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Literature summary extracted from

  • 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 (2016), Sci. Rep., 6, 33438.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.B60 expressed in Escherichia coli BL21(DE3)-CodonPlus RIL cells Gluconobacter oxydans
1.1.99.21 gene sldh, subcloning in Escherichia coli strain DH5alpha, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)-CodonPlus RIL Gluconobacter oxydans

Protein Variants

EC Number Protein Variants Comment Organism
1.1.99.21 K294Q site-directed mutagenesis, inactive mutant Gluconobacter oxydans
1.1.99.21 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 Gluconobacter oxydans

General Stability

EC Number General Stability Organism
1.1.1.B60 stability of the enzyme 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 Gluconobacter oxydans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.B60 D-sorbitol inhibitory at more than 10% (w/v) Gluconobacter oxydans
1.1.99.21 Ba2+
-
Gluconobacter oxydans
1.1.99.21 Ca2+
-
Gluconobacter oxydans
1.1.99.21 Cu2+
-
Gluconobacter oxydans
1.1.99.21 K+
-
Gluconobacter oxydans
1.1.99.21 additional information EDTA treatment does not affect the initial enzyme activity Gluconobacter oxydans
1.1.99.21 Zn2+
-
Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.B60 38.9
-
D-sorbitol at pH 10.0 and 25°C Gluconobacter oxydans
1.1.99.21 0.0882
-
NADP+ pH 10.0, 25°C Gluconobacter oxydans
1.1.99.21 38.9
-
D-sorbitol pH 10.0, 25°C Gluconobacter oxydans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.B60 Ba2+ activates Gluconobacter oxydans
1.1.1.B60 Ca2+ activates Gluconobacter oxydans
1.1.1.B60 Cu2+ activates Gluconobacter oxydans
1.1.1.B60 K+ activates Gluconobacter oxydans
1.1.1.B60 additional information Mg2+, Co2+, and Mn2+ ions show no stimulatory influence on enzyme activity Gluconobacter oxydans
1.1.1.B60 Zn2+ activates Gluconobacter oxydans
1.1.99.21 additional information Mg2+, Co2+, and Mn2+ ions show no stimulatory influence on GoSLDH activity Gluconobacter oxydans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.B60 54000
-
2 * 54000, SDS-PAGE Gluconobacter oxydans
1.1.99.21 53640
-
-
Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.21 D-sorbitol + NADP+ Gluconobacter oxydans
-
L-sorbose + NADPH
-
r
1.1.99.21 D-sorbitol + NADP+ Gluconobacter oxydans G624
-
L-sorbose + NADPH
-
r
1.1.99.21 additional information Gluconobacter oxydans 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 ?
-
?
1.1.99.21 additional information Gluconobacter oxydans G624 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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.B60 Gluconobacter oxydans
-
-
-
1.1.1.B60 Gluconobacter oxydans G624
-
-
-
1.1.99.21 Gluconobacter oxydans
-
-
-
1.1.99.21 Gluconobacter oxydans G624
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.B60 Ni-NTA column chromatography Gluconobacter oxydans
1.1.99.21 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-CodonPlus RIL Gluconobacter oxydans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.99.21 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 Gluconobacter oxydans
1.1.99.21 3570
-
purified recombinant enzyme, with D-sorbitol using NADP+ as a coenzyme, pH 10.0, 25°C Gluconobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.B60 D-arabinitol + NADP+
-
Gluconobacter oxydans ?
-
?
1.1.1.B60 D-sorbitol + NADP+ best substrate Gluconobacter oxydans L-sorbose + NADPH + H+
-
?
1.1.1.B60 D-sorbitol + NADP+ best substrate Gluconobacter oxydans G624 L-sorbose + NADPH + H+
-
?
1.1.1.B60 mannitol + NADP+
-
Gluconobacter oxydans ?
-
?
1.1.1.B60 additional information no activity is detected with L-arabinitol, xylitol, ribitol, myo-inositol, and glycerol Gluconobacter oxydans ?
-
?
1.1.1.B60 additional information no activity is detected with L-arabinitol, xylitol, ribitol, myo-inositol, and glycerol Gluconobacter oxydans G624 ?
-
?
1.1.99.21 D-sorbitol + NADP+
-
Gluconobacter oxydans L-sorbose + NADPH
-
r
1.1.99.21 D-sorbitol + NADP+
-
Gluconobacter oxydans G624 L-sorbose + NADPH
-
r
1.1.99.21 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 Gluconobacter oxydans ?
-
?
1.1.99.21 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 Gluconobacter oxydans ?
-
?
1.1.99.21 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 Gluconobacter oxydans G624 ?
-
?
1.1.99.21 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 Gluconobacter oxydans G624 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.B60 homodimer 2 * 54000, SDS-PAGE Gluconobacter oxydans
1.1.99.21 dimer
-
Gluconobacter oxydans

Synonyms

EC Number Synonyms Comment Organism
1.1.1.B60 D-sorbitol dehydrogenase (NADP+)
-
Gluconobacter oxydans
1.1.1.B60 D-sorbitol:NADP+ oxidoreductase (L-sorbose-forming)
-
Gluconobacter oxydans
1.1.1.B60 SLDH
-
Gluconobacter oxydans
1.1.99.21 GoSLDH
-
Gluconobacter oxydans
1.1.99.21 SLDH
-
Gluconobacter oxydans
1.1.99.21 sorbitol dehydrogenase
-
Gluconobacter oxydans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.B60 70
-
-
Gluconobacter oxydans
1.1.99.21 70
-
oxidation reaction Gluconobacter oxydans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.B60 25 75 more than 40% activity between 25 and 75°C Gluconobacter oxydans
1.1.99.21 20 80 activity range, profile overview Gluconobacter oxydans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.B60 3820
-
D-sorbitol at pH 10.0 and 25°C Gluconobacter oxydans
1.1.99.21 3820
-
D-sorbitol pH 10.0, 25°C Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.B60 10
-
-
Gluconobacter oxydans
1.1.99.21 10
-
oxidation reaction Gluconobacter oxydans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.99.21 7.5 11 activity range, profile overview Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.B60 NADP+ the enzyme exhibits high preference for NADP+ (vs. 2.5% relative activity with NAD+) Gluconobacter oxydans
1.1.99.21 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+ Gluconobacter oxydans
1.1.99.21 NADP+
-
Gluconobacter oxydans
1.1.99.21 NADPH
-
Gluconobacter oxydans

General Information

EC Number General Information Comment Organism
1.1.99.21 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 Gluconobacter oxydans
1.1.99.21 additional information structure comparisons and molecular docking, overview Gluconobacter oxydans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.B60 98.1
-
D-sorbitol at pH 10.0 and 25°C Gluconobacter oxydans
1.1.99.21 98.1
-
D-sorbitol pH 10.0, 25°C Gluconobacter oxydans