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Literature summary for 1.1.1.9 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
Search for more literature for 1.1.1.9

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ almost complete inhibition at 0.5 mM Gluconobacter oxydans
Fe3+ slight inhibition at 0.5 mM Gluconobacter oxydans
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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates at 0.5 mM Gluconobacter oxydans
Mg2+ activates slightly at 0.5 mM Gluconobacter oxydans
Mn2+ activates at 0.5 mM Gluconobacter oxydans
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
Zn2+ activates at 0.5 mM Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
-
-
Gluconobacter oxydans WSH-003
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-mannitol + NAD+ low activity, reaction of EC 1.1.1.67 Gluconobacter oxydans D-fructose + NADH + H+
-
 r
D-mannitol + NAD+ low activity, reaction of EC 1.1.1.67 Gluconobacter oxydans WSH-003 D-fructose + NADH + H+
-
 r
D-sorbitol + NAD+
-
 Gluconobacter oxydans D-fructose + NADH + H+
-
 r
D-sorbitol + NAD+
-
 Gluconobacter oxydans WSH-003 D-fructose + NADH + H+
-
 r
D-sorbose + NADH + H+ low activity Gluconobacter oxydans sorbitol + NAD+
-
 r
glycerol + NAD+ low activity Gluconobacter oxydans glycerone + NADH + H+
-
 r
glycerol + NAD+ low activity Gluconobacter oxydans WSH-003 glycerone + NADH + H+
-
 r
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 ?
-
-
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 ?
-
-
xylitol + NAD+
-
 Gluconobacter oxydans D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Gluconobacter oxydans WSH-003 D-xylulose + NADH + H+
-
 r

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
12
-
-
 Gluconobacter oxydans

pH Range

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

Cofactor

Cofactor Comment Organism Structure
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
NAD+
-
 Gluconobacter oxydans
NADH
-
 Gluconobacter oxydans

General Information

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