EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.9 | recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Gluconobacter oxydans |
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 |
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 |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.9 | Gluconobacter oxydans | - |
- |
- |
1.1.1.9 | Gluconobacter oxydans WSH-003 | - |
- |
- |
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 |
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 |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.9 | ? | x * 36600, about, sequence calculation, x * 38000, recombinant enzyme, SDS-PAGE | Gluconobacter oxydans |
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 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 57 | - |
- |
Gluconobacter oxydans |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 12 | - |
- |
Gluconobacter oxydans |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 11 | 13 | over 60% of maximal activity within this range | Gluconobacter oxydans |
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 |
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 |