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Information on EC 1.1.1.140 - sorbitol-6-phosphate 2-dehydrogenase Word Map on EC 1.1.1.140
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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sorbitol-6-phosphate 2-dehydrogenase
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D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
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degradation of sugar alcohols
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Fructose and mannose metabolism
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D-sorbitol degradation II
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L-sorbose degradation
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D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase
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D-glucitol-6-phosphate dehydrogenase
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D-sorbitol-6-phosphate 2-dehydrogenase
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D-sorbitol-6-phosphate dehydrogenase
dehydrogenase, D-sorbitol 6-phosphate
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Glucitol-6-phosphate dehydrogenase
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ketosephosphate reductase
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sorbitol-6-P-dehydrogenase
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sorbitol-6-phosphate dehydrogenase
additional information
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similar enzyme also named sorbitol-6-phosphate dehydrogenase from Eriobotrya japonica catalyzes following reaction: sorbitol-6-phosphate + NADP+ = glucose-6-phosphate + NADPH
D-sorbitol-6-phosphate dehydrogenase
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D-sorbitol-6-phosphate dehydrogenase
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S6PDH
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sorbitol-6-phosphate dehydrogenase
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sorbitol-6-phosphate dehydrogenase
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similar enzyme also named sorbitol-6-phosphate dehydrogenase catalyzes following reaction: sorbitol-6-phosphate + NADP+ = glucose 6-phosphate + NADPH
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strain LJ378
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UniProt
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enzyme induced by growth on D-sorbitol
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UniProt
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UniProt
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UniProt
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UniProt
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UniProt
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UniProt
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transgenic tobacco expressing Stpd 1 from apple
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fragment
UniProt
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enzyme induced by growth on sorbitol
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strain LJ378
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strain O157:H7 with a temperature-sensitive enzyme, strains grown at 40°C with much lower activity than them grown at 30°C
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ATCC 334 and BL23
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gene gutF
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Borkh. cv. 'Orin'
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cultivar Skala
UniProt
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D-dulcitol 6-phosphate + NAD+
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at 3% of reaction reaction with sorbitol 6-phosphate
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D-fructose 6-phosphate + NADH
D-sorbitol 6-phosphate + NAD+
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D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
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sorbitol is not detected when Stl6PDH is not overexpressed
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
mannitol 1-phosphate + NAD+
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at 1-5% of reaction with sorbitol 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for NAD+
high specificity for D-fructose 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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equilibrium far on the side of sorbitol 6-phosphate formation
high specificity for D-fructose 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for D-sorbitol 6-phosphate
high specificity for D-fructose 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for NAD+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for D-sorbitol 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for NAD+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for D-sorbitol 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for NAD+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for D-sorbitol 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for D-sorbitol 6-phosphate
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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hexitol catabolic enzyme
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D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
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D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
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key enzyme in the regulation of the sorbitol/sucrose ratio in apple leaves
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D-fructose 6-phosphate + NADH
D-sorbitol 6-phosphate + NAD+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
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key enzyme in the regulation of the sorbitol/sucrose ratio in apple leaves
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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hexitol catabolic enzyme
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NAD+
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inhibited by alteration of the 6-amino position of the adenine moiety of NAD+
NAD+
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inhibited by alteration of the 6-amino position of the adenine moiety of NAD+; specific for
NADH
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specific for
additional information
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no activity with NADP+
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additional information
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no activity with NADP+
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3-(5-((E)-[3,5-bis(methoxycarbonyl)phenyl]diazenyl)-2-hydroxyphenyl)propanoic acid
enzyme inhibition is accompanied by a decrease in total prostaglandin F2alpha
5-([5-(3-chlorophenyl)furan-2-yl]methyl)-1,3-thiazolidine-2,4-dione
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5-phospho-D-arabinonate
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substrate analogue inhibitor, IC50: 0.048 mM
5-phospho-D-arabinonohydroxamic acid
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substrate analogue inhibitor, IC50: 0.040 mM
D-mannose 6-phosphate
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potent inhibitor, IC50: 0.0075 mM
diethyl dicarbonate
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100% inactivation
disodium 4-(5-[(Z)-(4-oxido-2-oxo-1,3-thiazol-5(2H)-ylidene)methyl]furan-2-yl)benzoate
reduces deactivated prostaglandin F2alpha metabolite production in outer root sheath keratinocyte supernatant
ethyl 3-(5-[(2,4-dioxo-1,3-thiazolidin-5-yl)methyl]furan-2-yl)benzoate
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methyl 3-(3,5-dihydroxyphenyl)-2-(4-hydroxyphenyl)propanoate
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N-ethylmaleimide
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about 90% inactivation
NADH
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high concentrations of
additional information
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gut genes are repressed by glucose
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additional information
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gut genes are induced by sorbitol. GutR codes for a transcriptional activator of gut genes
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0.568 - 10.5
D-fructose 6-phosphate
3.3
D-sorbitol 6-phosphate
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2.8 - 7.8
fructose 6-phosphate
0.04 - 6.25
sorbitol 6-phosphate
additional information
additional information
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overview: various buffers, various substrate concentrations
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0.568
D-fructose 6-phosphate
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pH 7.5, 25°C, recombinant enzyme
10.5
D-fructose 6-phosphate
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2.8 - 3
fructose 6-phosphate
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+ 0.43 mM NADH, phosphate buffer
7.5 - 7.8
fructose 6-phosphate
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+ 1.08 mM NADH, phosphate buffer
0.07 - 0.08
NAD+
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0.11-0.45 mM NAD+, Tris-HCl buffer
0.19 - 0.21
NAD+
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0.11-0.45 mM NAD+, glycine-NaOH buffer
0.2 - 0.25
NAD+
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0.45-4.5 mM NAD+, Tris-HCl buffer
0.74 - 0.84
NAD+
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0.45-4.5 mM NAD+, glycine-NaOH buffer
0.02 - 0.03
NADH
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phosphate buffer
0.025
NADH
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pH 7.5, 25°C, recombinant enzyme
0.04 - 0.05
sorbitol 6-phosphate
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Tris-HCl buffer
0.4 - 0.44
sorbitol 6-phosphate
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glycine-NaOH buffer
6.25
sorbitol 6-phosphate
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0.00015
3-(5-((E)-[3,5-bis(methoxycarbonyl)phenyl]diazenyl)-2-hydroxyphenyl)propanoic acid
Pyrus pyrifolia
Q6L5U3
pH 7.5, 37°C
0.0051
5-([5-(3-chlorophenyl)furan-2-yl]methyl)-1,3-thiazolidine-2,4-dione
Pyrus pyrifolia
Q6L5U3
pH 7.5, 37°C
0.048
5-phospho-D-arabinonate
Escherichia coli
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substrate analogue inhibitor, IC50: 0.048 mM
0.04
5-phospho-D-arabinonohydroxamic acid
Escherichia coli
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substrate analogue inhibitor, IC50: 0.040 mM
0.0075
D-mannose 6-phosphate
Escherichia coli
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potent inhibitor, IC50: 0.0075 mM
0.0003
disodium 4-(5-[(Z)-(4-oxido-2-oxo-1,3-thiazol-5(2H)-ylidene)methyl]furan-2-yl)benzoate
Pyrus pyrifolia
Q6L5U3
pH 7.5, 37°C
0.0046
ethyl 3-(5-[(2,4-dioxo-1,3-thiazolidin-5-yl)methyl]furan-2-yl)benzoate
Pyrus pyrifolia
Q6L5U3
pH 7.5, 37°C
0.015
methyl 3-(3,5-dihydroxyphenyl)-2-(4-hydroxyphenyl)propanoate
Pyrus pyrifolia
Q6L5U3
pH 7.5, 37°C
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0.182
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strain BL232, grown on lactose, forward reaction
0.222
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strain BL232, grown on lactose, reverse reaction
additional information
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additional information
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additional information
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activities of different recombinant strains
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6.5 - 6.7
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reduction of fructose 6-phosphate, phosphate buffer
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oxidation of sorbitol 6-phosphate, glycine-NaOH buffer
7.5
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assay at
8.5
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oxidation of sorbitol 6-phosphate, Tris-HCl buffer
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5.7 - 7.5
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pH 5.7: about 50% of activity maximum, pH 7.5: about 35% of activity maximum
additional information
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in Tris buffer 32times greater activity than in NaHCO3 buffer
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additional information
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assay at room temperature
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assay at
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similar enzyme also named sorbitol-6-phosphate dehydrogenase from Eriobotrya japonica
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expression of mRNA, no detection of protein or its catalytic activity
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similar enzyme also named sorbitol-6-phosphate dehydrogenase from Eriobotrya japonica
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expression of mRNA, no detection of protein or its catalytic activity
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high level of expression at 30 days after full blooming, expression decreases at 38 days after full blooming and then is maintained at a constant level
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GutM
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26000
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4 * 26000, SDS-PAGE
34900
x * 34900, calculated
74000 - 94000
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gel filtration
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tetramer
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4 * 26000, SDS-PAGE
tetramer
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4 * 26000, SDS-PAGE
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40
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20 min, 85% loss of activity
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60 min, no appreciable loss of activity
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-20°C, more than 4 months, no appreciable loss of activity
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-80°C, 10 mM NaH2PO4 buffer, pH 7.5, 45% glycerol, 10 mM beta-mercaptoethanol
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176.5 fold purification
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approximately 100 fold purification
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GutR and GutM purified on Ni-NTA column
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recombinant enzyme from strain BL21 by ammonium sulfate fractionation and gel filtration
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similar enzyme also named sorbitol-6-phosphate dehydrogenase from Eriobotrya japonica
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using Ni-NTA chromatography
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cloning and subcloning of the gut operon and gutD gene
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constitutive expression in Lactobacillus plantarum
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expressed in Escherichia coli as a His-tagged fusion protein
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expression in host strain using Agrobacterium tumefaciens
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expression of Stpd 1 from apple in transgenic Nicotiana tabacum
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gene Ecs6pdh, overexpression in strain BL21
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gene gutF, construction of an overexpressing strain by gene insertion in the chromosomal lactose operon of strain BL155 resulting in strain BL232, subcloning in Escherichia coli strain DH5alpha
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His-tagged GutR and GutM expressed in Escherichia coli M15(pREP4)
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overexpression of Stl6PDH in lactate dehydrogenase-deficient Lactobacillus plantarum
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S6PDH promoter can be induced by cold, dark, and abscisic acid treatment
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additional information
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mutant with a frameshift in gutR (strain BL285). The mutant loses the ability to ferment sorbitol, and transcription of the gut operon in cells grown with a mixture of ribose plus sorbitol is abolished. Sorbitol uptake rate in strain BL285 is 88fold lower than in the wild-type. GutB mutant (strain BL282) constitutively expresses the gut operon but is impaired in sorbitol uptake. GutM mutant (strain BL286) shows lower levels of gutFRMCBA transcription than the wild-type strain
additional information
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constitutive expression of the two sorbitol-6-phosphate dehydrogenase genes srlD1 and srlD2 in a mutant strain deficient for both L- and D-lactate dehydrogenase activities. Both Stl6PDH enzymes are active, and high specific activity can be detected in the overexpressing strains. Using resting cells under pH control with glucose as a substrate, both Stl6PDHs are capable of rerouting the glycolytic flux from fructose-6-phosphate toward sorbitol production with a remarkably high efficiency of 61 to 65% glucose conversion
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synthesis
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constitutive expression of the two sorbitol-6-phosphate dehydrogenase genes srlD1 and srlD2 in a mutant strain deficient for both L- and D-lactate dehydrogenase activities. Both Stl6PDH enzymes are active, and high specific activity can be detected in the overexpressing strains. Using resting cells under pH control with glucose as a substrate, both Stl6PDHs are capable of rerouting the glycolytic flux from fructose-6-phosphate toward sorbitol production with a remarkably high efficiency of 61 to 65% glucose conversion
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Liss, M.; Horwitz, S.B.; Kaplan, N.O.
D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes
J. Biol. Chem.
237
1342-1350
1962
Klebsiella aerogenes
brenda
Sadegh Roohi, M.; Mitchell, W.J.
Regulation of sorbitol metabolism by glucose in Clostridium pasteurianum: a role for inducer exclusion
J. Gen. Microbiol.
133
2207-2215
1987
Clostridium pasteurianum
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brenda
Dills, S.S.; Seno, S.
Regulation of hexitol catabolism in Streptococcus mutans
J. Bacteriol.
153
861-866
1983
Streptococcus mutans
brenda
Du Toit, P.J.; Kotze, J.P.
The isolation and characterization of sorbitol-6-phosphate dehydrogenase from Clostridium pasteurianum
Biochim. Biophys. Acta
206
333-342
1970
Clostridium pasteurianum
brenda
Horwitz, S.B.
D-mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase from Aerobacter aerogenes
Methods Enzymol.
9
150-155
1966
Klebsiella aerogenes
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Novotny, M.J.; Reizer, J.; Esch, F.; Saier, M.H.
Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-glucitol-6-phosphate dehydrogenase from Escherichia coli
J. Bacteriol.
159
986-990
1984
Escherichia coli, Escherichia coli LJ378
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Hirai, M.
Sorbitol-6-phosphate dehydrogenase from loquat fruit
Plant Physiol.
63
715-717
1979
Eriobotrya japonica
brenda
Hirai, M.
Purification and characteristics of sorbitol-6-phosphate dehydrogenase from loquat leaves
Plant Physiol.
67
221-224
1981
Eriobotrya japonica
brenda
Bouvet, O.M.; Pernoud, S.; Grimont, P.A.
Temperature-dependent fermentation of D-sorbitol in Escherichia coli O157:H7
Appl. Environ. Microbiol.
65
4245-4247
1999
Escherichia coli
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Sheveleva, E.V.; Marquez, S.; Chmara, W.; Zegeer, A.; Jensen, R.G.; Bohnert, H.J.
Sorbitol-6-phosphate dehydrogenase expression in transgenic tobacco. High amounts of sorbitol lead to necrotic lesions
Plant Physiol.
117
831-839
1998
Nicotiana tabacum
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Kanamaru, N.; Ito, Y.; Komori, S.; Saito, M.; Kato, H.; Takahashi, S.; Omura, M.; Soejima, J.; Shiratake, K.; Yamada, K.; Yamaki, S.
Transgenic apple transformed by sorbitol-6-phosphate dehydrogenase cDNA. Switch between sorbitol and sucrose supply due to its gene expression.
Plant Sci.
167
55-61
2004
Malus domestica
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Nissen, L.; Perez-Martinez, G.; Yebra, M.J.
Sorbitol synthesis by an engineered Lactobacillus casei strain expressing a sorbitol-6-phosphate dehydrogenase gene within the lactose operon
FEMS Microbiol. Lett.
249
177-183
2005
Lactobacillus casei
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Roux, C.; Salmon, L.; Verchere-Beaur, C.
Preliminary studies on the inhibition of D-sorbitol-6-phosphate 2-dehydrogenase from Escherichia coli with substrate analogues
J. Enzyme Inhib. Med. Chem.
21
187-192
2006
Escherichia coli
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Ladero, V.; Ramos, A.; Wiersma, A.; Goffin, P.; Schanck, A.; Kleerebezem, M.; Hugenholtz, J.; Smid, E.J.; Hols, P.
High-level production of the low-calorie sugar sorbitol by Lactobacillus plantarum through metabolic engineering
Appl. Environ. Microbiol.
73
1864-1872
2007
Lactobacillus plantarum
brenda
Duangsrisai, S.; Yamada, K.; Bantog, N.A.; Shiratake, K.; Kanayama, Y.; Yamaki, S.
Presence and expression of NAD+-dependent sorbitol dehydrogenase and sorbitol-6-phosphate dehydrogenase genes in strawberry
J. Hortic. Sci. Biotechnol.
82
191-198
2007
Fragaria x ananassa (A7BGM9)
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brenda
Kim, H.; Ahn, J.C.; Choi, J.; Hwang, B.; Choi, D.
Expression and cloning of the full-length cDNA for sorbitol-6-phosphate dehydrogenase and NAD-dependent sorbitol dehydrogenase from pear (Pyrus pyrifolia N.)
Sci. Hortic.
112
406-412
2007
Pyrus pyrifolia (Q6L5U3)
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Alcantara, C.; Sarmiento-Rubiano, L.; Monedero, V.; Deutscher, J.; Perez-Martinez, G.; Yebra, M.
Regulation of Lactobacillus casei sorbitol utilization genes requires DNA-binding transcriptional activator GutR and the conserved protein GutM
Appl. Environ. Microbiol.
74
5731-5740
2008
Lactobacillus casei
brenda
Akinterinwa, O.; Khankal, R.; Cirino, P.
Metabolic engineering for bioproduction of sugar alcohols
Curr. Opin. Biotechnol.
19
461-467
2008
Lactobacillus plantarum
brenda
Liang, D.; Cui, M.; Wu, S.; Ma, F.
Genomic structure, sub-cellular localization, and promoter analysis of the gene encoding sorbitol-6-phosphate dehydrogenase from apple
Plant Mol. Biol. Rep.
30
904-914
2012
Malus domestica
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brenda
Boris, K.; Kudryavtsev, A.; Kochieva, E.
Sorbitol-6-phosphate dehydrogenase (S6PDH) gene polymorphism in Malus Mill. (Rosaceae)
Russ. J. Genet.
51
1069-1074
2015
Malus baccata (A0A0S1TLT7), Malus coronaria (A0A0S1TRV4), Malus domestica (G3FZ80), Malus florentina (A0A0S1TS61), Malus orientalis (A0A0S1TRG0), Malus sikkimensis (A0A0S1TQ28), Malus toringoides (A0A0S1TRT1)
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