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Literature summary extracted from
- A pH-dependent kinetic model of dihydrolipoamide dehydrogenase from multiple organisms (2014), Biophys. J., 107, 2993-3007 .
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.8.1.4 | additional information | - |
additional information | kinetic analysis and modelling, detailed overview | Homo sapiens | |
| 1.8.1.4 | additional information | - |
additional information | kinetic analysis and modelling, detailed overview | Spinacia oleracea | |
| 1.8.1.4 | additional information | - |
additional information | kinetic analysis and modelling, detailed overview | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.8.1.4 | mitochondrion | - |
Homo sapiens | 5739 | - |
| 1.8.1.4 | mitochondrion | - |
Spinacia oleracea | 5739 | - |
| 1.8.1.4 | mitochondrion | - |
Escherichia coli | 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 |  |
| 1.8.1.4 | dihydrolipoamide + NAD+ | Spinacia oleracea | - |
lipoamide + NADH + H+ | - |
r | |
| 1.8.1.4 | dihydrolipoamide + NAD+ | Escherichia coli | - |
lipoamide + NADH + H+ | - |
r | |
| 1.8.1.4 | protein N6-(lipoyl)lysine + NADH + H+ | Homo sapiens | - |
protein N6-(dihydrolipoyl)lysine + NAD+ | - |
r | |
| 1.8.1.4 | protein N6-(lipoyl)lysine + NADH + H+ | Spinacia oleracea | - |
protein N6-(dihydrolipoyl)lysine + NAD+ | - |
r | |
| 1.8.1.4 | protein N6-(lipoyl)lysine + NADH + H+ | Escherichia coli | - |
protein N6-(dihydrolipoyl)lysine + NAD+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.4 | Escherichia coli | P0A9P0 | - |
- |
| 1.8.1.4 | Homo sapiens | P09622 | - |
- |
| 1.8.1.4 | Spinacia oleracea | A0A0K9R8G5 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.8.1.4 | protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ | in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Ddihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview | Spinacia oleracea | |
| 1.8.1.4 | protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ | in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Dihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview | Homo sapiens | |
| 1.8.1.4 | protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ | in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Dihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview | Escherichia coli |
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 | |
| 1.8.1.4 | dihydrolipoamide + NAD+ | - |
Spinacia oleracea | lipoamide + NADH + H+ | - |
r | |
| 1.8.1.4 | dihydrolipoamide + NAD+ | - |
Escherichia coli | lipoamide + NADH + H+ | - |
r | |
| 1.8.1.4 | protein N6-(lipoyl)lysine + NADH + H+ | - |
Homo sapiens | protein N6-(dihydrolipoyl)lysine + NAD+ | - |
r | |
| 1.8.1.4 | protein N6-(lipoyl)lysine + NADH + H+ | - |
Spinacia oleracea | protein N6-(dihydrolipoyl)lysine + NAD+ | - |
r | |
| 1.8.1.4 | protein N6-(lipoyl)lysine + NADH + H+ | - |
Escherichia coli | protein N6-(dihydrolipoyl)lysine + NAD+ | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | dihydrolipoamide dehydrogenase | - |
Homo sapiens |
| 1.8.1.4 | dihydrolipoamide dehydrogenase | - |
Spinacia oleracea |
| 1.8.1.4 | dihydrolipoamide dehydrogenase | - |
Escherichia coli |
| 1.8.1.4 | LpdA | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.4 | FAD | flavoenzyme | Homo sapiens | |
| 1.8.1.4 | FAD | flavoenzyme | Spinacia oleracea | |
| 1.8.1.4 | FAD | flavoenzyme | Escherichia coli | |
| 1.8.1.4 | NAD+ | - |
Homo sapiens | |
| 1.8.1.4 | NAD+ | - |
Spinacia oleracea | |
| 1.8.1.4 | NAD+ | - |
Escherichia coli | |
| 1.8.1.4 | NADH | - |
Homo sapiens | |
| 1.8.1.4 | NADH | - |
Spinacia oleracea | |
| 1.8.1.4 | NADH | - |
Escherichia coli | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.1.4 | evolution | dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family | Homo sapiens |
| 1.8.1.4 | evolution | dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family | Spinacia oleracea |
| 1.8.1.4 | evolution | dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family | Escherichia coli |
| 1.8.1.4 | metabolism | dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxoglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions | Homo sapiens |
| 1.8.1.4 | metabolism | dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxoglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions | Escherichia coli |
| 1.8.1.4 | metabolism | dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxooglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions | Spinacia oleracea |
| 1.8.1.4 | physiological function | in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview | Homo sapiens |
| 1.8.1.4 | physiological function | in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview | Spinacia oleracea |
| 1.8.1.4 | physiological function | in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview | Escherichia coli |
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