KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | transient-state kinetics of reductive and oxidative half-reactions | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced lipoamide + NAD+ | Mycobacterium tuberculosis | enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes | oxidized lipoamide + NADH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ | formation of a FADH2-NAD+ intermediate in catalysis, reaction mechanism of reductive and oxidative half-reactions involving enzyme, FAD/FADH2, and NAD+/NADH | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced lipoamide + NAD+ | - |
Mycobacterium tuberculosis | oxidized lipoamide + NADH | - |
r | |
reduced lipoamide + NAD+ | enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes | Mycobacterium tuberculosis | oxidized lipoamide + NADH | - |
r |
Synonyms | Comment | Organism |
---|---|---|
lipoamide dehydrogenase | - |
Mycobacterium tuberculosis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
assays are performed at 4°C and at 25°C | Mycobacterium tuberculosis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 7.5 | assay at | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis | Mycobacterium tuberculosis | |
additional information | enzyme contains a redox-active disulfide, the cofactor cycles between reduced and oxidized state during catalysis | Mycobacterium tuberculosis | |
NAD+ | dependent on | Mycobacterium tuberculosis | |
NADH | - |
Mycobacterium tuberculosis |