Literature summary 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.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.1.1.67	0.01	-	NADH	in 50 mM glycine/NaOH buffer at pH 10.0	Pseudomonas fluorescens
1.1.1.67	0.093	-	NAD+	in 50 mM glycine/NaOH buffer at pH 10.0	Pseudomonas fluorescens
1.1.1.67	0.4	-	D-mannitol	in 50 mM glycine/NaOH buffer at pH 10.0	Pseudomonas fluorescens
1.1.1.67	0.44	-	D-fructose	in 50 mM glycine/NaOH buffer at pH 10.0	Pseudomonas fluorescens

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.1.1.67	54000	-	1 * 54000	Pseudomonas fluorescens

Organism

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

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
1.1.1.67	D-mannitol dehydrogenase	-	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	-	D-fructose	in 50 mM glycine/NaOH buffer at pH 10.0	Pseudomonas fluorescens
1.1.1.67	40	-	D-mannitol	in 50 mM glycine/NaOH buffer at pH 10.0	Pseudomonas fluorescens

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.1.1.67	10	-	-	Pseudomonas fluorescens

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Release 2023.1 (January 2023)