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Literature summary for 1.8.1.4 extracted from

  • Kim, H.
    Characterization of human dihydrolipoamide dehydrogenase mutant with significantly decreased catalytic power (2016), J. Korean Chem. Soc., 60, 378-382 .
No PubMed abstract available
Search for more literature for 1.8.1.4

Cloned(Commentary)

Cloned (Comment) Organism
gene dld, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha Homo sapiens

Protein Variants

Protein Variants Comment Organism
H329A site-directed mutagenesis, the kcat value of the mutant is significantly decreased by 24fold as compared to the wild-type, indicating that the mutation severely deteriorates the catalytic power of the enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme kinetic analysis Homo sapiens
0.16
-
 dihydrolipoamide enzyme mutant H329A, pH 8.0, 37°C Homo sapiens
0.19
-
 dihydrolipoamide wild-type enzyme, pH 8.0, 37°C Homo sapiens
0.29
-
 NAD+ enzyme mutant H329A, pH 8.0, 37°C Homo sapiens
0.64
-
 NAD+ wild-type enzyme, pH 8.0, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydrolipoamide + NAD+ Homo sapiens
-
 lipoamide + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Homo sapiens P09622
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by nickel affinity chromatography and dialysis Homo sapiens

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer homodimeric structure model of human E3, PDB ID for 1ZMC Homo sapiens

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
37
-
 NAD+ enzyme mutant H329A, pH 8.0, 37°C Homo sapiens
37
-
 dihydrolipoamide enzyme mutant H329A, pH 8.0, 37°C Homo sapiens
899
-
 NAD+ wild-type enzyme, pH 8.0, 37°C Homo sapiens
899
-
 dihydrolipoamide wild-type enzyme, pH 8.0, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD one FAD as a prosthetic group at each subunit, binding mode Homo sapiens
NAD+ binding mode Homo sapiens
NADH binding mode Homo sapiens

General Information

General Information Comment Organism
evolution residue H329 is absolutely conserved, H329 329 is a part of the long alpha-helix 8, which is composed of 16 amino acids and is a component of the central domain. His329 is also located near FAD and the active disulfide center between Cys45 and Cys50, which are essential to the catalytic activity of human E3 Homo sapiens
additional information location of residue H329 in human E3 enzyme, structure comparisons with E3 enzymes from other species Homo sapiens
physiological function E3 is an essential component in pyruvate, 2-oxoglutarate and branched-chain 2-oxo acid dehydrogenase complexes. E3 catalyzes the reoxidation of a dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of the three 2-oxo acid dehydrogenase complexes Homo sapiens