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Literature summary for 1.1.99.21 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
Search for more literature for 1.1.99.21

Cloned(Commentary)

Cloned (Comment) Organism
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

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

Inhibitors

Inhibitors Comment Organism Structure
Ba2+
-
 Gluconobacter oxydans
Ca2+
-
 Gluconobacter oxydans
Cu2+
-
 Gluconobacter oxydans
K+
-
 Gluconobacter oxydans
additional information EDTA treatment does not affect the initial enzyme activity Gluconobacter oxydans
Zn2+
-
 Gluconobacter oxydans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0882
-
 NADP+ pH 10.0, 25°C Gluconobacter oxydans
38.9
-
 D-sorbitol pH 10.0, 25°C Gluconobacter oxydans

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Mg2+, Co2+, and Mn2+ ions show no stimulatory influence on GoSLDH activity Gluconobacter oxydans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53640
-
-
 Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
-
-
Gluconobacter oxydans G624
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-CodonPlus RIL Gluconobacter oxydans

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-sorbitol + NADP+
-
 Gluconobacter oxydans L-sorbose + NADPH
-
 r
D-sorbitol + NADP+
-
 Gluconobacter oxydans G624 L-sorbose + NADPH
-
 r
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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

Subunits Comment Organism
dimer
-
 Gluconobacter oxydans

Synonyms

Synonyms Comment Organism
GoSLDH
-
 Gluconobacter oxydans
SLDH
-
 Gluconobacter oxydans
sorbitol dehydrogenase
-
 Gluconobacter oxydans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 oxidation reaction Gluconobacter oxydans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 80 activity range, profile overview Gluconobacter oxydans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3820
-
 D-sorbitol pH 10.0, 25°C Gluconobacter oxydans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
 oxidation reaction Gluconobacter oxydans

pH Range

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

Cofactor

Cofactor Comment Organism Structure
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
NADP+
-
 Gluconobacter oxydans
NADPH
-
 Gluconobacter oxydans

General Information

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
98.1
-
 D-sorbitol pH 10.0, 25°C Gluconobacter oxydans