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Literature summary for 1.8.1.4 extracted from

  • Kim, H.
    Characterization of two site-specific mutations in human dihydrolipoamide dehydrogenase (2013), Bull. Korean Chem. Soc., 34, 1621-1622.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
P325A mutation of highly conserved resdue in the central domain, about 150fold decrease in kcat value Homo sapiens
W366A mutation of highly conserved residue. kinetic parameters similar to wild-type Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
NAD+ mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
0.09
-
dihydrolipoamide mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
0.19
-
NAD+ mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
0.19
-
NAD+ wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
0.58
-
dihydrolipoamide mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
0.64
-
dihydrolipoamide wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydrolipoamide + NAD+
-
Homo sapiens lipoamide + NADH + H+
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6
-
dihydrolipoamide mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
899
-
dihydrolipoamide wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens
1032
-
dihydrolipoamide mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA Homo sapiens