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Information on EC 1.1.99.21 - D-sorbitol dehydrogenase (acceptor)
for references in articles please use BRENDA:EC1.1.99.21
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.99 With unknown physiological acceptors
1.1.99.21 D-sorbitol dehydrogenase (acceptor)
IUBMB Comments
A flavoprotein (FAD).
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
fad-sldh, gosldh, sldhab, msldh, pqq-dependent d-sorbitol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-sorbitol dehydrogenase
FAD-SLDH
GoSLDH
mSLDH
PQQ-dependent D-sorbitol dehydrogenase
SDH
SLDH
sldhAB
sorbitol dehydrogenase
D-sorbitol dehydrogenase
-
membrane-bound FAD-dependent D-sorbitol dehydrogenase FAD-SLDH
D-sorbitol dehydrogenase
-
membrane-bound FAD-dependent D-sorbitol dehydrogenase FAD-SLDH
-
D-sorbitol dehydrogenase
-
membrane-bound pyrroloquinoline quinine dependent, mSLDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-sorbitol + acceptor = L-sorbose + reduced acceptor
-
-
-
-
D-sorbitol + acceptor = L-sorbose + reduced acceptor
a flavoprotein, FAD
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
2-keto-L-gulonate biosynthesis, L-ascorbate biosynthesis III (D-sorbitol pathway)
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SYSTEMATIC NAME
IUBMB Comments
D-sorbitol:acceptor 1-oxidoreductase
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
86178-94-1
not distinguished from EC 1.1.1.15 in Chemical Abstracts
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
Substrates: -
Products: -
Products: -
?
D-arabitol + acceptor
D-xylulose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-gluconate + acceptor
5-keto-D-gluconate + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-mannitol + acceptor
? + reduced acceptor
-
Substrates: oxidation at 5% the rate of D-sorbitol
Products: -
Products: -
?
D-mannitol + acceptor
D-fructose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + phenazine methosulfate
?
-
Substrates: 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
Products: -
Products: -
?
glycerol + acceptor
dihydroxyacetone + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
meso-erythritol + acceptor
L-erythrulose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
1-(2-hydroxyethyl)amino-1-deoxy-D-sorbitol + acceptor
6-(2-hydroxyethyl)amino-6-deoxy-L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
1-(2-hydroxyethyl)amino-1-deoxy-D-sorbitol + acceptor
6-(2-hydroxyethyl)amino-6-deoxy-L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: 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
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: 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
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: high specificity
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: high specificity, the following dyes act in vitro as acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, potassium ferricyanide, nitro blue tetrazolium or tetramethyl-p-phenylenediamine
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
Substrates: D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
Products: the oxidation product accumulates in the culture medium
Products: the oxidation product accumulates in the culture medium
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
Substrates: D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
Products: the oxidation product accumulates in the culture medium
Products: the oxidation product accumulates in the culture medium
?
D-sorbitol + NADP+
L-sorbose + NADPH
-
Substrates: -
Products: -
Products: -
r
L-glucitol + NAD+
D-sorbose + NADH + H+
-
Substrates: 90% conversion
Products: -
Products: -
?
L-glucitol + NAD+
D-sorbose + NADH + H+
-
Substrates: 90% conversion
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of D-arabitol, L-iditol, meso-erythritol, galactitol, dulcitol, ribitol, xylitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of D-arabitol, L-iditol, meso-erythritol, galactitol, dulcitol, ribitol, xylitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of 5-keto-D-gluconate is solely dependent on enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glucitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
-
Substrates: high specificity
Products: -
Products: -
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
Substrates: D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
Products: the oxidation product accumulates in the culture medium
Products: the oxidation product accumulates in the culture medium
?
D-sorbitol + acceptor
L-sorbose + reduced acceptor
Substrates: D-sorbitol is oxidized in the periplasm in a chemo-, regio-, and stereoselective manner to L-sorbose by the membrane-bound dehydrogenase
Products: the oxidation product accumulates in the culture medium
Products: the oxidation product accumulates in the culture medium
?
D-sorbitol + NADP+
L-sorbose + NADPH
-
Substrates: -
Products: -
Products: -
r
L-glucitol + NAD+
D-sorbose + NADH + H+
-
Substrates: 90% conversion
Products: -
Products: -
?
L-glucitol + NAD+
D-sorbose + NADH + H+
-
Substrates: 90% conversion
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of 5-keto-D-gluconate is solely dependent on enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
acts in vitro as acceptor together with phenazine methosulfate
pyrroloquinoline quinone
-
the cofactor transfers redox equivalents to the respiratory chain during the biotransformation of NHEG to 6NSL
cytochrome c
-
tightly bound , dehydrogenase-cytochrome c complex, separable by SDS-PAGE
additional information
-
NAD+, NADP+ or molecular oxygen are completely inactive
-
additional information
-
NAD+, NADP+ or molecular oxygen are completely inactive
-
additional information
-
enzyme GoSLDH exhibits a preference for NADP+ over NAD+ as a coenzyme and is exclusively an NADP+-dependent enzyme showing only 2.5% relative activity with NAD+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Mg2+, Co2+, and Mn2+ ions show no stimulatory influence on GoSLDH activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-sorbose
-
non-competitive inhibition, sorbitol or phenazine methosulfate as substrates
additional information
-
EDTA treatment does not affect the initial enzyme activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
protein-ligand molecular docking and thermodynamics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3570
-
purified recombinant enzyme, with D-sorbitol using NADP+ as a coenzyme, pH 10.0, 25°C
additional information
-
Gluconobacter oxydans G624 shows SLDH activity of 43.2 U/mL and a 20% conversion yield from D-sorbitol to L-sorbose at 18 h of fermentation
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
small and large subunits, SldB and SldA
UniProt
brenda
identical with glycerol dehydrogenase, EC1.1.99.22, and D-arabitol dehydrogenase, EC1.1.1.11
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the membrane-bound dehydrogenase locates on the outer surface of the cytoplasmic membrane. The oxidation products accumulate in the culture medium
brenda
-
the membrane-bound dehydrogenase locates on the outer surface of the cytoplasmic membrane. The oxidation products accumulate in the culture medium
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
mutation of His302 results in the denaturation of protein structure and loss of stability
metabolism
-
membrane-bound D-sorbitol dehydrogenase is involved in the biotransformation of D-sorbitol to L-sorbose
additional information
evolution
-
GoSLDH sequencing, structure analyses, and biochemical studies, suggest that it belongs to the NADP+-dependent polyol specific long-chain sorbitol dehydrogenase family. GoSLDH possesses the active site residues of Asp190, Val228, Lys294, and Asp299 and the conserved catalytic motif (KXXXXHXXH) for polyol-specific long-chain dehydrogenase
evolution
-
GoSLDH sequencing, structure analyses, and biochemical studies, suggest that it belongs to the NADP+-dependent polyol specific long-chain sorbitol dehydrogenase family. GoSLDH possesses the active site residues of Asp190, Val228, Lys294, and Asp299 and the conserved catalytic motif (KXXXXHXXH) for polyol-specific long-chain dehydrogenase
-
additional information
-
sequence alignment-based homology modeling using the structure of NAD-bound sorbitol dehydrogenase, EC 1.1.1.14, with UniProt ID Q9KWR5 as template
additional information
-
structure comparisons and molecular docking, overview
additional information
-
structure comparisons and molecular docking, overview
-
Show AA Sequence and Transmembrane Helices (497 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE
51000
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE
63000
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE
additional information
-
1 * 63000 + 1 * 51000 + 1 * 17000, dissociation into 3 components, a flavoprotein (MW 63000), a cytochrome c (MW 51000) and an unknown polypeptide (MW 17000), SDS-PAGE
additional information
-
structure analysis by QM-polarized ligand docking and molecular dynamics simulations, modelling, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 1.4 M NaH2PO4/K2HPO4 pH 5.6
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K294Q
additional information
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ionic detergents, such as cetylpyridinium chloride, cetyltrimethyl ammonium bromide and sodium stearate, inactivate
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at 80°C for more than two months in the presence of 0.1% Tween-20
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE