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D-dulcitol 6-phosphate + NAD+
?
-
at 3% of reaction reaction with sorbitol 6-phosphate
-
-
?
D-fructose 6-phosphate + NADH
D-sorbitol 6-phosphate + NAD+
-
-
-
-
r
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
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+
?
-
at 1-5% of reaction with sorbitol 6-phosphate
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
the enzyme is much faster at oxidizing D-sorbitol 6-phosphate than in reducing D-fructose 6-phosphate, however, equilibrium analysis reveals that only part of the D-sorbitol 6-phosphate present in the in vitro environment is converted into D-fructose 6-phosphate
-
-
r
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
the enzyme is much faster at oxidizing D-sorbitol 6-phosphate than in reducing D-fructose 6-phosphate, however, equilibrium analysis reveals that only part of the D-sorbitol 6-phosphate present in the in vitro environment is converted into D-fructose 6-phosphate
-
-
r
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
AAV45891.1
-
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
AAV45891.1
the recombinant enzyme (HmS6PDH) has no activity to glucose or sorbitol
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
AAV45891.1
-
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
AAV45891.1
the recombinant enzyme (HmS6PDH) has no activity to glucose or sorbitol
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
-
sorbitol is not detected when Stl6PDH is not overexpressed
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
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+
in the plant pathogen Erwinia amylovora the enzyme (S6PDH, SrlD) is used by the bacterium to utilize sorbitol, which is used for carbohydrate transport in the host plants belonging to the Amygdaloideae subfamily (e.g., apple, pear, and quince)
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
the enzyme is much faster at oxidizing D-sorbitol 6-phosphate than in reducing D-fructose 6-phosphate, however, equilibrium analysis reveals that only part of the D-sorbitol 6-phosphate present in the in vitro environment is converted into D-fructose 6-phosphate
-
-
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
in the plant pathogen Erwinia amylovora the enzyme (S6PDH, SrlD) is used by the bacterium to utilize sorbitol, which is used for carbohydrate transport in the host plants belonging to the Amygdaloideae subfamily (e.g., apple, pear, and quince)
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
the enzyme is much faster at oxidizing D-sorbitol 6-phosphate than in reducing D-fructose 6-phosphate, however, equilibrium analysis reveals that only part of the D-sorbitol 6-phosphate present in the in vitro environment is converted into D-fructose 6-phosphate
-
-
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for NAD+
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for D-sorbitol 6-phosphate
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for NAD+
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for D-sorbitol 6-phosphate
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for NAD+
-
-
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for D-sorbitol 6-phosphate
-
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
high specificity for D-sorbitol 6-phosphate
-
-
r
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
hexitol catabolic enzyme
-
?
D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
-
-
-
?
D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
key enzyme in the regulation of the sorbitol/sucrose ratio in apple leaves
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose 6-phosphate + NADH
D-sorbitol 6-phosphate + NAD+
-
-
-
-
r
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NADP+
D-fructose 6-phosphate + NADPH + H+
-
key enzyme in the regulation of the sorbitol/sucrose ratio in apple leaves
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
AAV45891.1
-
-
-
?
D-fructose 6-phosphate + NADH + H+
D-sorbitol 6-phosphate + NAD+
AAV45891.1
-
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
in the plant pathogen Erwinia amylovora the enzyme (S6PDH, SrlD) is used by the bacterium to utilize sorbitol, which is used for carbohydrate transport in the host plants belonging to the Amygdaloideae subfamily (e.g., apple, pear, and quince)
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
in the plant pathogen Erwinia amylovora the enzyme (S6PDH, SrlD) is used by the bacterium to utilize sorbitol, which is used for carbohydrate transport in the host plants belonging to the Amygdaloideae subfamily (e.g., apple, pear, and quince)
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
-
-
-
?
D-sorbitol 6-phosphate + NAD+
D-fructose 6-phosphate + NADH + H+
-
hexitol catabolic enzyme
-
?
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.
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.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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.
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
-
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
-
brenda
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
brenda
Hirai, M.
Sorbitol-6-phosphate dehydrogenase from loquat fruit
Plant Physiol.
63
715-717
1979
Rhaphiolepis bibas
brenda
Hirai, M.
Purification and characteristics of sorbitol-6-phosphate dehydrogenase from loquat leaves
Plant Physiol.
67
221-224
1981
Rhaphiolepis bibas
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
brenda
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
brenda
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
brenda
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
Lacticaseibacillus casei
brenda
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
brenda
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
Lactiplantibacillus 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)
-
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)
-
brenda
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
Lacticaseibacillus casei
brenda
Akinterinwa, O.; Khankal, R.; Cirino, P.
Metabolic engineering for bioproduction of sugar alcohols
Curr. Opin. Biotechnol.
19
461-467
2008
Lactiplantibacillus 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
-
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 sikkimensis (A0A0S1TQ28), Malus orientalis (A0A0S1TRG0), Malus toringoides (A0A0S1TRT1), Malus coronaria (A0A0S1TRV4), Eriolobus florentinus (A0A0S1TS61), Malus domestica (G3FZ80)
-
brenda
Gao, J.; Sun, Y.; Zhu, B.; Peng, R.; Wang, B.; Wang, L.; Li, Z.; Chen, L.; Yao, Q.
Ectopic expression of sorbitol-6-phosphate 2-dehydrogenase gene from Haloarcula marismortui enhances salt tolerance in transgenic Arabidopsis thaliana
Acta Physiol. Plant.
40
108
2018
Haloarcula marismortui (AAV45891.1), Haloarcula marismortui ATCC 43049 (AAV45891.1)
-
brenda
Salomone-Stagni, M.; Bartho, J.D.; Kalita, E.; Rejzek, M.; Field, R.A.; Bellini, D.; Walsh, M.A.; Benini, S.
Structural and functional analysis of Erwinia amylovora SrlD. The first crystal structure of a sorbitol-6-phosphate 2-dehydrogenase
J. Struct. Biol.
203
109-119
2018
Erwinia amylovora (D4I194), Erwinia amylovora, Erwinia amylovora CFBP1430 (D4I194)
brenda