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D-allose
D-psicose + D-altrose
-
-
-
-
?
D-allose
D-talose
-
-
-
-
?
D-allulose
D-psicose
best ketose substrate
-
-
r
D-altrose
D-psicose + D-altrose
-
-
-
-
r
D-arabinose
D-ribulose + D-ribose
-
-
-
-
r
D-erythrose
D-erythrulose + D-threose
-
-
-
-
r
D-Galactose
?
-
slight activity
-
-
?
D-galactose
D-tagatose
-
-
-
-
r
D-glucose
D-fructose + D-mannose
-
-
-
-
r
D-Gulose
?
-
10% of the activity relative to L-rhamnose
-
-
?
D-Lyxose
?
-
slight activity
-
-
?
D-lyxose
D-xylulose + D-xylose
-
-
-
-
r
D-ribose
D-ribulose + D-arabinose
-
-
-
-
r
D-ribulose
D-ribose
-
-
-
r
D-talose
?
-
slight activity
-
-
?
D-talose
D-allose
-
slight activity
-
-
?
D-threose
D-erythrulose + D-erythrose
-
-
-
-
r
D-xylose
D-xylulose + D-lyxose
-
-
-
-
r
L-Arabinose
?
-
slight activity
-
-
?
L-arabinose
L-ribulose
-
-
-
-
r
L-erythrose
L-erythrulose + L-threose
-
-
-
-
r
L-galactose
?
-
slight activity
-
-
?
L-galactose
L-tagatose + L-talose
-
-
-
-
r
L-glucose
L-fructose + L-mannose
-
-
-
-
r
L-lyxose
L-xylulose + L-xylose
-
-
-
-
r
L-mannose
L-fructose + L-glucose
-
-
-
-
r
L-rhamnulose
L-rhamnulose
-
-
-
-
r
L-ribose
?
-
slight activity
-
-
?
L-ribose
L-ribulose + L-arabinose
-
-
-
-
r
L-tagatose
L-talose
10% conversion at 50°C
-
-
r
L-threose
L-erythrulose + L-erythrose
-
-
-
-
r
L-xylose
L-xylulose + L-lyxose
-
-
-
-
r
additional information
?
-
3-Deoxy-L-rhamnose
?
-
-
-
-
?
3-Deoxy-L-rhamnose
?
-
0.6% of the activity with L-rhamnose
-
-
?
D-Allose
?
-
-
-
-
?
D-allose
D-psicose
35% conversion at 50°C
-
-
r
D-allose
D-psicose
-
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
?
D-allose
D-psicose
-
-
-
?
D-allose
D-psicose
-
-
-
?
D-allose
D-psicose
-
-
-
?
D-allose
D-psicose
-
10% of the activity relative to L-rhamnose
-
-
?
D-allose
D-psicose
-
only reverse reaction described
-
?
D-allose
D-psicose
-
only reverse reaction described
-
?
D-allose
D-psicose
-
-
-
-
r
D-allose
D-psicose
-
-
-
?
D-allose
D-psicose
-
-
-
-
?
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
r
D-allose
D-psicose
-
-
-
-
r
D-Arabinose
?
-
slight activity
-
-
?
D-glucose
?
-
slight activity
-
-
?
D-gulose
D-sorbose
-
-
-
r
D-gulose
D-sorbose
-
-
-
-
r
D-gulose
D-sorbose
-
-
-
-
r
D-gulose
D-sorbose
Halalkalibacterium halodurans
-
5% activity compared to L-rhamnose
-
-
?
D-gulose
D-sorbose
Halalkalibacterium halodurans ATCC BAA-125
-
5% activity compared to L-rhamnose
-
-
?
D-gulose
D-sorbose
-
-
-
-
r
D-gulose
D-sorbose
-
-
-
-
r
D-Mannose
?
-
-
-
-
?
D-Mannose
?
-
slight activity
-
-
?
D-psicose
D-allose
-
-
-
r
D-psicose
D-allose
-
-
-
r
D-psicose
D-allose
-
-
the product mixture contains 25% D-allose, 8% D-altrose, and 67% D-psicose
-
?
D-psicose
D-allose
-
-
-
r
D-psicose
D-allose
-
-
-
r
D-Ribose
?
-
-
-
-
?
D-ribose
D-ribulose
16% conversion at 50°C
-
-
r
D-ribose
D-ribulose
-
-
-
r
D-ribose
D-ribulose
-
-
-
r
D-ribose
D-ribulose
very minimal activity toward D-ribose
-
-
?
D-ribose
D-ribulose
very minimal activity toward D-ribose
-
-
?
D-ribose
D-ribulose
worst substrate
-
-
?
D-ribose
D-ribulose
worst substrate
-
-
?
D-ribose
D-ribulose
-
-
-
-
?
D-ribose
D-ribulose
-
-
-
-
?
D-ribose
D-ribulose
-
equilibrium ratio of D-ribose:D-ribulose is 70:30
-
?
D-ribose
D-ribulose
-
16% of the activity relative to L-rhamnose
-
?
D-ribose
D-ribulose
-
-
-
?
D-ribose
D-ribulose
-
-
-
r
D-ribose
D-ribulose
-
-
-
?
D-ribose
D-ribulose
-
-
-
?
D-ribose
D-ribulose
-
-
-
r
D-ribose
D-ribulose
-
-
-
r
D-ribose
D-ribulose
-
-
-
-
r
D-ribose
D-ribulose
-
-
-
-
r
L-fructose
L-mannose
-
-
-
r
L-fructose
L-mannose
-
-
-
r
L-fructose
L-mannose
-
-
-
?
L-fructose
L-mannose
-
-
-
r
L-fructose
L-mannose
-
-
-
-
r
L-lyxose
?
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
?
L-lyxose
L-xylulose
-
-
-
?
L-lyxose
L-xylulose
second best substrate
-
-
?
L-lyxose
L-xylulose
second best substrate
-
-
?
L-lyxose
L-xylulose
-
-
-
?
L-lyxose
L-xylulose
Halalkalibacterium halodurans
-
144% activity compared to L-rhamnose
-
-
?
L-lyxose
L-xylulose
Halalkalibacterium halodurans ATCC BAA-125
-
144% activity compared to L-rhamnose
-
-
?
L-lyxose
L-xylulose
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-lyxose
L-xylulose
-
equilibrium ratio of L-lyxose:L-xylulose is 70:30
-
?
L-lyxose
L-xylulose
-
97% of the activity relative to L-rhamnose
-
?
L-lyxose
L-xylulose
-
equilibrium ratio of L-lyxose:L-xylulose is 70:30
-
?
L-lyxose
L-xylulose
-
97% of the activity relative to L-rhamnose
-
?
L-lyxose
L-xylulose
-
-
-
?
L-lyxose
L-xylulose
-
-
-
r
L-lyxose
L-xylulose
-
-
-
r
L-lyxose
L-xylulose
-
-
-
r
L-lyxose
L-xylulose
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-mannose
?
-
-
-
-
?
L-Mannose
L-Fructose
25% conversion at 50°C
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
?
L-Mannose
L-Fructose
-
-
-
?
L-Mannose
L-Fructose
-
-
-
?
L-Mannose
L-Fructose
-
-
-
?
L-Mannose
L-Fructose
-
-
-
-
r
L-Mannose
L-Fructose
Halalkalibacterium halodurans
-
59% activity compared to L-rhamnose
-
-
?
L-Mannose
L-Fructose
Halalkalibacterium halodurans ATCC BAA-125
-
59% activity compared to L-rhamnose
-
-
?
L-Mannose
L-Fructose
-
-
-
-
?
L-Mannose
L-Fructose
-
0.6% of the activity with L-rhamnose
-
-
?
L-Mannose
L-Fructose
-
-
-
-
?
L-Mannose
L-Fructose
-
-
-
-
?
L-Mannose
L-Fructose
-
only reverse direction described. At equilibrium the production of L-mannose from L-fructose is 30%
-
?
L-Mannose
L-Fructose
-
30% of the activity relative to L-rhamnose
-
?
L-Mannose
L-Fructose
-
equilibrium ratio of L-mannose:L-fructose is 30:70
-
?
L-Mannose
L-Fructose
-
only reverse direction described. At equilibrium the production of L-mannose from L-fructose is 30%
-
?
L-Mannose
L-Fructose
-
30% of the activity relative to L-rhamnose
-
?
L-Mannose
L-Fructose
-
equilibrium ratio of L-mannose:L-fructose is 30:70
-
?
L-Mannose
L-Fructose
-
-
-
?
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
Arthrobacter pyridinolis
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
best substrate, conversion yield of 43%
-
-
?
L-Rhamnose
L-Rhamnulose
best substrate, conversion yield of 43%
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
Halalkalibacterium halodurans
-
100% activity
-
-
r
L-Rhamnose
L-Rhamnulose
Halalkalibacterium halodurans
-
i.e 6-deoxy-L-mannose
i.e 6-deoxy-L-fructose
-
r
L-Rhamnose
L-Rhamnulose
Halalkalibacterium halodurans ATCC BAA-125
-
i.e 6-deoxy-L-mannose
i.e 6-deoxy-L-fructose
-
r
L-Rhamnose
L-Rhamnulose
Halalkalibacterium halodurans ATCC BAA-125
-
100% activity
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
the equilibrium is reached at 57% rhamnose and 43% rhamnulose
-
?
L-Rhamnose
L-Rhamnulose
-
highest activity
-
-
?
L-Rhamnose
L-Rhamnulose
-
highest activity
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
L-RhI catalyzes not only the reversible isomerization of L-rhamnose to L-rhamnulose, but also isomerization between various rare aldoses and ketoses
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
r
L-Rhamnose
L-Rhamnulose
best aldose substrate
-
-
r
L-Rhamnose
L-Rhamnulose
best aldose substrate
-
-
r
L-Rhamnose
L-Rhamnulose
-
highest specific activity
-
-
r
L-Rhamnose
L-Rhamnulose
-
highest specific activity
-
-
r
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-Rhamnose
L-Rhamnulose
-
-
-
?
L-talose
?
Halalkalibacterium halodurans
-
3% activity compared to L-rhamnose
-
-
?
L-talose
?
Halalkalibacterium halodurans ATCC BAA-125
-
3% activity compared to L-rhamnose
-
-
?
L-xylulose
L-lyxose
-
-
-
?
L-xylulose
L-lyxose
-
-
-
-
r
L-xylulose
L-lyxose
-
-
-
-
r
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
the enzyme generally occurs in the metabolism of fructose and mannose
-
-
?
additional information
?
-
Arthrobacter pyridinolis
-
inducible enzyme of L-rhamnose metabolism
-
-
?
additional information
?
-
-
in mutants adapted to grow on L-lyxose: enzyme of the rhamnose metabolism and L-lyxose metabolism, inducable by L-rhamnose or L-lyxose
-
-
?
additional information
?
-
-
substrate binding structue, overview, L-RhI can efficiently catalyze the isomerization between various aldoses and ketoses, showing a broad substrate specificity compared to L-RhI from Escherichia coli, relationship between structure and substrate specificity, overview, the beta1-alpha1 loop, Gly60Arg76, of L-RhI is involved in the substrate binding of a neighbouring molecule
-
-
?
additional information
?
-
the Pseudomonas stutzeri enzyme shows a broader substrate specificity compared to the enzyme from Escherichia coli, overview
-
-
?
additional information
?
-
-
the Pseudomonas stutzeri enzyme shows a broader substrate specificity compared to the enzyme from Escherichia coli, overview
-
-
?
additional information
?
-
the enzyme recognizes substrates at C2 and C3 but not at C4 and C5
-
-
?
additional information
?
-
-
the enzyme recognizes substrates at C2 and C3 but not at C4 and C5
-
-
?
additional information
?
-
-
enzyme of L-rhamnose degradation. Induced by L-rhamnose, but not repressed by D-glucose
-
-
?
additional information
?
-
-
no activity is observed with D-ribose 5-phosphate, D-glucose 6-phosphate and D-mannose 6-phosphate
-
-
?
additional information
?
-
-
no activity is observed with D-ribose 5-phosphate, D-glucose 6-phosphate and D-mannose 6-phosphate
-
-
?
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Al3+
-
1 mM, activates to 104% of control
Ca2+
the enzyme shows 1% activity in the presence of 1 mM Ca2+ as compared to 1 mM Co2+
Li+
-
1 mM, activates to 106% of control
Na+
the enzyme shows 19% activity in the presence of 1 mM Na+ as compared to 1 mM Co2+
Co2+
strictly dependent on Mn2+ or Co2+, activates
Co2+
1 mM, 10fold activiation
Co2+
maximum activity in the presence of Co2+
Co2+
-
most effective activator of metal ions tested
Co2+
Halalkalibacterium halodurans
-
required for catalytic activity, 93% activity at 1 mM compared to Mn2+
Co2+
-
30% of the activation compared to Mn2+
Co2+
100% activity in the presence of 1 mM Co2+
Co2+
1 mM, 93% of the activity with Mn2+
Mg2+
1 mM, 2.9fold activiation
Mg2+
Halalkalibacterium halodurans
-
required for catalytic activity, 57% activity at 1 mM compared to Mn2+
Mg2+
-
6% of the activiation compared to Mn2+
Mg2+
the enzyme shows 9% activity in the presence of 1 mM Mg2+ as compared to 1 mM Co2+
Mg2+
1 mM, 64% of the activity with Mn2+
Mn2+
strictly dependent on Mn2+ or Co2+, activates at 1 mM
Mn2+
1 mM, 47fold activation
Mn2+
-
1 mM, 25fold increase in activity
Mn2+
the enzyme shows 58% of the maximum activity in the presence of Mn2+
Mn2+
in the crystal structure, although not necessarily in vivo, rhamnose isomerase appears to bind Zn2+ at a structural site. In the presence of substrate the enzyme also binds Mn2+ at a nearby catalytic site
Mn2+
Halalkalibacterium halodurans
-
required for catalytic activity, 100% activity at 1 mM
Mn2+
-
optimal concentration: 0.12 mM
Mn2+
-
most effective activator of divalent cations tested
Mn2+
-
highest activity in the presence of Mn2+
Mn2+
-
1 mM MnCl2 enhances activity 4fold
Mn2+
-
immobilized as well as free enzyme requires Mn2+ for maximal activity
Mn2+
-
1 mM, activates to 112% of control
Mn2+
the enzyme shows 61% activity in the presence of 1 mM Mn2+ as compared to 1 mM Co2+
Mn2+
1 mM, best activator
Mn2+
1 mM, optimum concentration, 7fold increase in activity
Mn2+
-
enzyme activity is the highest with Mn2+, the optimal Mn2+ concentration is 1 mM (6.7fold increase activity relative to no treatment)
Ni2+
-
Ni2+
1 mM, 78% of the activity with Mn2+
Zn2+
in the crystal structure, although not necessarily in vivo, rhamnose isomerase appears to bind Zn2+ at a structural site. In the presence of substrate the enzyme also binds Mn2+ at a nearby catalytic site
Zn2+
Halalkalibacterium halodurans
-
required for catalytic activity, 20% activity at 1 mM compared to Mn2+
Zn2+
the enzyme shows 2% activity in the presence of 1 mM Zn2+ as compared to 1 mM Co2+
additional information
divalent cation required
additional information
no activity in the presence of Na+, Mg2+, Ca2+, Cu2+, K+, and Zn2+ or in the absence of any ions
additional information
-
no activity in the presence of Na+, Mg2+, Ca2+, Cu2+, K+, and Zn2+ or in the absence of any ions
additional information
Halalkalibacterium halodurans
-
enzyme without any metal ions shows a negligible activity. The enzyme activity is not stimulated by Ca2+, Ba2+, Na2+, Fe2+, or Cu2+
additional information
the enzyme shows null activity in the absence of any ions, as well as in the presence of Cu2+ and K+
additional information
-
the enzyme shows null activity in the absence of any ions, as well as in the presence of Cu2+ and K+
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70.4
D-psicose
pH 7.5, 65°C
5.25
L-talose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
2.7
D-allose
wild type enzyme, pH and temperature not specified in the publication
5.98
D-allose
pH 8.5, 60°C
7.11
D-allose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
14.3
D-allose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
25.9
D-allose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
33.9
D-allose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
35.6
D-allose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
41.8
D-allose
pH 7.0, 65°C, recombinant enzyme
42
D-allose
50°C, pH 9.0, recombinant enzyme
44.7
D-allose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
53.3
D-allose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
60
D-allose
mutant enzyme H101N, pH and temperature not specified in the publication
61.5
D-allose
at pH 8.0 and 75°C
87.9
D-allose
pH 7.5, 65°C
121
D-allose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
71
D-altrose
-
-
71
D-altrose
50°C, pH 9.0, recombinant enzyme
127
D-arabinose
-
-
127.4
D-arabinose
50°C, pH 9.0, recombinant enzyme
564
D-glucose
-
-
564
D-glucose
50°C, pH 9.0, recombinant enzyme
3 - 3.5
D-ribose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
3.53
D-ribose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
6.18
D-ribose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
8.64
D-ribose
pH 8.5, 60°C
34.9
D-ribose
pH 7.0, 65°C, recombinant enzyme
38.5
D-ribose
50°C, pH 9.0, recombinant enzyme
39.1
D-ribose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
44.4
D-ribose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
54.5
D-ribose
at pH 8.0 and 75°C
65.6
D-ribose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
67.3
D-ribose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
85.1
D-ribose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
250
D-xylose
-
-
250
D-xylose
50°C, pH 9.0, recombinant enzyme
73.2
L-Fructose
at pH 8.0 and 75°C
123
L-Fructose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
3.65
L-Lyxose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
23.5
L-Lyxose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
28.9
L-Lyxose
pH 7.0, 65°C, recombinant enzyme
33.4
L-Lyxose
at pH 8.0 and 75°C
45.2
L-Lyxose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
61.7
L-Lyxose
50°C, pH 9.0, recombinant enzyme
69
L-Lyxose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
86
L-Lyxose
-
pH 8.0, 60°C
771
L-Lyxose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
2 - 3.4
L-Mannose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
3.64
L-Mannose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
16.1
L-Mannose
pH 7.0, 65°C, recombinant enzyme
36.8
L-Mannose
at pH 8.0 and 75°C
47.9
L-Mannose
pH 7.5, 65°C
55.5
L-Mannose
50°C, pH 9.0, recombinant enzyme
58.9
L-Mannose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
76
L-Mannose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
97
L-Mannose
-
pH 8.0, 60°C
119
L-Mannose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
0.49
L-rhamnose
pH 8.5, 60°C
0.92
L-rhamnose
wild type enzyme, pH and temperature not specified in the publication
1.03
L-rhamnose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
3.53
L-rhamnose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
4.89
L-rhamnose
pH 7.0, 65°C, recombinant enzyme
5
L-rhamnose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
7.9
L-rhamnose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
9.4
L-rhamnose
mutant enzyme H101N, pH and temperature not specified in the publication
11.9
L-rhamnose
50°C, pH 9.0, recombinant enzyme
12.2
L-rhamnose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
18.5
L-rhamnose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
19.4
L-rhamnose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
24.2
L-rhamnose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
24.6
L-rhamnose
at pH 8.0 and 75°C
33.8
L-rhamnose
pH 7.5, 65°C
37
L-rhamnose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
53
L-rhamnose
-
pH 8.0, 60°C
55
L-rhamnose
50°C, pH 9.0, intrinsic enzyme from Pseudomonas stutzeri
528
L-rhamnose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
1.7
L-rhamnulose
-
-
202
L-Xylose
-
-
203
L-Xylose
50°C, pH 9.0, recombinant enzyme
63
L-xylulose
at pH 8.0 and 75°C
111
L-xylulose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7
L-talose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
0.74
D-allose
pH 8.5, 60°C
1.3
D-allose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
2.7
D-allose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
3.8
D-allose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
7.4
D-allose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
9.8
D-allose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
14.2
D-allose
pH 7.0, 65°C, recombinant enzyme
16.8
D-allose
wild type enzyme, pH and temperature not specified in the publication
21.2
D-allose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
24.5
D-allose
mutant enzyme H101N, pH and temperature not specified in the publication
33.9
D-allose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
68.1
D-allose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
81
D-allose
at pH 8.0 and 75°C
0.1
D-ribose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
1.7
D-ribose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
1.8
D-ribose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
3.3
D-ribose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
8.9
D-ribose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
11.4
D-ribose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
21.5
D-ribose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
30.7
D-ribose
pH 8.5, 60°C
34.5
D-ribose
pH 7.0, 65°C, recombinant enzyme
49
D-ribose
at pH 8.0 and 75°C
118
D-ribose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
116
L-Fructose
at pH 8.0 and 75°C
274
L-Fructose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
53
L-Lyxose
-
pH 8.0, 60°C
73.8
L-Lyxose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
76.8
L-Lyxose
pH 7.0, 65°C, recombinant enzyme
186
L-Lyxose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
200
L-Lyxose
at pH 8.0 and 75°C
216
L-Lyxose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
240
L-Lyxose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
462
L-Lyxose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
10
L-Mannose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
10.5
L-Mannose
pH 8.5, 60°C
30
L-Mannose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
31
L-Mannose
pH 7.0, 65°C, recombinant enzyme
37
L-Mannose
-
pH 8.0, 60°C
78.7
L-Mannose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
88.88
L-Mannose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
155
L-Mannose
at pH 8.0 and 75°C
442
L-Mannose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
5.1
L-rhamnose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
7.7
L-rhamnose
pH 8.5, 60°C
13.3
L-rhamnose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
50.5
L-rhamnose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
53.6
L-rhamnose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
68
L-rhamnose
pH 7.0, 65°C, recombinant enzyme
99.9
L-rhamnose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
142
L-rhamnose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
146
L-rhamnose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
149.5
L-rhamnose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
153
L-rhamnose
-
pH 8.0, 60°C
180
L-rhamnose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
192
L-rhamnose
mutant enzyme H101N, pH and temperature not specified in the publication
195
L-rhamnose
at pH 8.0 and 75°C
224
L-rhamnose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
374
L-rhamnose
wild type enzyme, pH and temperature not specified in the publication
130
L-xylulose
at pH 8.0 and 75°C
281
L-xylulose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.04
D-psicose
pH 7.5, 65°C
1.3
L-talose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
0.02
D-allose
pH 7.5, 65°C
0.071
D-allose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.081
D-allose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.12
D-allose
pH 8.5, 60°C
0.2
D-allose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
0.27
D-allose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.28
D-allose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
0.28
D-allose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.41
D-allose
mutant enzyme H101N, pH and temperature not specified in the publication
0.47
D-allose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
1.3
D-allose
at pH 8.0 and 75°C
4.77
D-allose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
6.2
D-allose
wild type enzyme, pH and temperature not specified in the publication
0.0027
D-ribose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.0043
D-ribose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.005
D-ribose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.13
D-ribose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.15
D-ribose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
0.2
D-ribose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.8
D-ribose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
0.9
D-ribose
at pH 8.0 and 75°C
3.54
D-ribose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
3.6
D-ribose
pH 8.5, 60°C
1.6
L-Fructose
at pH 8.0 and 75°C
2.23
L-Fructose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
0.62
L-Lyxose
-
pH 8.0, 60°C
3.1
L-Lyxose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
5.3
L-Lyxose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
6
L-Lyxose
at pH 8.0 and 75°C
6.72
L-Lyxose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
50.8
L-Lyxose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
0.27
L-Mannose
pH 7.5, 65°C
0.38
L-Mannose
-
pH 8.0, 60°C
0.4
L-Mannose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
0.51
L-Mannose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
1.3
L-Mannose
pH 8.5, 60°C
4.2
L-Mannose
at pH 8.0 and 75°C
5.82
L-Mannose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
21.6
L-Mannose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
0.283
L-rhamnose
Halalkalibacterium halodurans
-
in 50 mM malate buffer, at pH 7.0 and 70°C
0.41
L-rhamnose
mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.55
L-rhamnose
mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
0.59
L-rhamnose
pH 7.5, 65°C
2.89
L-rhamnose
-
pH 8.0, 60°C
6.8
L-rhamnose
mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
7.7
L-rhamnose
mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
7.9
L-rhamnose
at pH 8.0 and 75°C
10.1
L-rhamnose
-
in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C
11.6
L-rhamnose
wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C
15.75
L-rhamnose
pH 8.5, 60°C
20
L-rhamnose
mutant enzyme H101N, pH and temperature not specified in the publication
39.36
L-rhamnose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
50.8
L-rhamnose
at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0
97.1
L-rhamnose
in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C
410
L-rhamnose
wild type enzyme, pH and temperature not specified in the publication
2.1
L-xylulose
at pH 8.0 and 75°C
2.55
L-xylulose
-
purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)
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.
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.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 47636, sequence calculation, x * 47000, SDS-PAGE, native enzyme
?
-
x * 48000, SDS-PAGE
-
?
x * 48300, claculated from sequence, 4 * 48000, SDS-PAGE
?
-
x * 48300, claculated from sequence, 4 * 48000, SDS-PAGE
-
?
Halalkalibacterium halodurans
-
x * 48000, SDS-PAGE
?
Halalkalibacterium halodurans ATCC BAA-125
-
x * 48000, SDS-PAGE
-
?
-
x * 46946, calculated from amino acid sequence
?
-
x * 46946, calculated from amino acid sequence
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 43000, SDS-PAGE, x * 47681, recombinant His-tagged enzyme, MALDI-TOF mass spectrometry
?
x * 48960, calculated from amino acid sequence
?
-
x * 48000, SDS-PAGE
-
?
-
x * 48960, calculated from amino acid sequence
-
?
x * 465850, calculated from sequence, x * 46000, SDS-PAGE
?
-
x * 465850, calculated from sequence, x * 46000, SDS-PAGE
-
homodimer
Halalkalibacterium halodurans
-
2 * 48000, SDS-PAGE
homodimer
Halalkalibacterium halodurans
-
2 * 48178, calculated from amino acid sequence
homodimer
Halalkalibacterium halodurans ATCC BAA-125
-
2 * 48000, SDS-PAGE
-
homodimer
Halalkalibacterium halodurans ATCC BAA-125
-
2 * 48178, calculated from amino acid sequence
-
homotetramer
4 * 48000, SDS-PAGE
homotetramer
4 * 48292, MALDI-TOF mass spectrometry
homotetramer
4 * 48294, calculated from amino acid sequence
homotetramer
-
4 * 48000, SDS-PAGE
-
homotetramer
-
4 * 48292, MALDI-TOF mass spectrometry
-
homotetramer
-
4 * 48294, calculated from amino acid sequence
-
homotetramer
4 * 46695, calculated from amino acid sequence
homotetramer
4 * 47000, His6-tagged enzyme, SDS-PAGE
homotetramer
-
4 * 46695, calculated from amino acid sequence
-
homotetramer
-
4 * 47000, His6-tagged enzyme, SDS-PAGE
-
tetramer
-
4 * 48600, SDS-PAGE, 4 * 49468, calculated from sequence
tetramer
-
4 * 48600, SDS-PAGE, 4 * 49468, calculated from sequence
-
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 42000, SDS-PAGE
-
tetramer
-
L-RhI has a large domain with a (beta/alpha)8 barrel fold and an additional small domain composed of seven alpha-helices, forming a homotetramer, crystal structure analysis
tetramer
-
4 * 46000, SDS-PAGE
tetramer
-
4 * 45527, calculated from amino acid sequence
tetramer
-
4 * 46000, SDS-PAGE
-
tetramer
-
4 * 45527, calculated from amino acid sequence
-
trimer
3 * 49000, SDS-PAGE, 3 * 48998, calculated from sequence
trimer
-
3 * 49000, SDS-PAGE, 3 * 48998, calculated from sequence
-
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Noltmann, E.A.
Aldose-ketose isomerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
271-354
1972
Klebsiella aerogenes, Escherichia coli, Lactiplantibacillus plantarum, Yersinia pestis, Escherichia coli B / ATCC 11303
-
brenda
Domagk, G.F.; Zech, R.
Ueber den Abbau der Desoxyzucker durch Bacterienenzyme. I. L-Rhamnose-isomerase aus Lactobacillus plantarum
Biochem. Z.
339
145-153
1963
Lactiplantibacillus plantarum
-
brenda
Domagk, G.F.; Zech, R.
L-Rhamnose isomerase
Methods Enzymol.
9
579-582
1966
Escherichia coli, Lactiplantibacillus plantarum, Yersinia pestis
-
brenda
Izumori, K.; Mitchell, M.; Elbein, A.D.
Evidence that the isomerization of D-ribose and L-rhamnose is catalyzed by the same enzyme in Mycobacterium smegmatis
J. Bacteriol.
126
553-555
1976
Mycolicibacterium smegmatis
brenda
Levinson, S.L.; Krulwich, T.A.
Metabolism of L-rhamnose in Arthrobacter pyridinolis
J. Gen. Microbiol.
95
277-286
1976
Arthrobacter pyridinolis
brenda
Akhy, M.T.; Brown, C.M.; Old, D.C.
L-Rhamnose utilization in Salmonella typhimurium
J. Appl. Bacteriol.
56
269-274
1984
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Bhuiyan, S.H.; Itami, Y.; Izumori, K.
Immobilization of L-rhamnose isomerase and its application in L-mannose production from L-fructose
J. Ferment. Bioeng.
84
558-562
1997
Pseudomonas sp., Pseudomonas sp. LL172
-
brenda
Bhuiyan, S.H.; Itami, Y.; Izumori, K.
Isolation of an L-rhamnose isomerase-constitutive mutant of Pseudomonas sp. strain LL172: purification and characterization of the enzyme
J. Ferment. Bioeng.
84
319-323
1997
Pseudomonas sp., Pseudomonas sp. LL172
-
brenda
Bhuiyan, S.H.; Itami, Y.; Rokui, Y.; Katayama, T.; Izumori, K.
D-Allose production from D-psicose using immobilized D-rhamnose isomerase
J. Ferment. Bioeng.
85
539-541
1998
Pseudomonas sp., Pseudomonas sp. LL172
-
brenda
Garcia-Junceda, E.; Shen, G.J.; Alajarin, R.; Wong, C.H.
Cloning and overexpression of rhamnose isomerase and fucose isomerase
Bioorg. Med. Chem.
3
1349-1355
1995
Escherichia coli
brenda
Badia, J.; Baldoma, L.; Aguilar, J.; Boronat, A.
Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12
FEMS Microbiol. Lett.
65
253-258
1989
Escherichia coli
brenda
Badia, J.; Gimenez, R.; Baldoma, L.; Barnes, E.; Fessner, W.D.; Aguilar, J.
L-Lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose
J. Bacteriol.
173
5144-5150
1991
Escherichia coli
brenda
Korndrfer, I.P.; Fessner, W.D.; Matthews, B.W.
The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution
J. Mol. Biol.
300
917-933
2000
Escherichia coli (P32170), Escherichia coli
brenda
Leang, K.; Takada, G.; Ishimura, A.; Okita, M.; Izumori, K.
Cloning, nucleotide sequence, and overexpression of the L-rhamnose isomerase gene from Pseudomonas stutzeri in Escherichia coli
Appl. Environ. Microbiol.
70
3298-3304
2004
Pseudomonas stutzeri (Q75WH8), Pseudomonas stutzeri
brenda
Leang, K.; Takada, G.; Fukai, Y.; Morimoto, K.; Granstrom, T.B.; Izumori, K.
Novel reactions of L-rhamnose isomerase from Pseudomonas stutzeri and its relation with D-xylose isomerase via substrate specificity
Biochim. Biophys. Acta
1674
68-77
2004
Pseudomonas stutzeri
brenda
Granstroem, T.B.; Takata, G.; Morimoto, K.; Leisola, M.; Izumori, K.
L-Xylose and L-lyxose production from xylitol using Alcaligenes 701B strain and immobilized L-rhamnose isomerase enzyme
Enzyme Microb. Technol.
36
976-981
2005
Pseudomonas stutzeri
-
brenda
Yoshida, H.; Wayoon, P.; Takada, G.; Izumori, K.; Kamitori, S.
Crystallization and preliminary X-ray diffraction studies of L-rhamnose isomerase from Pseudomonas stutzeri
Acta Crystallogr. Sect. F
62
550-552
2006
Pseudomonas stutzeri (Q75WH8), Pseudomonas stutzeri
brenda
Poonperm, W.; Takata, G.; Okada, H.; Morimoto, K.; Granstroem, T.B.; Izumori, K.
Cloning, sequencing, overexpression and characterization of L-rhamnose isomerase from Bacillus pallidus Y25 for rare sugar production
Appl. Microbiol. Biotechnol.
76
1297-1307
2007
Aeribacillus pallidus (A8CEF6)
brenda
Menavuvu, B.T.; Poonperm, W.; Leang, K.; Noguchi, N.; Okada, H.; Morimoto, K.; Granstroem, T.B.; Takada, G.; Izumori, K.
Efficient biosynthesis of D-allose from D-psicose by cross-linked recombinant L-rhamnose isomerase: separation of product by ethanol crystallization
J. Biosci. Bioeng.
101
340-345
2006
Pseudomonas stutzeri
brenda
Yoshida, H.; Yamada, M.; Ohyama, Y.; Takada, G.; Izumori, K.; Kamitori, S.
The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity
J. Mol. Biol.
365
1505-1516
2007
Pseudomonas stutzeri
brenda
Yoshida, H.; Yamaji, M.; Ishii, T.; Izumori, K.; Kamitori, S.
Catalytic reaction mechanism of Pseudomonas stutzeri L-rhamnose isomerase deduced from X-ray structures
FEBS J.
277
1045-1057
2010
Pseudomonas stutzeri (Q75WH8), Pseudomonas stutzeri
brenda
Wu, R.; Xie, H.; Mo, Y.; Cao, Z.
Broad substrate specificity and catalytic mechanism of Pseudomonas stutzeri L-rhamnose isomerase: insights from QM/MM molecular dynamics simulations
J. Phys. Chem. A
113
11595-11603
2009
Pseudomonas stutzeri (Q75WH8), Pseudomonas stutzeri
brenda
Doan, T.N.; Prabhu, P.; Kim, J.K.; Ahn, Y.J.; Natarajan, S.; Kang, L.W.; Park, G.T.; Lim, S.B.; Lee, J.K.
Crystallization and preliminary X-ray crystallographic analysis of L-rhamnose isomerase with a novel high thermostability from Bacillus halodurans
Acta Crystallogr. Sect. F
66
677-680
2010
Halalkalibacterium halodurans, Halalkalibacterium halodurans ATCC BAA-125
brenda
Prabhu, P.; Doan, T.T.; Jeya, M.; Kang, L.W.; Lee, J.K.
Cloning and characterization of a rhamnose isomerase from Bacillus halodurans
Appl. Microbiol. Biotechnol.
89
635-644
2011
Halalkalibacterium halodurans, Halalkalibacterium halodurans ATCC BAA-125
brenda
Takata, G.; Uechi, K.; Taniguchi, E.; Kanbara, Y.; Yoshihara, A.; Morimoto, K.; Izumori, K.
Characterization of Mesorhizobium loti L-rhamnose isomerase and its application to L-talose production
Biosci. Biotechnol. Biochem.
75
1006-1009
2011
Mesorhizobium loti, Mesorhizobium loti Tono
brenda
Park, C.S.; Yeom, S.J.; Lim, Y.R.; Kim, Y.S.; Oh, D.K.
Characterization of a recombinant thermostable L-rhamnose isomerase from Thermotoga maritima ATCC 43589 and its application in the production of L-lyxose and L-mannose
Biotechnol. Lett.
32
1947-1953
2010
Thermotoga maritima, Thermotoga maritima ATCC 43589
brenda
Lin, C.J.; Tseng, W.C.; Lin, T.H.; Liu, S.M.; Tzou, W.S.; Fang, T.Y.
Characterization of a thermophilic L-rhamnose isomerase from Thermoanaerobacterium saccharolyticum NTOU1
J. Agric. Food Chem.
58
10431-10436
2010
Thermoanaerobacterium saccharolyticum (D5LNE5), Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum NTOU1 (D5LNE5), Thermoanaerobacterium saccharolyticum NTOU1
brenda
Yoshida, H.; Takeda, K.; Izumori, K.; Kamitori, S.
Elucidation of the role of Ser329 and the C-terminal region in the catalytic activity of Pseudomonas stutzeri L-rhamnose isomerase
Protein Eng. Des. Sel.
23
919-927
2010
Pseudomonas stutzeri (Q75WH8), Pseudomonas stutzeri
brenda
Kim, Y.S.; Shin, K.C.; Lim, Y.R.; Oh, D.K.
Characterization of a recombinant L-rhamnose isomerase from Dictyoglomus turgidum and its application for L-rhamnulose production
Biotechnol. Lett.
35
259-264
2013
Dictyoglomus turgidum (B8E1U6), Dictyoglomus turgidum, Dictyoglomus turgidum DSM 6724 (B8E1U6)
brenda
Yoshida, H.; Yoshihara, A.; Teraoka, M.; Yamashita, S.; Izumori, K.; Kamitori, S.
Structure of L-rhamnose isomerase in complex with L-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site
FEBS Open Bio
3
35-40
2013
Pseudomonas stutzeri (Q75WH8)
brenda
Lin, C.J.; Tseng, W.C.; Fang, T.Y.
Characterization of a thermophilic L-rhamnose isomerase from Caldicellulosiruptor saccharolyticus ATCC 43494
J. Agric. Food Chem.
59
8702-8708
2011
Caldicellulosiruptor saccharolyticus (A4XHV7), Caldicellulosiruptor saccharolyticus, Caldicellulosiruptor saccharolyticus ATCC 43494 (A4XHV7)
brenda
Park, C.
Characterization of a recombinant L-rhamnose isomerase from Bacillus subtilis and its application on production of L-lyxose and L-mannose
Biotechnol. Bioprocess Eng.
19
18-25
2014
Bacillus subtilis, Bacillus subtilis ATCC 23857
-
brenda
Seo, M.J.; Choi, J.H.; Kang, S.H.; Shin, K.C.; Oh, D.K.
Characterization of L-rhamnose isomerase from Clostridium stercorarium and its application to the production of D-allose from D-allulose (D-psicose)
Biotechnol. Lett.
40
325-334
2018
Thermoclostridium stercorarium subsp. stercorarium (L7VQ35), Thermoclostridium stercorarium subsp. stercorarium DSM 8532 (L7VQ35)
brenda
Bai, W.; Shen, J.; Zhu, Y.; Men, Y.; Sun, Y.; Ma, Y.
Characteristics and kinetic properties of L-rhamnose isomerase from Bacillus subtilis by isothermal titration calorimetry for the production of D-allose
Food Sci. Technol. Res.
21
13-22
2015
Bacillus subtilis (O05264), Bacillus subtilis 168 (O05264)
-
brenda
Chen, Z.; Xu, W.; Zhang, W.; Zhang, T.; Jiang, B.; Mu, W.
Characterization of a thermostable recombinant L-rhamnose isomerase from Caldicellulosiruptor obsidiansis OB47 and its application for the production of L-fructose and L-rhamnulose
J. Sci. Food Agric.
98
2184-2193
2018
Caldicellulosiruptor obsidiansis (D9TIY8), Caldicellulosiruptor obsidiansis OB47 (D9TIY8), Caldicellulosiruptor obsidiansis OB47
brenda
Xu, W.; Zhang, W.; Tian, Y.; Zhang, T.; Jiang, B.; Mu, W.
Characterization of a novel thermostable L-rhamnose isomerase from Thermobacillus composti KWC4 and its application for production of D-allose
Process Biochem.
53
153-161
2017
Thermobacillus composti (L0ECT7), Thermobacillus composti DSM 18247 (L0ECT7)
-
brenda