Literature summary for 1.1.1.67 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.

Search for more literature for 1.1.1.67

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas fluorescens

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas fluorescens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein	Pseudomonas fluorescens

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
MDH	-	Pseudomonas fluorescens

Turnover Number [1/s]

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

pH Optimum

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

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Release 2023.1 (January 2023)