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Literature summary extracted from
- Characterization of human dihydrolipoamide dehydrogenase mutant with significantly decreased catalytic power (2016), J. Korean Chem. Soc., 60, 378-382 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.1.4 | gene dld, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.4 | additional information | - |
additional information | enzyme kinetic analysis | Homo sapiens | |
| 1.8.1.4 | 0.16 | - |
dihydrolipoamide | enzyme mutant H329A, pH 8.0, 37°C | Homo sapiens |  |
| 1.8.1.4 | 0.19 | - |
dihydrolipoamide | wild-type enzyme, pH 8.0, 37°C | Homo sapiens | |
| 1.8.1.4 | 0.29 | - |
NAD+ | enzyme mutant H329A, pH 8.0, 37°C | Homo sapiens | |
| 1.8.1.4 | 0.64 | - |
NAD+ | wild-type enzyme, pH 8.0, 37°C | Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.8.1.4 | mitochondrion | - |
Homo sapiens | 5739 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.4 | dihydrolipoamide + NAD+ | Homo sapiens | - |
lipoamide + NADH + H+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.4 | Homo sapiens | P09622 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.1.4 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.4 | dihydrolipoamide + NAD+ | - |
Homo sapiens | lipoamide + NADH + H+ | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | homodimer | homodimeric structure model of human E3, PDB ID for 1ZMC | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | dihydrolipoamide dehydrogenase | - |
Homo sapiens |
| 1.8.1.4 | dihydrolipoamide:NAD+ oxidoreductase | - |
Homo sapiens |
| 1.8.1.4 | DLD | - |
Homo sapiens |
| 1.8.1.4 | DLDH | - |
Homo sapiens |
| 1.8.1.4 | E3 | - |
Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.4 | 37 | - |
assay at | Homo sapiens |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.4 | 37 | - |
NAD+ | enzyme mutant H329A, pH 8.0, 37°C | Homo sapiens | |
| 1.8.1.4 | 37 | - |
dihydrolipoamide | enzyme mutant H329A, pH 8.0, 37°C | Homo sapiens | |
| 1.8.1.4 | 899 | - |
NAD+ | wild-type enzyme, pH 8.0, 37°C | Homo sapiens | |
| 1.8.1.4 | 899 | - |
dihydrolipoamide | wild-type enzyme, pH 8.0, 37°C | Homo sapiens | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.4 | 8 | - |
assay at | Homo sapiens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.4 | FAD | one FAD as a prosthetic group at each subunit, binding mode | Homo sapiens | |
| 1.8.1.4 | NAD+ | binding mode | Homo sapiens | |
| 1.8.1.4 | NADH | binding mode | Homo sapiens | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | 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 |
| 1.8.1.4 | additional information | location of residue H329 in human E3 enzyme, structure comparisons with E3 enzymes from other species | Homo sapiens |
| 1.8.1.4 | 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 |
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Release 2023.1 (January 2023)
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