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Literature summary for 1.8.1.4 extracted from

  • Liu, T.C.; Korotchkina, L.G.; Hyatt, S.L.; Vettakkorumakankav, N.N.; Patel, M.S.
    Spectroscopic studies of the characterization of recombinant human dihydrolipoamide dehydrogenase and its site-directed mutants (1995), J. Biol. Chem., 270, 15545-15550.
    View publication on PubMed
Search for more literature for 1.8.1.4

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes K37E, H452Q and E457Q Homo sapiens
wild-type and mutant enzymes K37E, H452Q and E457Q, overexpression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
E457Q molar ratio of FAD to enzyme is 0.9 compared to 1 for the wild-type enzyme, mutation affects the environment surrounding FAD, decrease in efficiency of electron transfer from the reduced flavin to the oxidized substrate Homo sapiens
H452Q molar ratio of FAD to enzyme is 0.94 compared to 1 for the wild-type enzyme, no production of NADH when the enzyme is reduced by dihydrolipoamide, transfer of electrons from the substrate dihydrolipoamide to NAD+ is extremely low Homo sapiens
K37E molar ratio of FAD to enzyme is 0.76 compared to 1 for the wild-type enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
 NAD+ mutant enzyme K37E Homo sapiens
0.32
-
 NAD+ native enzyme and mutant enzyme E457Q Homo sapiens
0.38
-
 NAD+ mutant enzyme H452Q Homo sapiens
0.69
-
 dihydrolipoamide native enzyme Homo sapiens
0.76
-
 dihydrolipoamide mutant enzyme K37E Homo sapiens
2.9
-
 dihydrolipoamide mutant enzyme H457Q Homo sapiens
43.6
-
 dihydrolipoamide mutant enzyme H452Q Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes K37E, H452Q and E457Q Homo sapiens

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD wild-type enzyme contains 1 FAD per subunit, mutant enzyme K37E has about 25% less bound FAD Homo sapiens
NAD+
-
 Homo sapiens