EC Number   |
Protein Variants |
Reference |
|---|
    1.8.1.4 | A1444G |
substitution located in exon 13 leading to 20% of wild type activity |
673943 |
| 1.8.1.4 | A181V |
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme |
-, 711225 |
| 1.8.1.4 | A290R |
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme |
-, 711225 |
| 1.8.1.4 | A328V |
site-directed mutagenesis of the conserved residue, the site-specific dihydrolipoamide dehydrogenase mutant shows a switched kinetic mechanism, it shows a random sequential kinetic mechanism with an interaction factor (alpha) of 8.5. The mutation deteriorates substantially the catalytic power of human E3 enzyme increasing the binding affinity for NAD+ and dihydrolipoamide . The mutation triggers this potential intrinsic property of the enzyme causing the kinetic mechanism of the mutant to switch from a ping-pong mechanism to a random sequential mechanism |
742221 |
| 1.8.1.4 | A48I |
the mutation decreases the Km for dihydrolipoamide substrate by 3fold compared to the wild type enzyme |
764880 |
| 1.8.1.4 | A54I |
the mutation increases the Km for dihydrolipoamide substrate by 1fold and NAD+ by 3fold compared to the wild type enzyme |
764880 |
| 1.8.1.4 | C15T |
the mutation increases the Km for dihydrolipoamide substrate by 5fold and NAD+ by 3fold compared to the wild type enzyme |
764880 |
| 1.8.1.4 | C38G |
the mutation increases the Km for NAD+ by 9fold without affecting Km for dihydrolipoamide compared to the wild type enzyme |
764880 |
| 1.8.1.4 | C44S |
0.003% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature |
393989 |
| 1.8.1.4 | C45S |
Ser-45 mutant is highly purified, shows 5270fold lower activity than wild-type enzyme. Destroyed disulfide bond between Cys-45 and Cys-50 of the active disulfide center in human E3. UV-visible spectrum of the Ser-45 mutant is similar to that of the reduced form of the enzyme and the second fluorescence emission of the mutant disappears |
691569 |
