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Literature summary extracted from

  • Horecker, B.L.
    Mannitol dehydrogenase (crystalline) from Lactobacillus brevis (1966), Methods Enzymol., 9, 143-146.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.67
-
Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.67 Levilactobacillus brevis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.67
-
Levilactobacillus brevis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.67 27.3
-
-
Levilactobacillus brevis

Storage Stability

EC Number Storage Stability Organism
1.1.1.67 -16°C, 0.02 M sodium acetate buffer pH 6.0, 1 mM 2-mercaptoethanol, several weeks Levilactobacillus brevis
1.1.1.67 3°C, crystalline enzyme in ammonium sulfate, 2 months Levilactobacillus brevis

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.67 5.3
-
D-fructose reduction Levilactobacillus brevis
1.1.1.67 8.6
-
D-mannitol oxidation Levilactobacillus brevis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.67 6 6.5
-
Levilactobacillus brevis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.67 NAD+
-
Levilactobacillus brevis
1.1.1.67 NADH
-
Levilactobacillus brevis