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Information on EC 5.3.1.4 - L-arabinose isomerase
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5.3.1.4 L-arabinose isomeraseIUBMB Comments
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+) . The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism . The enzyme can also convert D-galactose to D-tagatose with lower efficiency .
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Word Map
- 5.3.1.4
- d-tagatose
-
isomerization
- l-ribulose
- nutrition
- geobacillus
- isomerases
-
sweetener
- stearothermophilus
- synthesis
- food industry
- l-ribulokinase
- thermodenitrificans
-
low-calorie
-
arabad
- sakei
-
4-epimerase
-
packed-bed
- industry
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
AI, AraA, arabinose isomerase, D-galactose isomerase, ECAI, gali 152, gali 153, GSAI, GSAI 152, GSAI 153, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AI
AraA
D-galactose isomerase
gali 152
GSAI
Geobacillus stearothermophilus L-arabinose isomease
Isomerase, L-arabinose
-
-
-
-
L-AI
L-AI NC8
L-arabinose aldose-ketose-isomerase
L-arabinose isomerase
L-arabinose ketol-isomerase
-
-
-
-
pL151
gali 152
mutated L-arabinose isomerase from pL152 gene
-
L-arabinose aldose-ketose-isomerase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-Arabinose = L-ribulose
-
-
-
-
L-Arabinose = L-ribulose
compulsory ordered mechanism that involves the formation of a ternary complex of enzyme-Mn-substrate
Lactobacillus gayonii
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
isomerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-arabinose aldose-ketose-isomerase
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+) [2]. The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [5]. The enzyme can also convert D-galactose to D-tagatose with lower efficiency [4].
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CAS REGISTRY NUMBER
COMMENTARY
9023-80-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-Xylose
D-Xylulose
7.0%, relative activity compared to activity with 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
?
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
-
at elevated temperatures, not dependent on divalent metal ions
-
-
?
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
-
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
-
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
-
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
Limosilactobacillus fermentum CGMCC2921
100% activity, conversion rate of 55% with 1mM Mn2+ after 12 h at 65°C
-
-
?
D-galactose
D-tagatose
Limosilactobacillus fermentum CGMCC2921
-
39% conversion after 48 h at pH 6.0 and 65°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
-
-
43.9% yield with immobilized enzyme
-
?
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-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
?
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
L-Ribulose
40% activity compared to D-galactose
-
-
?
L-Arabinose
L-Ribulose
40% activity compared to D-galactose
-
-
?
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 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
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
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
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
-
-
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
high preference for L-arabinose (220% compared to D-galactose)
-
-
r
L-Arabinose
L-Ribulose
Limosilactobacillus fermentum CGMCC2921
high preference for L-arabinose (220% compared to D-galactose)
-
-
r
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
-
70% conversion to L-ribulose in 6 h at 80°C
-
?
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
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-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
?
-
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
?
-
Limosilactobacillus fermentum CGMCC2921
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 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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fucose
D-fuculose
221% activity compared to D-galactose
-
-
r
D-galactose
D-tagatose
-
at elevated temperatures, not dependent on divalent metal ions
-
-
?
D-galactose
D-tagatose
-
at elevated temperatures in the presence of divalent metal ions
-
-
?
D-galactose
D-tagatose
-
-
-
?
L-Arabinose
L-Ribulose
the enzyme has a high preference only for L-arabinose
-
-
?
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
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
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
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
-
-
33% conversion yield within 720 h at pH 7.5 and 60°C
-
?
L-Arabinose
L-Ribulose
244% activity compared to D-galactose
-
-
r
L-Arabinose
L-Ribulose
244% activity compared to D-galactose
-
-
r
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
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
?
-
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)
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ba2+
inhibits galactose isomerization, remaining activity 94%
Ca2+
the addition of Ca2+ has slightly positive but no significant effect on the enzyme activity
Ca2+
-
the most effective enzyme activator with the reaction rate by 150%
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+
activating, highest activity of the mutated enzyme at 1.0 mM
Co2+
increase in activity at 80°C only, no effect at 65°C
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+
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+
addition of CoSO4 reactivates the enzyme to 45% after inactivation with EDTA
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+
-
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+
inhibits galactose isomerization remaining activity 42%
Fe2+
inhibits galactose isomerization remaining activity 98%
Fe2+
addition of FeSO4 reactivates the enzyme to 76% after inactivation with EDTA
Mg2+
the addition of Mg2+ has slightly positive but no significant effect on the enzyme activity
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+
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+
-
essential for catalysis, but also competitive inhibitor for L-arabinose
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+
activating, highest activity of the wild type enzyme at 1.0 mM
Mn2+
increase in activity at 80°C only, no effect at 65°C
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+
-
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+
-
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+
298% activity at 1 mM, Mn2+ is required for enzymatic activity and thermostability
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+
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
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 conversion of D-galactose into D-tagatose is not dependent on divalent metal ions
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
-
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+
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+
additional information
-
Ca2+, Ni2+, Zn2+, Mg2+, Fe2+, Cu2+ show no effect
additional information
Ca2+, Ni2+, Zn2+, Mg2+, Fe2+, Cu2+ show no effect
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
-
the enzyme is not affected by Zn2+, Ca2+, Co2+, Fe2+, and Ba2+
additional information
not influenced by Mg2+ and Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe2+
strong inhibitory effect, over 70% of the activity is lost already at 0.5 mM Fe2+
Fe3+
strong inhibitory effect, over 70% of the activity is lost already at 0.5 mM Fe3+
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
ribitol
strongest competitive inhibitor, no detectable activity left
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Borate
the catalytic efficiency (kcat/Km) for D-galactose with borate is twice as much as that without borate
Borate
-
borate addition (1 mM) to the reaction mixture is essential for high conversion of L-arabinose to L-ribulose as it results in an equilibrium shift in favor of the product
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.328
D-galactose
mutant F280N/C450S/N475K, pH 8, 55°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
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
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
56
D-galactose
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
60.2
D-galactose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C
61
D-galactose
mutant enzyme D269K/D299K, at pH 4.0 and 65°C
117
D-galactose
mutant enzyme D268K/D269K, at pH 5.0 and 65°C
122
D-galactose
in 25 mM Tris-HCl buffer (pH 7.5), at 60°C
129
D-galactose
mutant enzyme D268K/D269K, at pH 6.0 and 65°C
137
D-galactose
mutant enzyme D268K/D269K, at pH 4.0 and 65°C
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
252
D-galactose
N-His-tagged recombinant protein, Michaelis-Menten kinetics, pH 5.6, 50°C
279
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis
287
D-galactose
mutant enzyme D268K/D299K, at pH 4.0 and 65°C
426
D-galactose
C-His-tagged recombinant protein, K0.5 value, cooperative interaction model, pH 5.6, 50°C
578
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
2564
D-galactose
in the presence of 1 mM Mn2+, enzyme treated with EDTA
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
28
L-arabinose
-
in the presence of 0.4 mM Mn2+, at pH 7.5 and 60°C
29.9
L-arabinose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°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
39
L-arabinose
-
in the presence of 0.2 mM Mn2+, at pH 7.5 and 60°C
61
L-arabinose
-
in the presence of 0.1 mM Mn2+, at pH 7.5 and 60°C
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
100
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
352
L-arabinose
-
immobilized enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C
369
L-arabinose
-
free enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
2.2
D-galactose
without borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
4.9
D-galactose
in 25 mM Tris-HCl buffer (pH 7.5), at 60°C
20.18
D-galactose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
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
0.9
L-arabinose
in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C
75.25
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis
107.9
L-arabinose
pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli
207.6
L-arabinose
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.035
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
0.05
D-galactose
mutant enzyme D268K, at pH 6.0 and 65°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
0.09
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
0.103
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
0.108
D-galactose
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
0.113
D-galactose
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
0.135
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
0.32
L-arabinose
in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C
0.57
L-arabinose
pH and temperature not specified in the publication
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.055
recovered activity after immobilization of the enzyme
0.056
0.06
0.103
activity determined from the cell extracts of Escherichia coli UP1110 3 h after the onset of IPTG induction