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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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EC NUMBER 
COMMENTARY 
1.1.1.140
-
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RECOMMENDED NAME
GeneOntology No.
sorbitol-6-phosphate 2-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-69-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
similar enzyme also named sorbitol-6-phosphate dehydrogenase catalyzes following reaction: sorbitol-6-phosphate + NADP+ = glucose 6-phosphate + NADPH
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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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-
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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-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 + H+
D-sorbitol 6-phosphate + NAD+
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sorbitol is not detected when Stl6PDH is not overexpressed
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-
?
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
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
equilibrium far on the side of sorbitol 6-phosphate formation
high specificity for D-fructose 6-phosphate
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for D-sorbitol 6-phosphate
high specificity for D-fructose 6-phosphate
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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high specificity for NAD+
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-
r
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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r
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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-
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
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-
-
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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+
-
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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key enzyme in the regulation of the sorbitol/sucrose ratio in apple leaves
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-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-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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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-phospho-D-arabinonohydroxamic acid
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substrate analogue inhibitor, IC50: 0.040 mM
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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overview: various buffers, various substrate concentrations
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
substrate analogue inhibitor, IC50: 0.048 mM
0.04
5-phospho-D-arabinonohydroxamic acid
Escherichia coli
-
substrate analogue inhibitor, IC50: 0.040 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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
in Tris buffer 32times greater activity than in NaHCO3 buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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similar enzyme also named sorbitol-6-phosphate dehydrogenase from Eriobotrya japonica
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
expression of mRNA, no detection of protein or its catalytic activity
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 10 mM NaH2PO4 buffer, pH 7.5, 45% glycerol, 10 mM beta-mercaptoethanol
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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overexpression of Stl6PDH in lactate dehydrogenase-deficient Lactobacillus plantarum
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.140)
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