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Literature summary extracted from
- Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme (1997), Protein Eng., 10, 687-690.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.4.1.9 | D203A | dual specificity for NAD+ and NADP+ | Thermoactinomyces intermedius |
| 1.4.1.9 | D203A/I204R | high affinity for NADP+ | Thermoactinomyces intermedius |
| 1.4.1.9 | D203A/I204R/D210R | high affinity for NADP+ | Thermoactinomyces intermedius |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.1.9 | 0.4 | - |
L-Ile | - |
Thermoactinomyces intermedius |  |
| 1.4.1.9 | 2.5 | - |
NADP+ | mutant D203A/I204R/D210R | Thermoactinomyces intermedius | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.1.9 | Thermoactinomyces intermedius | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.1.9 | L-Ile + H2O + NAD+ | - |
Thermoactinomyces intermedius | 3-methyl-2-oxopentanoate + NH3 + NADH | - |
? | |
| 1.4.1.9 | L-Leu + H2O + NAD+ | - |
Thermoactinomyces intermedius | 4-methyl-2-oxopentanoate + NH3 + NADH | - |
r | |
| 1.4.1.9 | L-leucine + H2O + NADP+ | - |
Thermoactinomyces intermedius | 4-methyl-2-oxopentanoate + NH3 + NADPH + H+ | - |
r | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.1.9 | 13 | - |
NADP+ | mutant enzyme D203A/I204R and D203A/I204R/D210R | Thermoactinomyces intermedius | |
| 1.4.1.9 | 90 | - |
NAD+ | wild-type enzyme | Thermoactinomyces intermedius | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.9 | NAD+ | - |
Thermoactinomyces intermedius | |
| 1.4.1.9 | NADH | - |
Thermoactinomyces intermedius | |
| 1.4.1.9 | NADP+ | wild-type enzyme is inactive, mutant enzyme D203A exhibits dual specificity for NAD+ and NADP+, mutant enzymes D203A/I204R and D203A/I204R/D210R show high affinity for NADP+ | Thermoactinomyces intermedius | |
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