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Literature summary extracted from

  • Slatner, M.; Nidetzky, B.; Kulbe, K.D.
    Kinetic study of the catalytic mechanism of mannitol dehydrogenase from Pseudomonas fluorescens (1999), Biochemistry, 38, 10489-10498.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.67 expression in Escherichia coli Pseudomonas fluorescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.67 1.2
-
D-mannitol recombinant protein Pseudomonas fluorescens
1.1.1.67 25
-
D-fructose recombinant protein Pseudomonas fluorescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.67 45000
-
recombinant protein, gel filtration Pseudomonas fluorescens
1.1.1.67 54000
-
1 * 54000, SDS-PAGE, recombinant protein   Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.67 Pseudomonas fluorescens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.67 recombinant protein Pseudomonas fluorescens

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.1.1.67 monomer 1 * 54000, SDS-PAGE, recombinant protein   Pseudomonas fluorescens

Synonyms

EC Number Synonyms Comment Organism
1.1.1.67 MDH
-
Pseudomonas fluorescens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.67 20
-
NAD+ recombinant protein Pseudomonas fluorescens
1.1.1.67 54
-
NADH recombinant protein Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.67 7
-
D-fructose reduction, recombinant protein Pseudomonas fluorescens
1.1.1.67 10
-
D-mannitol oxidation, recombinant protein Pseudomonas fluorescens