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Literature summary extracted from

  • Liu, T.C.; Soo Hong, Y.; Korotchkina, L.G.; Vettakkorumakankav, N.N.; Patel, M.S.
    Site-directed mutagenesis of human dihydrolipoamide dehydrogenase: role of lysine-54 and glutamate-192 in stabilizing the thiolate-FAD intermediate (1999), Protein Expr. Purif., 16, 27-39.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.4 wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q, overexpression in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 E192Q specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced Homo sapiens
1.8.1.4 K54E about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-value for lipoamide is increased by about twofold Homo sapiens
1.8.1.4 S53K/K54S about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced. The catalytic rate constant, turnover number/Km, is significantly lower than wild-type Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.4 0.05
-
 dihydrolipoamide mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 0.071
-
 NADH mutant enzyme E192Q Homo sapiens
1.8.1.4 0.12
-
 dihydrolipoamide mutant enzyme E192Q Homo sapiens
1.8.1.4 0.13
-
 NADH mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 0.31
-
 NAD+ mutant enzyme E192Q Homo sapiens
1.8.1.4 0.31
-
 Lipoamide mutant enzyme E192Q Homo sapiens
1.8.1.4 0.4
-
 NAD+ wild-type enzyme Homo sapiens
1.8.1.4 0.55
-
 NAD+ mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 0.63
-
 Lipoamide mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 0.88
-
 dihydrolipoamide wild-type enzyme Homo sapiens
1.8.1.4 2.25
-
 Lipoamide wild-type enzyme Homo sapiens
1.8.1.4 5
-
 Lipoamide mutant enzyme K54E Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q Homo sapiens

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.4 6.75
-
 NAD+ mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 8.5
-
 dihydrolipoamide mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 14.4
-
 Lipoamide mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 19.8
-
 NADH mutant enzyme S53K/K54S Homo sapiens
1.8.1.4 23
-
 Lipoamide mutant enzyme K54E Homo sapiens
1.8.1.4 26.2
-
 NADH mutant enzyme E192Q Homo sapiens
1.8.1.4 29.7
-
 dihydrolipoamide mutant enzyme E192Q Homo sapiens
1.8.1.4 30
-
 NAD+ mutant enzyme E192Q Homo sapiens
1.8.1.4 81.3
-
 Lipoamide mutant enzyme E192Q Homo sapiens
1.8.1.4 340
-
 NADH wild-type enzyme Homo sapiens
1.8.1.4 567
-
 dihydrolipoamide wild-type enzyme Homo sapiens
1.8.1.4 574
-
 NAD+ wild-type enzyme Homo sapiens
1.8.1.4 649
-
 Lipoamide wild-type enzyme Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD Homo sapiens
1.8.1.4 NAD+
-
 Homo sapiens