KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | transient-state and steady-state kinetics of the enzyme in two-electron-reduced and four-electron-reduced state at 4°C and 25°C, respectively | 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+ | in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron-reduced enzyme, both redox centers are reduced, mechanism of the diaphorase reaction which occurs when the enzyme is in the four-electron-reduced state | Mycobacterium tuberculosis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferricyanide + NADH | - |
Mycobacterium tuberculosis | 2 ferrocyanide + NAD+ + H+ | - |
? | |
2,6-dimethyl-1,4-benzoquinone + NADH | 90fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state | Mycobacterium tuberculosis | 2,6-dimethyl-1,4-benzoquinol + NAD+ | - |
? | |
DL-lipoate + NADH | - |
Mycobacterium tuberculosis | ? + NAD+ | - |
? | |
DL-lipoylbutanoate + NADH | - |
Mycobacterium tuberculosis | ? + NAD+ | - |
? | |
DL-lipoylpentanoate + NADH | 100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state | Mycobacterium tuberculosis | ? + NAD+ | - |
? | |
NADH + H+ + oxidized 2,6-dichlorophenolindophenol | - |
Mycobacterium tuberculosis | NAD+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
O2 + NADH | 40fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state | Mycobacterium tuberculosis | H2O2 + NAD+ | - |
? | |
reduced DL-lipoamide + NAD+ | - |
Mycobacterium tuberculosis | oxidized DL-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 |
---|---|---|
diaphorase | - |
Mycobacterium tuberculosis |
lipoamide dehydrogenase | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Mycobacterium tuberculosis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.25 | - |
O2 | pH 7.5, 25°C | Mycobacterium tuberculosis | |
190 | - |
2,6-dimethyl-1,4-benzoquinone | pH 7.5, 25°C | Mycobacterium tuberculosis | |
220 | - |
DL-lipoylpentanoate | pH 7.5, 25°C | Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
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 disulfid, the cofactor cycles between reduced and oxidized state during catalysis, in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron.reduced enzyme, both redox centers are reduced | Mycobacterium tuberculosis | |
NAD+ | - |
Mycobacterium tuberculosis | |
NADH | - |
Mycobacterium tuberculosis |