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D-ribulose
D-ribose
-
-
-
r
D-tagatose
D-talose
-
-
-
r
L-gulose
L-sorbose
-
-
-
r
L-ribulose
L-ribose
-
-
-
r
L-talose
L-tagatose
-
-
-
-
r
additional information
?
-
D-allose
D-psicose
-
-
-
-
r
D-allose
D-psicose
-
-
-
-
r
D-fructose
D-mannose
-
-
-
r
D-fructose
D-mannose
-
-
-
-
?
D-fructose
D-mannose
-
-
-
-
r
D-fructose
D-mannose
-
-
-
r
D-fructose
D-mannose
reaction of EC 5.3.1.7
-
-
r
D-fructose
D-mannose
reaction of EC 5.3.1.7
-
-
r
D-fructose
D-mannose
-
reaction of EC 5.3.1.7
-
-
r
D-Lyxose
D-Xylulose
-
-
-
r
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
r
D-Lyxose
D-Xylulose
-
-
-
r
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
highest specific activity, the enzyme converts 500 g D-xylulose/l to 380 g D-lyxose/l after 2 h
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
highest specific activity, the enzyme converts 500 g D-xylulose/l to 380 g D-lyxose/l after 2 h
-
-
?
D-Lyxose
D-Xylulose
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
-
?
D-Lyxose
D-Xylulose
-
-
-
-
?
D-Lyxose
D-Xylulose
-
highest specific activity
-
-
r
D-Lyxose
D-Xylulose
highest activity
-
-
r
D-Lyxose
D-Xylulose
highest activity
-
-
r
D-Lyxose
D-Xylulose
best substrate
-
-
r
D-Lyxose
D-Xylulose
best substrate
-
-
r
D-Lyxose
D-Xylulose
-
best substrate
-
-
r
D-Mannose
D-Fructose
no activity with L-lyxose, Dxylose,L-xylose, D-arabinose, L-arabinose, D-ribose, L-fucose, D-glucose, D-galactose, D-erythrose, L-rhamnose, 2-deoxy-D-ribose, and ribose-5-phosphate
-
-
r
D-Mannose
D-Fructose
no activity with L-lyxose, Dxylose,L-xylose, D-arabinose, L-arabinose, D-ribose, L-fucose, D-glucose, D-galactose, D-erythrose, L-rhamnose, 2-deoxy-D-ribose, and ribose-5-phosphate
-
-
r
D-Mannose
D-Fructose
-
-
-
r
D-Mannose
D-Fructose
-
-
-
r
D-Mannose
D-Fructose
-
-
-
-
?
D-Mannose
D-Fructose
-
-
-
-
r
D-Mannose
D-Fructose
-
-
-
r
D-Mannose
D-Fructose
-
-
-
r
D-ribose
D-ribulose
-
-
-
-
r
D-ribose
D-ribulose
-
-
-
-
r
D-talose
D-tagatose
-
-
-
r
D-talose
D-tagatose
-
-
-
r
D-talose
D-tagatose
-
-
-
-
r
D-talose
D-tagatose
-
-
-
r
D-talose
D-tagatose
-
-
-
r
D-xylulose
D-lyxose
-
-
-
r
D-xylulose
D-lyxose
-
-
-
-
r
D-xylulose
D-lyxose
-
-
-
r
L-allose
L-psicose
-
-
-
r
L-allose
L-psicose
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-lyxose
L-xylulose
-
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-Mannose
L-Fructose
-
-
-
-
r
L-ribose
L-ribulose
-
-
-
r
L-ribose
L-ribulose
-
-
-
r
L-ribose
L-ribulose
-
-
-
r
L-ribose
L-ribulose
-
-
-
r
L-ribose
L-ribulose
-
-
-
-
r
L-ribose
L-ribulose
-
-
-
r
L-ribose
L-ribulose
-
-
-
r
additional information
?
-
no activity with D-glucose, D-xylose, L-arabinose, and L-rhamnose
-
-
?
additional information
?
-
-
no activity with D-glucose, D-xylose, L-arabinose, and L-rhamnose
-
-
?
additional information
?
-
-
the enzyme does not isomerizes D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
-
-
?
additional information
?
-
-
the enzyme does not isomerizes D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
-
-
?
additional information
?
-
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
-
-
?
additional information
?
-
-
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
-
-
?
additional information
?
-
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
-
-
?
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Fe3+
-
metal ion required, Fe3+ activates
Ca2+
-
metal ion required, Ca2+ activates slightly
Ca2+
the addition of Ca2+ ion to EDTA-treated enzyme enhances the activity of D-lyxose isomerization
Co2+
about 40% activity in the presence of 1 mM Co2+ as compared to Mn2+
Co2+
activating at 1 mM, D-xylose as substrate
Co2+
maximum activity (6.6fold) in the presence of 0.5 mM Co2+
Co2+
-
metal ion required, Co2+ activates slightly
Co2+
1 mM, 9.1fold activation
Fe2+
-
metal ion required, Fe2+ activates
Fe2+
1 mM, 2.1fold activation
Mg2+
about 50% activity in the presence of 1 mM Mg2+ as compared to Mn2+
Mg2+
-
about 150% activity at 1 mM Mg2+
Mn2+
highest activity (100%) in the presence of 1.0 mM Mn2+
Mn2+
at 1 mM, D-xylose as substrate, requires divalent metal ions
Mn2+
stimulates activity but to a lesser extent than Co2+
Mn2+
-
metal ion required, Mn2+ activates most effectively. Km: 0.0004 mM
Mn2+
-
maximal activity (about 250%) in the presence of 1 mM Mn2+
Mn2+
-
optimum activity in the presence of 1 mM Mn2+
Mn2+
maximum activity (190%) in the presence of 1 mM Mn2+
Mn2+
1 mM, 12.5fold activation
Ni2+
activating at 1 mM, D-xylose as substrate
Ni2+
1 mM, 11.8fold activation
additional information
not activated by Zn2+, Cu2+, and Ni2+
additional information
-
not activated by Zn2+, Cu2+, and Ni2+
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0.002
-
using L-tagatose as substrate, at pH 7.5 and 45°C
0.003
-
using L-mannose as substrate, at pH 7.5 and 45°C
0.005
-
using D-psicose as substrate, at pH 7.5 and 45°C
0.007
-
using L-lyxose as substrate, at pH 7.5 and 45°C
0.008
after 38fold purification, using L-allose as substrate, at pH 7.5 and 75°C
0.01
-
using L-psicose as substrate, at pH 7.5 and 45°C
0.011
-
using L-talose as substrate, at pH 7.5 and 45°C
0.013
-
using D-allose as substrate, at pH 7.5 and 45°C
0.014
-
using D-ribose as substrate, at pH 7.5 and 45°C
0.015
-
using D-tagatose as substrate, at pH 7.5 and 45°C
0.017
-
using L-fructose as substrate, at pH 7.5 and 45°C
0.02
using L-sorbose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
0.045
-
using D-tagatose as substrate, at pH 7.5 and 45°C
0.077
after 38fold purification, using D-ribulose as substrate, at pH 7.5 and 75°C
0.094
after 38fold purification, using D-fructose as substrate, at pH 7.5 and 75°C
0.096
-
using D-ribulose as substrate, at pH 7.5 and 45°C
0.106
after 38fold purification, using D-talose as substrate, at pH 7.5 and 75°C
0.119
after 38fold purification, using L-ribose as substrate, at pH 7.5 and 75°C
0.14
using L-ribose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
0.18
-
using L-xylulose as substrate, at pH 7.5 and 45°C
0.19
using D-talose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
0.219
-
using L-ribose as substrate, at pH 7.5 and 45°C
0.28
using D-tagatose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
0.292
after 38fold purification, using L-ribulose as substrate, at pH 7.5 and 75°C
0.4
using L-ribulose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
0.403
-
using D-fructose as substrate, at pH 7.5 and 45°C
0.5
crude extract, using D-lyxose as substrate, at pH 7.5 and 75°C
0.523
-
using D-mannose as substrate, at pH 7.5 and 45°C
0.872
-
using L-ribulose as substrate, at pH 7.5 and 45°C
1.05
using L-gulose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
1.41
using D-fructose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
1.668
after 38fold purification, using D-mannose as substrate, at pH 7.5 and 75°C
10
using D-lyxose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
18.8
after 38fold purification, using D-lyxose as substrate, at pH 7.5 and 75°C
22.33
-
using D-lyxose as substrate, at pH 7.5 and 45°C
24
after 10fold purification, in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C
24.04
-
using D-xylulose as substrate, at pH 7.5 and 45°C
26.2
using D-xylulose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
33.1
after 38fold purification, using D-xylulose as substrate, at pH 7.5 and 75°C
4.2
crude extract, in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C
5.42
using D-mannose as substrate, at pH 7.5 and 40°C, in the presence of 1 mM Mn2+
50.2
of the recombinant enzyme after purification, at 70°C, with L-ribose as substrate
8.4
of the native enzyme after purification, at 70°C, with L-ribose as substrate
0.022
after 38fold purification, using D-tagatose as substrate, at pH 7.5 and 75°C
0.022
-
using L-allose as substrate, at pH 7.5 and 45°C
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60 - 85
at pH 7.5 and 75°C and in the presence of 0.5 mM Co2+ the enzyme has a half-life of 108 min. After incubation at 75°C for 5 min, more than 97% of the enzyme activity remains. The half-lives of the enzyme at 60, 65, 70, 75, 80 and 85°C are 547, 247, 171, 108, 49, and 16 min, respectively
30 - 50
the enzyme shows half-lives of 140 h, 62 h, 30 h, 18 h, and 7 h at 30°C, 35°C, 40°C, 45°C, and 50°C, respectively
30 - 50
-
the half-lives of the free enzyme at 35, 40, 45, and 50°C are 14 h, 8.9 h, 3.4 h, and 1.4 h, while those of the enzyme immobilized on Duolite A568 are 30 h, 15 h, 5.1 h, and 2.2 h, respectively
30 - 50
-
the enzyme shows half-lives of 36 h, 14 h, 8.9 h, 3.4 h, and 1.4 h at 30°C, 35°C, 40°C, 45°C, and 50 °C, respectively
30 - 50
the enzyme shows half-lives of 84 h, 17 h, 2.6 h, 0.3 h, and 0.09 h at 30°C, 35°C, 40°C, 45°C, and 50°C, respectively
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food industry
-
the enzyme is an industrial producer of D-lyxose
food industry
-
the enzyme is an industrial producer of D-lyxose
-
synthesis
about 60.0 g/l D-mannose is obtained from 400 g/l D-glucose in 8 h by coexpression of the D-glucose isomerase from Acidothermus cellulolyticus and D-lyxose isomerase from Thermosediminibacter oceani in Escherichia coli cells. The system exhibits maximum activity at pH 6.5 and 65°C with Co2+ supplement
synthesis
bioproduction of D-tagatose from D-galactose via L-ribose synthesis performed by two step-isomerization using L-arabinose isomerase from shigella flexneri and D-lyxose/ribose isomerase. The overall 22.3% and 25% conversion rate are observed for D-tagatose and L-ribose production from D-galactose and L-arabinose, respectively
synthesis
under optimum conditions, 101.6 g/l D-mannose is produced from 400 g/l D-fructose after reaction for 9 h, giving a conversion yield of 25.4%
synthesis
-
about 60.0 g/l D-mannose is obtained from 400 g/l D-glucose in 8 h by coexpression of the D-glucose isomerase from Acidothermus cellulolyticus and D-lyxose isomerase from Thermosediminibacter oceani in Escherichia coli cells. The system exhibits maximum activity at pH 6.5 and 65°C with Co2+ supplement
-
synthesis
-
under optimum conditions, 101.6 g/l D-mannose is produced from 400 g/l D-fructose after reaction for 9 h, giving a conversion yield of 25.4%
-
synthesis
-
under optimum conditions, 101.6 g/l D-mannose is produced from 400 g/l D-fructose after reaction for 9 h, giving a conversion yield of 25.4%
-
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Anderson, R.L.; Allison, D.P.
Purification and characterization of D-lyxose isomerase
J. Biol. Chem.
240
2367-2372
1965
Klebsiella aerogenes
brenda
Anderson, R.L.
D-Lyxose isomerase
Methods Enzymol.
9
593-596
1966
Klebsiella aerogenes
-
brenda
Izumori, K.; Yamanaka, K.; Elbein, A.D.
Pentose metabolism in Mycobacterium smegmatis: specificity of induction of pentose isomerase
J. Bacteriol.
128
587-591
1976
Mycolicibacterium smegmatis
brenda
Cho, E.A.; Lee, D.W.; Cha, Y.H.; Lee, S.J.; Jung, H.C.; Pan, J.G.; Pyun, Y.R.
Characterization of a novel D-lyxose isomerase from Cohnella laevoribosii RI-39 sp. nov
J. Bacteriol.
189
1655-1663
2007
Cohnella laeviribosi (A3E7Z6), Cohnella laeviribosi, Cohnella laeviribosi RI-39 (A3E7Z6)
brenda
Patel, D.; Wi, S.; Lee, S.; Lee, D.; Song, Y.; Bae, H.
Substrate specificity of the Bacillus licheniformis lyxose isomerase YdaE and its application in in vitro catalysis for bioproduction of lyxose and glucose by two-step isomerization
Appl. Environ. Microbiol.
77
3343-3350
2011
Bacillus licheniformis (Q65N98), Bacillus licheniformis
brenda
Park, C.S.; Kwon, H.J.; Yeom, S.J.; Oh, D.K.
Mannose production from fructose by free and immobilized D-lyxose isomerases from Providencia stuartii
Biotechnol. Lett.
32
1305-1309
2010
Providencia stuartii
brenda
Kwon, H.J.; Yeom, S.J.; Park, C.S.; Oh, D.K.
Substrate specificity of a recombinant D-lyxose isomerase from Providencia stuartii for monosaccharides
J. Biosci. Bioeng.
110
26-31
2010
Providencia stuartii, Providencia stuartii KCTC 2568
brenda
Park, C.S.; Yeom, S.J.; Lim, Y.R.; Kim, Y.S.; Oh, D.K.
Substrate specificity of a recombinant D-lyxose isomerase from Serratia proteamaculans that produces D-lyxose and D-mannose
Lett. Appl. Microbiol.
51
343-350
2010
Serratia proteamaculans (D5MTT1), Serratia proteamaculans, Serratia proteamaculans KCTC 2936 (D5MTT1)
brenda
Marles-Wright, J.; Lewis, R.
The structure of a D-lyxose isomerase from the deltaB regulon of Bacillus subtilis
Proteins Struct. Funct. Bioinform.
79
2015-2019
2011
Bacillus subtilis (P96578), Bacillus subtilis, Bacillus subtilis 168 (P96578)
brenda
Choi, J.G.; Hong, S.H.; Kim, Y.S.; Kim, K.R.; Oh, D.K.
Characterization of a recombinant thermostable D-lyxose isomerase from Dictyoglomus turgidum that produces D-lyxose from D-xylulose
Biotechnol. Lett.
34
1079-1085
2012
Dictyoglomus turgidum (B8DZQ9), Dictyoglomus turgidum DSM 6724 (B8DZQ9)
brenda
Patel, M.J.; Akhani, R.C.; Patel, A.T.; Dedania, S.R.; Patel, D.H.
A single and two step isomerization process for D-tagatose and L-ribose bioproduction using L-arabinose isomerase and D-lyxose isomerase
Enzyme Microb. Technol.
97
27-33
2017
Cohnella laeviribosi (A3E7Z6), Cohnella laeviribosi
brenda
Huang, J.; Yu, L.; Zhang, W.; Zhang, T.; Guang, C.; Mu, W.
Production of D-mannose from D-glucose by co-expression of D-glucose isomerase and D-lyxose isomerase in Escherichia coli
J. Sci. Food. Agric.
98
4895-4902
2018
Thermosediminibacter oceani (D9RZ53), Thermosediminibacter oceani, Thermosediminibacter oceani DSM 16646 (D9RZ53)
brenda
Yu, L.; Zhang, W.; Zhang, T.; Jiang, B.; Mu, W.
Efficient biotransformation of D-fructose to D-mannose by a thermostable D-lyxose isomerase from Thermosediminibacter oceani
Process Biochem.
51
2026-2033
2016
Thermosediminibacter oceani (D9RZ53), Thermosediminibacter oceani DSM 1664 (D9RZ53)
-
brenda