EC Number   |
Natural Substrates |
|---|
    1.8.1.4 | alpha-lipoamide + NADH + H+ |
- |
| 1.8.1.4 | dihydrolipoamide + NAD+ |
- |
| 1.8.1.4 | dihydrolipoamide + NAD+ |
regulation of activity dependent on tyrosine-phosphorylation of the enzyme |
| 1.8.1.4 | dihydrolipoamide + NAD+ |
the forward reaction is the physiological one |
| 1.8.1.4 | lipoamide + NADH + H+ |
- |
| 1.8.1.4 | more |
the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system |
| 1.8.1.4 | more |
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids |
| 1.8.1.4 | more |
the physiological substrates are the dihydrolipoyl domain of the E2 component, dihydrolipoyl acyltransferase, of the 2-oxoacid dehydrogenase multienzyme complexs or the dihydrolipoyl H-protein of the mitochobdrial glycine decarboxylase |
| 1.8.1.4 | more |
lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport |
| 1.8.1.4 | more |
LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase |
