EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.86 | expression in Escherichia coli BL21(DE3) | Streptococcus pneumoniae |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.86 | micro-batch and hanging-drop vapor-diffusion methods. The crystal structure is determined at 1.69 A resolution. The crystal structure of SpIlvC contains an asymmetric dimer in which one subunit is in apo-form and the other in NADP(H) and Mg2+-bound form | Streptococcus pneumoniae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.86 | D191G | crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | D191K | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | D83G | crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | E195A | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | E195K | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | E195S | crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | R49A | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | R49E | crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | R49G | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | S53A | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | S53G | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | S53K | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
1.1.1.86 | S53T | mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme | Streptococcus pneumoniae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.86 | 0.07 | - |
NADPH | wild-type enzyme, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.199 | - |
NADPH | mutant enzyme S53G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.33 | - |
NADPH | mutant enzyme D83G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.345 | - |
NADPH | mutant enzyme S53T, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.355 | - |
NADPH | mutant enzyme D191G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.395 | - |
NADPH | mutant enzyme R49G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.47 | 1 | NADPH | mutant enzyme S53K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.472 | - |
NADPH | mutant enzyme R49E, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.588 | - |
NADPH | mutant enzyme R49A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.677 | - |
NADPH | mutant enzyme S53A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.732 | - |
NADPH | mutant enzyme E195A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.895 | - |
NADPH | mutant enzyme E195K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 1.036 | - |
NADPH | mutant enzyme D191K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 1.467 | - |
NADPH | mutant enzyme E195S, pH 8.0, 30°C | Streptococcus pneumoniae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.86 | Streptococcus pneumoniae | Q04M32 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.86 | - |
Streptococcus pneumoniae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.86 | (2S)-2-acetolactate + NADPH + H+ | - |
Streptococcus pneumoniae | (R)-2,3-dihydroxyisovalerate + NADP+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.86 | dimer | the enzyme retains dimeric arrangement in solution | Streptococcus pneumoniae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.86 | ilvC | - |
Streptococcus pneumoniae |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.86 | 0.1 | - |
NADPH | wild-type enzyme, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.11 | - |
NADPH | mutant enzyme S53G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.12 | - |
NADPH | mutant enzyme D191K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.12 | - |
NADPH | mutant enzyme E195A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.12 | - |
NADPH | mutant enzyme S53T, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.13 | - |
NADPH | mutant enzyme D83G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.14 | - |
NADPH | mutant enzyme S53K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.15 | - |
NADPH | mutant enzyme D191G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.16 | - |
NADPH | mutant enzyme R49G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.17 | - |
NADPH | mutant enzyme S53A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.18 | - |
NADPH | mutant enzyme E195K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.18 | - |
NADPH | mutant enzyme R49A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.18 | - |
NADPH | mutant enzyme R49E, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.25 | - |
NADPH | mutant enzyme E195S, pH 8.0, 30°C | Streptococcus pneumoniae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.86 | metabolism | the enzyme catalyzes the second step in the BCAA biosynthetic pathway | Streptococcus pneumoniae |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.86 | 0.16 | - |
NADPH | mutant enzyme E195A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.17 | - |
NADPH | mutant enzyme E195S, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.2 | - |
NADPH | mutant enzyme E195K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.21 | - |
NADPH | mutant enzyme D191K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.25 | - |
NADPH | mutant enzyme S53A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.3 | - |
NADPH | mutant enzyme R49A, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.3 | - |
NADPH | mutant enzyme S53K, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.34 | - |
NADPH | mutant enzyme S53T, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.38 | - |
NADPH | mutant enzyme R49E, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.39 | - |
NADPH | mutant enzyme D83G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.42 | - |
NADPH | mutant enzyme D191G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.43 | - |
NADPH | mutant enzyme R49G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 0.55 | - |
NADPH | mutant enzyme S53G, pH 8.0, 30°C | Streptococcus pneumoniae | |
1.1.1.86 | 1.4 | - |
NADPH | wild-type enzyme, pH 8.0, 30°C | Streptococcus pneumoniae |