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

BRENDA support

Literature summary for 1.1.1.67 extracted from

  • Klimacek, M.; Nidetzky, B.
    Examining the relative timing of hydrogen abstraction steps during NAD+-dependent oxidation of secondary alcohols catalyzed by long-chain D-mannitol dehydrogenase from Pseudomonas fluorescens using pH and kinetic isotope effects (2002), Biochemistry, 41, 10158-10165.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
NADH in 50 mM glycine/NaOH buffer at pH 10.0 Pseudomonas fluorescens
0.093
-
NAD+ in 50 mM glycine/NaOH buffer at pH 10.0 Pseudomonas fluorescens
0.4
-
D-mannitol in 50 mM glycine/NaOH buffer at pH 10.0 Pseudomonas fluorescens
0.44
-
D-fructose in 50 mM glycine/NaOH buffer at pH 10.0 Pseudomonas fluorescens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
1 * 54000 Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose + NADH + H+
-
Pseudomonas fluorescens D-mannitol + NAD+
-
r
D-mannitol + NAD+
-
Pseudomonas fluorescens D-fructose + NADH + H+
-
r

Subunits

Subunits Comment Organism
monomer 1 * 54000 Pseudomonas fluorescens

Synonyms

Synonyms Comment Organism
D-mannitol dehydrogenase
-
Pseudomonas fluorescens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
20
-
D-fructose in 50 mM glycine/NaOH buffer at pH 10.0 Pseudomonas fluorescens
40
-
D-mannitol in 50 mM glycine/NaOH buffer at pH 10.0 Pseudomonas fluorescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
Pseudomonas fluorescens