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Literature summary for 1.8.1.4 extracted from

  • Kim, H.
    Characterization of a site-specifically modified human dihydrolipoamide dehydrogenase mutant showing significantly changed kinetic properties (2021), J. Korean Chem. Soc., 65, 83-87 .
No PubMed abstract available
Search for more literature for 1.8.1.4

Protein Variants

Protein Variants Comment Organism
P387A the mutation deteriorates severely the catalytic power of the enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.031
-
 dihydrolipoamide mutant enzyme P387A, at pH 8.0 and 37°C Homo sapiens
0.035
-
 NAD+ mutant enzyme P387A, at pH 8.0 and 37°C Homo sapiens
0.19
-
 NAD+ wild type enzyme, at pH 8.0 and 37°C Homo sapiens
0.64
-
 dihydrolipoamide wild type enzyme, at pH 8.0 and 37°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P09622
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer 2 * 50000, SDS-PAGE Homo sapiens
homodimer 2 * 50216, calculated from amino acid sequence Homo sapiens

Synonyms

Synonyms Comment Organism
dihydrolipoamide dehydrogenase
-
 Homo sapiens
dihydrolipoamide:NAD+ oxidoreductase
-
 Homo sapiens
E3
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
116
-
 NAD+ mutant enzyme P387A, at pH 8.0 and 37°C Homo sapiens
116
-
 dihydrolipoamide mutant enzyme P387A, at pH 8.0 and 37°C Homo sapiens
899
-
 NAD+ wild type enzyme, at pH 8.0 and 37°C Homo sapiens
899
-
 dihydrolipoamide wild type enzyme, at pH 8.0 and 37°C Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Homo sapiens
NAD+
-
 Homo sapiens