant enzyme D268K/D269K/D299K, at pH 4.0 and 65°C; mutant enzyme D299R, at pH 4.0 and 65°C
0.113
D-galactose
mutant enzyme D268K/D269K/D299K, at pH 6.0 and 65°C; mutant enzyme D299K, at pH 5.0 and 65°C
0.117
D-galactose
mutant enzyme D269K/D299K, at pH 4.0 and 65°C
0.118
D-galactose
mutant enzyme D299R, at pH 5.0 and 65°C
0.12
D-galactose
mutant enzyme D268K/D269K/D299K, at pH 5.0 and 65°C
0.127
D-galactose
mutant enzyme D299R, at pH 6.0 and 65°C
0.13
D-galactose
wild type enzyme, at pH 6.0 and 65°C
0.135
D-galactose
mutant enzyme D269K/D299K, at pH 6.0 and 65°C
0.15
D-galactose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C
0.152
D-galactose
mutant enzyme D269K/D299K, at pH 5.0 and 65°C
0.16
D-galactose
with 10 mM borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
0.165
D-galactose
mutant enzyme D269K, at pH 5.0 and 65°C
0.17
D-galactose
-
with 0.8 mM MgCl2 and 0.8 mM MnCl2, in 100 mM sodium acetate buffer (pH 5.0), at 35°C
0.173
D-galactose
mutant enzyme D269K, at pH 6.0 and 65°C
0.01
L-arabinose

in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
0.04
L-arabinose
mutant F280N/C450S/N475K, pH 8, 55°C
0.048
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333V
0.067
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333I
0.08
L-arabinose
-
mutant enzyme E261L, at pH 7.5 and 70°C
0.11
L-arabinose
pH 7.0, 40°C
0.12
L-arabinose
-
mutant enzyme D195V, at pH 7.5 and 70°C
0.145
L-arabinose
pH 7.5, 60°C
0.15
L-arabinose
-
mutant enzyme D333V, at pH 7.5 and 70°C
0.24
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333W
0.28
L-arabinose
-
mutant enzyme D118V, at pH 7.5 and 70°C
0.32
L-arabinose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C
0.35
L-arabinose
-
mutant enzyme N460L, at pH 7.5 and 70°C
0.38
L-arabinose
pH 7.5, 50°C, recombinant mutant Y333F
0.56
L-arabinose
pH 7.5, 50°C, recombinant wild-type enzyme
0.57
L-arabinose
pH and temperature not specified in the publication
0.575
L-arabinose
-
at pH 7.0 and 70°C
0.58
L-arabinose
-
wild type enzyme, at pH 7.5 and 70°C
0.68
L-arabinose
wild-type, pH 7.0, 65°C
0.8
L-arabinose
at pH 6.5 and 45°C
1.08
L-arabinose
-
with 0.8 mM MgCl2 and 0.8 mM MnCl2, in 100 mM sodium acetate buffer (pH 5.0), at 35°C
1.12
L-arabinose
mutant D478Q, pH 7.0, 65°C
1.3
L-arabinose
mutant D478R, pH 7.0, 65°C
1.81
L-arabinose
mutant D478K, pH 7.0, 65°C
1.95
L-arabinose
mutant D478N, pH 7.0, 65°C
2.27
L-arabinose
mutant C450S/N475K, pH 8, 55°C
2.48
L-arabinose
mutant D478A, pH 7.0, 65°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.004
D228N mutant, D-galactose as substrate
0.026
cell extract, at pH 7.5 and 52°C
0.029
R408V mutant, D-galactose as substrate
0.043
wild type, D-galactose as substrate
0.05
L408V mutant, D-galactose as substrate
0.055
recovered activity after immobilization of the enzyme
0.06
Q408V mutant, at pH 7.5, D-galactose as substrate; R408V mutant, at pH 7.5, D-galactose as substrate
0.062
Q408V mutant, D-galactose as substrate
0.103
activity determined from the cell extracts of Escherichia coli UP1110 3 h after the onset of IPTG induction
0.11
T393S mutant, D-galactose as substrate
0.122
after ammonium sulfate precipitation
0.14
wild type, D-galactose as substrate
0.163
after heat treatment
0.183
activity determined from the cell extracts of Lactobacillus plantarum BPT232 1h after the induction with the peptide SPPIP
0.232
after 8.9fold purification, at pH 7.5 and 52°C
0.25
-
cell-free extract, at pH 7.0 and 50°C
0.26
N428K mutant, D-galactose as substrate
0.27
V322M mutant, D-galactose as substrate
0.33
substrate D-galactose, mutant D478R, pH 7.0, 65°C
0.37
G408V mutant, D-galactose as substrate; Q475N mutant, D-galactose as substrate
0.38
R475N mutant, D-galactose as substrate
0.39
K475N mutant, D-galactose as substrate; K475N mutant found in GSAI152, D-galactose as substrate
0.44
substrate D-galactose, pH 7.5, 35°C
0.48
A408V mutant, D-galactose as substrate; A475N mutant found in GSAI153, D-galactose as substrate
0.49
GSAI1 152, D-galactose as substrate
0.52
substrate D-galactose, wild-type, pH 7.0, 65°C
0.59
A408V/K475N mutant found in GSAI152 or GASI 153w D-galactose as substrate
0.73
substrate D-galactose, mutant D478A, pH 7.0, 65°C
0.74
GSAI1 153, D-galactose as substrate
0.75
substrate D-galactose, mutant D478N, pH 7.0, 65°C
0.76
substrate D-galactose, mutant D478K, pH 7.0, 65°C
0.81
substrate D-galactose, mutant D478Q, pH 7.0, 65°C
0.84
-
in the absence of Mn2+, at pH 7.5 and 60°C
0.9
-
purified enzyme, in the absence of Mn2+, at pH 7.5 and 60°C
1
after Hi-trap Q ion exchange chromatography
1 - 2
mutant enzyme D299E, at pH 7.0 and 65°C
1.1
substrate D-galactose, pH 7.5, 60°C
1.3
-
with D-galactose as substrate