Literature summary for 1.1.1.67 extracted from

Horecker, B.L.
Mannitol dehydrogenase (crystalline) from Lactobacillus brevis (1966), Methods Enzymol., 9, 143-146.

No PubMed abstract available

Search for more literature for 1.1.1.67

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-mannitol + NAD+	Levilactobacillus brevis	-	D-fructose + NADH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Levilactobacillus brevis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Levilactobacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
27.3	-	-	Levilactobacillus brevis

Storage Stability

Storage Stability	Organism
-16°C, 0.02 M sodium acetate buffer pH 6.0, 1 mM 2-mercaptoethanol, several weeks	Levilactobacillus brevis
3°C, crystalline enzyme in ammonium sulfate, 2 months	Levilactobacillus brevis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-mannitol + NAD+	-	Levilactobacillus brevis	D-fructose + NADH + H+	-	?
D-mannitol + NAD+	enzyme highly specific for D-mannitol and D-fructose	Levilactobacillus brevis	D-fructose + NADH + H+	-	r

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.3	-	D-fructose reduction	Levilactobacillus brevis
8.6	-	D-mannitol oxidation	Levilactobacillus brevis

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
6	6.5	-	Levilactobacillus brevis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Levilactobacillus brevis
NADH	-	Levilactobacillus brevis

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Release 2023.1 (January 2023)