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Literature summary for 1.1.1.431 extracted from

  • Rawat, U.B.; Rao, M.B.
    Purification, kinetic characterization and involvement of tryptophan residue at the NADPH binding site of xylose reductase from Neurospora crassa (1996), Biochim. Biophys. Acta, 1293, 222-230.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-bromosuccinimide NADPH protects Neurospora crassa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
2 * 29000, SDS-PAGE Neurospora crassa
60000
-
gel filtration Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Neurospora crassa

Reaction

Reaction Comment Organism Reaction ID
xylitol + NADP+ = D-xylose + NADPH + H+ kinetic mechanism of xylose reductase is iso-ordered bi bi Neurospora crassa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
72.5
-
-
Neurospora crassa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADPH + H+ kinetic mechanism of xylose reductase is iso-ordered bi bi Neurospora crassa xylitol + NADP+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 29000, SDS-PAGE Neurospora crassa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Neurospora crassa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4638
-
D-xylose pH 6.3, 25°C Neurospora crassa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3
-
assay at Neurospora crassa

Cofactor

Cofactor Comment Organism Structure
NADPH specific for NADPH Neurospora crassa