Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.307 extracted from

  • Zeng, Q.K.; Du, H.L.; Wang, J.F.; Wei, D.Q.; Wang, X.N.; Li, Y.X.; Lin, Y.
    Reversal of coenzyme specificity and improvement of catalytic efficiency of Pichia stipitis xylose reductase by rational site-directed mutagenesis (2009), Biotechnol. Lett., 31, 1025-1029.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Scheffersomyces stipitis

Protein Variants

Protein Variants Comment Organism
K21A strong preference for NADH over NADPH Scheffersomyces stipitis
K21A/N272D catalytic efficiency is almost 9fold that of the K21A mutant and 2fold that of the wild-type enzyme. Strong preference for NADH over NADPH Scheffersomyces stipitis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
NADH mutant K21A/N272D, pH 6.5, 35°C Scheffersomyces stipitis
0.02
-
NADH wild-type, pH 6.5, 35°C Scheffersomyces stipitis
0.03
-
NADH mutant K21A, pH 6.5, 35°C Scheffersomyces stipitis
0.03
-
NADPH wild-type, pH 6.5, 35°C Scheffersomyces stipitis
33
-
D-xylose wild-type, cosubstrate NADPH, pH 6.5, 35°C Scheffersomyces stipitis
67
-
D-xylose mutant K21A/N272D, cosubstrate NADH, pH 6.5, 35°C Scheffersomyces stipitis
67
-
D-xylose wild-type, cosubstrate NADH, pH 6.5, 35°C Scheffersomyces stipitis
167
-
D-xylose mutant K21A, cosubstrate NADH, pH 6.5, 35°C Scheffersomyces stipitis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
x * 36000, SDS-PAGE of recombinant enzyme Scheffersomyces stipitis

Organism

Organism UniProt Comment Textmining
Scheffersomyces stipitis P31867
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Scheffersomyces stipitis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4
-
mutant K21A, substrate NADH, pH 6.5, 35°C Scheffersomyces stipitis
5
-
mutant K21A, substrate NADPH, pH 6.5, 35°C Scheffersomyces stipitis
6.6
-
wild-type, substrate NADH, pH 6.5, 35°C Scheffersomyces stipitis
20.3
-
wild-type, substrate NADPH, pH 6.5, 35°C Scheffersomyces stipitis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylose + NADH + H+
-
Scheffersomyces stipitis xylitol + NAD+
-
?
D-xylose + NADPH + H+
-
Scheffersomyces stipitis xylitol + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 36000, SDS-PAGE of recombinant enzyme Scheffersomyces stipitis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.7
-
NADH mutant K21A, pH 6.5, 35°C Scheffersomyces stipitis
12.7
-
NADH mutant K21A/N272D, pH 6.5, 35°C Scheffersomyces stipitis
13.1
-
NADH wild-type, pH 6.5, 35°C Scheffersomyces stipitis
40.27
-
NADPH wild-type, pH 6.5, 35°C Scheffersomyces stipitis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
146.8
-
NADH mutant K21A, pH 6.5, 35°C Scheffersomyces stipitis
614
-
NADH wild-type, pH 6.5, 35°C Scheffersomyces stipitis
1271
-
NADH mutant K21A/N272D, pH 6.5, 35°C Scheffersomyces stipitis
1592
-
NADPH wild-type, pH 6.5, 35°C Scheffersomyces stipitis