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1-(2-hydroxyethyl)amino-1-deoxy-D-sorbitol + acceptor
6-(2-hydroxyethyl)amino-6-deoxy-L-sorbose + reduced acceptor
1-benzyloxycarbonylamino-1-deoxy-D-sorbitol + acceptor
N-benzyloxycarbonyl-6-amino-L-sorbose + reduced acceptor
-
-
-
-
?
D-arabitol + acceptor
D-xylulose + reduced acceptor
-
-
-
-
?
D-glucitol + NAD+
D-fructose + NADH + H+
D-gluconate + acceptor
5-keto-D-gluconate + reduced acceptor
-
-
-
-
?
D-mannitol + acceptor
? + reduced acceptor
-
oxidation at 5% the rate of D-sorbitol
-
-
?
D-mannitol + acceptor
D-fructose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
D-sorbitol + NADP+
L-sorbose + NADPH
D-sorbitol + phenazine methosulfate
?
-
the catalytic reaction follows an ordered Bi Bi mechanism, the native mSLDH bears two different substrate-binding sites, one for ubiquinone using as electron acceptor and the other for D-sorbitol, in addition to PQQ-binding and Mg2+-binding sites in the catalytic center
-
-
?
D-sorbitol + ubiquinone-2
?
-
-
-
-
?
glycerol + acceptor
dihydroxyacetone + reduced acceptor
-
-
-
-
?
L-glucitol + NAD+
D-sorbose + NADH + H+
meso-erythritol + acceptor
L-erythrulose + reduced acceptor
-
-
-
-
?
ribitol + acceptor
? + reduced acceptor
-
-
-
-
?
additional information
?
-
1-(2-hydroxyethyl)amino-1-deoxy-D-sorbitol + acceptor
6-(2-hydroxyethyl)amino-6-deoxy-L-sorbose + reduced acceptor
-
-
-
-
?
1-(2-hydroxyethyl)amino-1-deoxy-D-sorbitol + acceptor
6-(2-hydroxyethyl)amino-6-deoxy-L-sorbose + reduced acceptor
-
-
-
-
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
production of L-sorbose is similar in the wild-type strain and the FAD-SLDH defective strain, the enzyme is induced by L-sorbose and by D-sorbitol, FAD-SLDH links preferably to the cyanide-insensitive terminal oxidase
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
production of L-sorbose is similar in the wild-type strain and the FAD-SLDH defective strain, the enzyme is induced by L-sorbose and by D-sorbitol, FAD-SLDH links preferably to the cyanide-insensitive terminal oxidase
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
high specificity
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
high specificity, the following dyes act in vitro as acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, potassium ferricyanide, nitro blue tetrazolium or tetramethyl-p-phenylenediamine
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
the oxidation product accumulates in the culture medium
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
the oxidation product accumulates in the culture medium
-
?
D-sorbitol + NADP+
L-sorbose + NADPH
-
-
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH
-
-
-
-
r
L-glucitol + NAD+
D-sorbose + NADH + H+
-
90% conversion
-
-
?
L-glucitol + NAD+
D-sorbose + NADH + H+
-
90% conversion
-
-
?
additional information
?
-
-
no oxidation of D-arabitol, L-iditol, meso-erythritol, galactitol, dulcitol, ribitol, xylitol
-
-
?
additional information
?
-
-
no oxidation of D-arabitol, L-iditol, meso-erythritol, galactitol, dulcitol, ribitol, xylitol
-
-
?
additional information
?
-
-
production of 5-keto-D-gluconate is solely dependent on enzyme
-
-
?
additional information
?
-
-
this SLDH is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry shows that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirms a higher turnover rate
-
-
?
additional information
?
-
-
binding mode of D-sorbitol with sorbitol dehydrogenase using QM-polarized ligand docking and molecular dynamics simulations, His302, Met366, and Asp368 actively participate in D-sorbitol binding, H302 directly forms hydrogen bonds with D-sorbitol and the role of His302 is to hold the D-sorbitol, overview
-
-
?
additional information
?
-
-
GoSLDH is highly specific towards D-sorbitol, mannitol, and D-arabinitol (Table S2). No activity is detected with L-arabinitol, xylitol, ribitol, myo-inositol, and glycerol
-
-
?
additional information
?
-
-
this SLDH is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry shows that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirms a higher turnover rate
-
-
?
additional information
?
-
-
GoSLDH is highly specific towards D-sorbitol, mannitol, and D-arabinitol (Table S2). No activity is detected with L-arabinitol, xylitol, ribitol, myo-inositol, and glycerol
-
-
?
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D-glucitol + NAD+
D-fructose + NADH + H+
D-sorbitol + acceptor
L-sorbose + reduced acceptor
D-sorbitol + NADP+
L-sorbose + NADPH
L-glucitol + NAD+
D-sorbose + NADH + H+
additional information
?
-
D-glucitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
-
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
high specificity
-
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
the oxidation product accumulates in the culture medium
-
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
the oxidation product accumulates in the culture medium
-
?
D-sorbitol + NADP+
L-sorbose + NADPH
-
-
-
-
r
D-sorbitol + NADP+
L-sorbose + NADPH
-
-
-
-
r
L-glucitol + NAD+
D-sorbose + NADH + H+
-
90% conversion
-
-
?
L-glucitol + NAD+
D-sorbose + NADH + H+
-
90% conversion
-
-
?
additional information
?
-
-
production of 5-keto-D-gluconate is solely dependent on enzyme
-
-
?
additional information
?
-
-
this SLDH is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry shows that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirms a higher turnover rate
-
-
?
additional information
?
-
-
this SLDH is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry shows that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirms a higher turnover rate
-
-
?
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K294Q
-
site-directed mutagenesis, inactive mutant
K294Q
-
site-directed mutagenesis, inactive mutant
-
additional information
-
enzyme disruption mutant, oxidation activity against D-arabitol, D-sorbitol, D-mannitol, ribitol, meso-erythritol and glycerol are diminished
additional information
method evaluation and optimization for engineered L-sorbose production in Gluconobater oxydans by self-overexpressing the sldhAB gene in Gluconobacter oxydans strain WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose are enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of Gluconobacter oxydans-sldhAB6 cells further improves the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation. Immobilization of recombinant enzyme in calcium alginate beads, the L-sorbose titer is improved by 33.7% by the immobilization of sldhAB6 cells
additional information
-
method evaluation and optimization for engineered L-sorbose production in Gluconobater oxydans by self-overexpressing the sldhAB gene in Gluconobacter oxydans strain WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose are enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of Gluconobacter oxydans-sldhAB6 cells further improves the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation. Immobilization of recombinant enzyme in calcium alginate beads, the L-sorbose titer is improved by 33.7% by the immobilization of sldhAB6 cells
additional information
-
stability of GoSLDH significantly improves up to 13.6fold after cross-linking of immobilized enzyme on silica nanoparticles and retains 62.8% residual activity after 10 cycles of reuse. Covalent immobilization of GoSLDH onto SiO2 nanoparticles: the amino groups of amino acids such as lysine present on the surface of GoSLDH react with the glutaraldehyde activates SiO2 nanoparticles to form covalent bonds during immobilization at pH 7. The IY and IE of GoSLDH immobilized on different silica nanoparticles are in the ranges of 40.4-71.2% and 53.5-76.7%, respectively
additional information
-
stability of GoSLDH significantly improves up to 13.6fold after cross-linking of immobilized enzyme on silica nanoparticles and retains 62.8% residual activity after 10 cycles of reuse. Covalent immobilization of GoSLDH onto SiO2 nanoparticles: the amino groups of amino acids such as lysine present on the surface of GoSLDH react with the glutaraldehyde activates SiO2 nanoparticles to form covalent bonds during immobilization at pH 7. The IY and IE of GoSLDH immobilized on different silica nanoparticles are in the ranges of 40.4-71.2% and 53.5-76.7%, respectively
-
additional information
-
method evaluation and optimization for engineered L-sorbose production in Gluconobater oxydans by self-overexpressing the sldhAB gene in Gluconobacter oxydans strain WSH-003 with an optimal poly(A/T) tail under the constitutive promoter PtufB, the titer and the productivity of L-sorbose are enhanced by 36.3% and 25.0%, respectively, in a 1-L fermenter. Immobilization of Gluconobacter oxydans-sldhAB6 cells further improves the L-sorbose titer by 33.7% after 20 days of semi-continuous fed-batch fermentation. Immobilization of recombinant enzyme in calcium alginate beads, the L-sorbose titer is improved by 33.7% by the immobilization of sldhAB6 cells
-
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pharmacology
-
miglitol (N-hydroxyethyl-1-deoxynojirimycin), a type of hypoglycemic drug works by competitively inhibiting alpha-glucosidase activity to control postprandial blood glucose, can be used in the treatment of type II diabetes mellitus. 6-(N-hydroxyethyl)-amino-6-deoxy-alpha-L-sorbofuranose, is a key intermediate for the synthesis of miglitol, is produced from N-2-hydroxyethyl glucamine (NHEG) by biotransformation with resting cells of Gluconobacter oxydans. Balanced co-expression of both the mSLDH and the PQQ synthases is effective for the industrial production of 6-(N-hydroxyethyl)-amino-6-deoxy-L-sorbofuranose
pharmacology
-
synergistic improvement of PQQ-dependent D-sorbitol dehydrogenase activity from Gluconobacter oxydans for the biosynthesis of miglitol precursor 6-(N-hydroxyethyl)-amino-6-deoxy-alpha-L-sorbofuranose. Miglitol (N-hydroxyethyl-1-deoxynojirimycin) is a pseudomonosaccharide glucosidase inhibitor in the treatment of non-insulin-dependent mellitus
pharmacology
-
synergistic improvement of PQQ-dependent D-sorbitol dehydrogenase activity from Gluconobacter oxydans for the biosynthesis of miglitol precursor 6-(N-hydroxyethyl)-amino-6-deoxy-alpha-L-sorbofuranose. Miglitol (N-hydroxyethyl-1-deoxynojirimycin) is a pseudomonosaccharide glucosidase inhibitor in the treatment of non-insulin-dependent mellitus
-
synthesis
-
production of 6-amino-L-sorbose, which is an intermediate in the miglitol production and an intermediate for oral alpha-glucosidase-inhibitors
synthesis
the most prominent industrial method of producing L-sorbose is the biotransformation of D-sorbitol to L-sorbose in Gluconobacter species or Acetobacter species. L-sorbose is an important carbohydrate that is predominantly used as a starting material in the biosynthesis of L-ascorbic acid
synthesis
-
biosynthesis of miglitol intermediate 6-(N-hydroxyethyl)-amino-6-deoxy-alpha-L-sorbofuranose by an improved D-sorbitol dehydrogenase from Gluconobacter oxydans. Miglitol (N-hydroxyethyl-1-deoxynojirimycin) is a pseudomonosaccharide alpha-glucosidase inhibitor in the treatment of non-insulin-dependent mellitus
synthesis
-
biosynthesis of miglitol intermediate 6-(N-hydroxyethyl)-amino-6-deoxy-alpha-L-sorbofuranose by an improved D-sorbitol dehydrogenase from Gluconobacter oxydans. Miglitol (N-hydroxyethyl-1-deoxynojirimycin) is a pseudomonosaccharide alpha-glucosidase inhibitor in the treatment of non-insulin-dependent mellitus
-
synthesis
-
the most prominent industrial method of producing L-sorbose is the biotransformation of D-sorbitol to L-sorbose in Gluconobacter species or Acetobacter species. L-sorbose is an important carbohydrate that is predominantly used as a starting material in the biosynthesis of L-ascorbic acid
-
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Shinagawa, E.; Matsushita, K.; Adachi, O.; Ameyama, M.
Purification and characterization of D-sorbitol dehydrogenase from membrane of Gluconobacter suboxydans var. alpha
Agric. Biol. Chem.
46
135-141
1982
Gluconobacter oxydans
-
brenda
Shinagawa, E.; Ameyama, M.
D-Sorbitol dehydrogenase from Gluconobacter suboxydans, membrane-bound
Methods Enzymol.
89
141-145
1982
Gluconobacter oxydans
-
brenda
Matsushita, K.; Fujii, Y.; Ano, Y.; Toyama, H.; Shinjoh, M.; Tomiyama, N.; Miyazaki, T.; Sugisawa, T.; Hoshino, T.; Adachi, O.
5-Keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in Gluconobacter species
Appl. Environ. Microbiol.
69
1959-1966
2003
Gluconobacter oxydans
brenda
Kinast, G.; Schedel, M.
Vierstufige 1-Desoxynojirimycin-Synthese mit einer Biotransformation als zentralem Reaktionsschritt
Angew. Chem.
93
799-800
1981
Gluconobacter oxydans
-
brenda
Toyama, H.; Soemphol, W.; Moonmangmee, D.; Adachi, O.; Matsushita, K.
Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand
Biosci. Biotechnol. Biochem.
69
1120-1129
2005
Gluconobacter frateurii
brenda
Yang, X.P.; Wei, L.J.; Ye, J.B.; Yin, B.; Wei, D.Z.
A pyrroloquinoline quinine-dependent membrane-bound d-sorbitol dehydrogenase from Gluconobacter oxydans exhibits an ordered Bi Bi reaction mechanism
Arch. Biochem. Biophys.
477
206-210
2008
Gluconobacter oxydans
brenda
Soemphol, W.; Adachi, O.; Matsushita, K.; Toyama, H.
Distinct physiological roles of two membrane-bound dehydrogenases responsible for D-sorbitol oxidation in Gluconobacter frateurii
Biosci. Biotechnol. Biochem.
72
842-850
2008
Gluconobacter frateurii
brenda
Yang, X.P.; Wei, L.J.; Lin, J.P.; Yin, B.; Wei, D.Z.
Membrane-bound pyrroloquinoline quinone-dependent dehydrogenase in Gluconobacter oxydans M5, responsible for production of 6-(2-hydroxyethyl) amino-6-deoxy-L-sorbose
Appl. Environ. Microbiol.
74
5250-5253
2008
Gluconobacter oxydans, Gluconobacter oxydans M5
brenda
Soemphol, W.; Saichana, N.; Yakushi, T.; Adachi, O.; Matsushita, K.; Toyama, H.
Characterization of genes involved in D-sorbitol oxidation in thermotolerant Gluconobacter frateurii
Biosci. Biotechnol. Biochem.
76
1497-1505
2012
Gluconobacter frateurii, Gluconobacter frateurii THD32
brenda
Fredslund, F.; Otten, H.; Gemperlein, S.; Poulsen, J.C.; Carius, Y.; Kohring, G.W.; Lo Leggio, L.
Structural characterization of the thermostable Bradyrhizobium japonicum D-sorbitol dehydrogenase
Acta Crystallogr. Sect. F
72
846-852
2016
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA110
brenda
Selvaraj, C.; Krishnasamy, G.; Jagtap, S.; Patel, S.; Dhiman, S.; Kim, T.; Singh, S.; Lee, J.
Structural insights into the binding mode of D-sorbitol with sorbitol dehydrogenase using QM-polarized ligand docking and molecular dynamics simulations
Biochem. Eng. J.
114
244-256
2016
Gluconobacter oxydans
-
brenda
Xu, S.; Wang, X.; Du, G.; Zhou, J.; Chen, J.
Enhanced production of L-sorbose from D-sorbitol by improving the mRNA abundance of sorbitol dehydrogenase in Gluconobacter oxydans WSH-003
Microb. Cell Fact.
13
146
2014
Gluconobacter oxydans (Q70JP0 AND Q70JN9), Gluconobacter oxydans, Gluconobacter oxydans WSH-003 (Q70JP0 AND Q70JN9), Gluconobacter oxydans WSH-003
brenda
Kim, T.S.; Patel, S.K.; Selvaraj, C.; Jung, W.S.; Pan, C.H.; Kang, Y.C.; Lee, J.K.
A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization
Sci. Rep.
6
33438
2016
Gluconobacter oxydans, Gluconobacter oxydans G624
brenda
Ke, X.; Wang, N.N.; Yu, P.H.; Lu, Y.H.; Hu, Z.C.; Zheng, Y.G.
Biosynthesis of miglitol intermediate 6-(N-hydroxyethyl)-amino-6-deoxy-?-l-sorbofuranose by an improved d-sorbitol dehydrogenase from Gluconobacter oxydans
3 Biotech
8
231
2018
Gluconobacter oxydans, Gluconobacter oxydans ZJB16009
brenda
Liu, D.; Ke, X.; Hu, Z.C.; Zheng, Y.G.
Combinational expression of D-sorbitol dehydrogenase and pyrroloquinoline quinone increases 6-(N-hydroxyethyl)-amino-6-deoxy-?-L-sorbofuranose production by Gluconobacter oxydans through cofactor manipulation
Enzyme Microb. Technol.
141
109670
2020
Gluconobacter oxydans
brenda
Ke, X.; Pan-Hong, Y.; Hu, Z.C.; Chen, L.; Sun, X.Q.; Zheng, Y.G.
Synergistic improvement of PQQ-dependent D-sorbitol dehydrogenase activity from Gluconobacter oxydans for the biosynthesis of miglitol precursor 6-(N-hydroxyethyl)-amino-6-deoxy-?-L-sorbofuranose
J. Biotechnol.
300
55-62
2019
Gluconobacter oxydans, Gluconobacter oxydans ZJB-605
brenda