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Literature summary extracted from

  • Liu, L.; Zeng, W.; Du, G.; Chen, J.; Zhou, J.
    Identification of NAD-dependent xylitol dehydrogenase from Gluconobacter oxydans WSH-003 (2019), ACS omega, 4, 15074-15080 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.9 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Gluconobacter oxydans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.9 Cu2+ almost complete inhibition at 0.5 mM Gluconobacter oxydans
1.1.1.9 Fe3+ slight inhibition at 0.5 mM Gluconobacter oxydans
1.1.1.9 additional information 5 mM EDTA elicits no obvious effect on NAD-dependent xylitol dehydrogenase 2, indicating that the enzyme does not require a chelator for its activity Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.9 0.00492
-
 D-sorbitol pH 12.0, 30°C, recombinant enzyme Gluconobacter oxydans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.9 Co2+ activates at 0.5 mM Gluconobacter oxydans
1.1.1.9 Mg2+ activates slightly at 0.5 mM Gluconobacter oxydans
1.1.1.9 Mn2+ activates at 0.5 mM Gluconobacter oxydans
1.1.1.9 additional information no significant effect by Ni2+, Ca2+, Fe2+, and Cr3+ at 0.5 mM. 5 mM EDTA elicits no obvious effect on NAD-dependent xylitol dehydrogenase 2, indicating that the enzyme does not require a chelator for its activity Gluconobacter oxydans
1.1.1.9 Zn2+ activates at 0.5 mM Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.9 xylitol + NAD+ Gluconobacter oxydans
-
 D-xylulose + NADH + H+
-
 r
1.1.1.9 xylitol + NAD+ Gluconobacter oxydans WSH-003
-
 D-xylulose + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.9 Gluconobacter oxydans
-
-
-
1.1.1.9 Gluconobacter oxydans WSH-003
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.9 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatograpphy and dialysis Gluconobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.9 D-mannitol + NAD+ low activity, reaction of EC 1.1.1.67 Gluconobacter oxydans D-fructose + NADH + H+
-
 r
1.1.1.9 D-mannitol + NAD+ low activity, reaction of EC 1.1.1.67 Gluconobacter oxydans WSH-003 D-fructose + NADH + H+
-
 r
1.1.1.9 D-sorbitol + NAD+
-
 Gluconobacter oxydans D-fructose + NADH + H+
-
 r
1.1.1.9 D-sorbitol + NAD+
-
 Gluconobacter oxydans WSH-003 D-fructose + NADH + H+
-
 r
1.1.1.9 D-sorbose + NADH + H+ low activity Gluconobacter oxydans sorbitol + NAD+
-
 r
1.1.1.9 glycerol + NAD+ low activity Gluconobacter oxydans glycerone + NADH + H+
-
 r
1.1.1.9 glycerol + NAD+ low activity Gluconobacter oxydans WSH-003 glycerone + NADH + H+
-
 r
1.1.1.9 additional information the enzyme shows high activity to convert D-sorbitol to D-fructose. The enzyme is highly specific toward D-sorbitol and xylitol, but shows limited activity toward D-mannitol, sorbose, and glycerol. The enzyme shows no activity when glucose, inositol, galactose, mannose, rhamnose, xylose, fructose, glucuronic acid, glucolactone, 2-oxo-L-gulonic acid (2-KLG), gluconic, propanol, isopropanol, methanol, and ethanol are used as substrates Gluconobacter oxydans ?
-
-
1.1.1.9 additional information the enzyme shows high activity to convert D-sorbitol to D-fructose. The enzyme is highly specific toward D-sorbitol and xylitol, but shows limited activity toward D-mannitol, sorbose, and glycerol. The enzyme shows no activity when glucose, inositol, galactose, mannose, rhamnose, xylose, fructose, glucuronic acid, glucolactone, 2-oxo-L-gulonic acid (2-KLG), gluconic, propanol, isopropanol, methanol, and ethanol are used as substrates Gluconobacter oxydans WSH-003 ?
-
-
1.1.1.9 xylitol + NAD+
-
 Gluconobacter oxydans D-xylulose + NADH + H+
-
 r
1.1.1.9 xylitol + NAD+
-
 Gluconobacter oxydans WSH-003 D-xylulose + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.9 ? x * 36600, about, sequence calculation, x * 38000, recombinant enzyme, SDS-PAGE Gluconobacter oxydans

Synonyms

EC Number Synonyms Comment Organism
1.1.1.9 NAD-dependent xylitol dehydrogenase
-
 Gluconobacter oxydans
1.1.1.9 nicotinamide adenine dinucleotide-dependent xylitol dehydrogenase 2
-
 Gluconobacter oxydans
1.1.1.9 xylitol dehydrogenase 2
-
 Gluconobacter oxydans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.9 57
-
-
 Gluconobacter oxydans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.9 45 70 over 30% of maximal activity within this range Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.9 12
-
-
 Gluconobacter oxydans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.9 11 13 over 60% of maximal activity within this range Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.9 additional information the enzyme exhibits high preference for NAD+ as the cofactor, while no activity with NADP+, FAD, or pyrroloquinoline quinone is observed Gluconobacter oxydans
1.1.1.9 NAD+
-
 Gluconobacter oxydans
1.1.1.9 NADH
-
 Gluconobacter oxydans

General Information

EC Number General Information Comment Organism
1.1.1.9 evolution the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family Gluconobacter oxydans