EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.307 | dithiothreitol | 1 mM, 25% inhibition | Scheffersomyces stipitis | |
1.1.1.307 | Hg2+ | 0.001 mM, 2 min, complete inhibition | Scheffersomyces stipitis | |
1.1.1.307 | additional information | no effect by 5 mM EDTA, 500 mM sulfate, 5 mM 2-mercaptoethanol | Scheffersomyces stipitis | |
1.1.1.307 | NAD+ | strong inhibition with the NADH-linked reaction, no inhibition of NADPH-linked reaction. NAD+ is a non-competitive inhibitor with respect to xylose and a competitive inhibitor with respect to NADH | Scheffersomyces stipitis | |
1.1.1.307 | NADP+ | potent inhibitor of both the NADPH- and NADH-linked xylose reduction. Competition with NADPH and non-competitive inhibition with xylose in the NADPH-linked xylose reduction | Scheffersomyces stipitis | |
1.1.1.307 | p-chloromercuribenzoate | 0.001 mM, 2 min, complete inhibition | Scheffersomyces stipitis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.307 | 0.0091 | - |
NADPH | - |
Scheffersomyces stipitis | |
1.1.1.307 | 0.021 | - |
NADH | - |
Scheffersomyces stipitis | |
1.1.1.307 | 42 | - |
D-xylose | cofactor: NADH | Scheffersomyces stipitis | |
1.1.1.307 | 42 | - |
D-xylose | cofactor: NADPH | Scheffersomyces stipitis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.307 | additional information | no requirement for divalent cation is observed | Scheffersomyces stipitis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.307 | 34000 | - |
2 * 34000, SDS-PAGE | Scheffersomyces stipitis |
1.1.1.307 | 63000 | 65000 | gel filtration | Scheffersomyces stipitis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.307 | D-xylose + NADPH + H+ | Scheffersomyces stipitis | whereas in most bacteria metabolism of D-xylose proceeds via direct isomerization to D-xylulose, catalysed by xylose isomerase (EC 5.3.1.5), in yeasts this conversion is catalysed by the sequential action of two oxidoreductases: xylose reductase and xylitol dehydrogenase (EC 1.1.1.9) | xylitol + NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.307 | Scheffersomyces stipitis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.307 | - |
Scheffersomyces stipitis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.307 | 16.7 | - |
NADH-dependent activity | Scheffersomyces stipitis |
1.1.1.307 | 23.2 | - |
NADPH-dependent activity | Scheffersomyces stipitis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.307 | D-galactose + NADH + H+ | - |
Scheffersomyces stipitis | ? | - |
? | |
1.1.1.307 | D-galactose + NADPH + H+ | - |
Scheffersomyces stipitis | ? | - |
? | |
1.1.1.307 | D-glucose + NADH + H+ | - |
Scheffersomyces stipitis | ? | - |
? | |
1.1.1.307 | D-glucose + NADPH + H+ | - |
Scheffersomyces stipitis | ? | - |
? | |
1.1.1.307 | D-ribose + NADH + H+ | - |
Scheffersomyces stipitis | ? | - |
? | |
1.1.1.307 | D-ribose + NADPH + H+ | - |
Scheffersomyces stipitis | ? | - |
? | |
1.1.1.307 | D-xylose + NADH + H+ | active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. Rate of xylitol oxidation is 4% of the rate of D-xylose reduction. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol | Scheffersomyces stipitis | xylitol + NAD+ | - |
r | |
1.1.1.307 | D-xylose + NADPH + H+ | whereas in most bacteria metabolism of D-xylose proceeds via direct isomerization to D-xylulose, catalysed by xylose isomerase (EC 5.3.1.5), in yeasts this conversion is catalysed by the sequential action of two oxidoreductases: xylose reductase and xylitol dehydrogenase (EC 1.1.1.9) | Scheffersomyces stipitis | xylitol + NADP+ | - |
? | |
1.1.1.307 | D-xylose + NADPH + H+ | active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. Rate of xylitol oxidation is 5% of the rate of D-xylose reduction. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol | Scheffersomyces stipitis | xylitol + NADP+ | - |
r | |
1.1.1.307 | DL-glyceraldehyde + NADH + H+ | low activity in direction of glycerol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol | Scheffersomyces stipitis | glycerol + NAD+ | - |
r | |
1.1.1.307 | DL-glyceraldehyde + NADPH + H+ | low activity in direction of glycerol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol | Scheffersomyces stipitis | glycerol + NADP+ | - |
r | |
1.1.1.307 | L-arabinose + NADH + H+ | low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol | Scheffersomyces stipitis | arabinitol + NAD+ | - |
r | |
1.1.1.307 | L-arabinose + NADPH + H+ | low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol | Scheffersomyces stipitis | arabinitol + NADP+ | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.307 | dimer | 2 * 34000, SDS-PAGE | Scheffersomyces stipitis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.307 | NAD(P)H-dependent xylose reductase | - |
Scheffersomyces stipitis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.307 | 6 | - |
NADH- and NADPH-dependent activity | Scheffersomyces stipitis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.307 | 5 | 8 | the ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8 | Scheffersomyces stipitis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.307 | NADH | active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. The ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8 | Scheffersomyces stipitis | |
1.1.1.307 | NADPH | active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. The ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8 | Scheffersomyces stipitis |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.307 | 0.006 | - |
NADP+ | concentration of NADH varied | Scheffersomyces stipitis | |
1.1.1.307 | 0.03 | - |
NADP+ | concentration of NADPH varied | Scheffersomyces stipitis | |
1.1.1.307 | 0.13 | - |
NAD+ | concentration of NADH varied | Scheffersomyces stipitis | |
1.1.1.307 | 0.17 | - |
NADP+ | concentration of D-xylose varied | Scheffersomyces stipitis | |
1.1.1.307 | 0.65 | - |
NAD+ | concentration of D-xylose varied | Scheffersomyces stipitis |