Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Gluconobacter oxydans |
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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00492 | - |
D-sorbitol | pH 12.0, 30°C, recombinant enzyme | Gluconobacter oxydans |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Gluconobacter oxydans | - |
- |
- |
Gluconobacter oxydans WSH-003 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatograpphy and dialysis | Gluconobacter oxydans |
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 | Comment | Organism |
---|---|---|
? | x * 36600, about, sequence calculation, x * 38000, recombinant enzyme, SDS-PAGE | Gluconobacter oxydans |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
57 | - |
- |
Gluconobacter oxydans |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | 70 | over 30% of maximal activity within this range | Gluconobacter oxydans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
12 | - |
- |
Gluconobacter oxydans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
11 | 13 | over 60% of maximal activity within this range | Gluconobacter oxydans |
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 | 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 |