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Literature summary for 1.8.1.4 extracted from

  • Kawahara, Y.; Misaka, E.; Nakanishi, K.
    Purification and properties of lipoamide dehydrogenase from yeast, Candida krusei (1963), J. Biochem., 63, 77-82.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization by dialysis Pichia kudriavzevii

Inhibitors

Inhibitors Comment Organism Structure
NADH
-
Pichia kudriavzevii

Organism

Organism UniProt Comment Textmining
Pichia kudriavzevii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pichia kudriavzevii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Pichia kudriavzevii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+
-
Pichia kudriavzevii lipoamide + NADH
-
r
methylene blue + NADH
-
Pichia kudriavzevii ? + NAD+
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
-
Pichia kudriavzevii ? + NAD+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
NADH-lipoamide oxidoreductase activity Pichia kudriavzevii
8
-
dihydrolipoamide-NAD+ oxidoreductase activity Pichia kudriavzevii

pH Range

pH Minimum pH Maximum Comment Organism
5.5 7.5 pH 5.5: about 75% of maximal activity, pH 7.5: about 40% of maximal activity, NADH-lipoamide oxidoreductase activity Pichia kudriavzevii
7.5 8.8 pH 7.5: about 50% of maximal activity, pH 8.8: about 60% of maximal activity, dihydrolipoamide-NAD+ oxidoreductase activity Pichia kudriavzevii

Cofactor

Cofactor Comment Organism Structure
FAD 0.01882 mM of FAD per mg of protein Pichia kudriavzevii
NAD+
-
Pichia kudriavzevii
NADH
-
Pichia kudriavzevii