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Literature summary extracted from

  • Verduyn, C.; van Kleef, R.; Frank, J.; Schreuder, H.; van Dijken, J.P.; Scheffers, W.A.
    Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis (1985), Biochem. J., 226, 669-677.
    View publication on PubMedView publication on EuropePMC

Inhibitors

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

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.307 additional information no requirement for divalent cation is observed Scheffersomyces stipitis

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.307 Scheffersomyces stipitis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.307
-
Scheffersomyces stipitis

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.1.1.307 dimer 2 * 34000, SDS-PAGE Scheffersomyces stipitis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.307 NAD(P)H-dependent xylose reductase
-
Scheffersomyces stipitis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.307 6
-
NADH- and NADPH-dependent activity Scheffersomyces stipitis

pH Range

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

Cofactor

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

Ki Value [mM]

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