Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NADP+ | product inhibition, competitive versus NADPH, noncompetitive versus 3-dehydroshikimate | Mycobacterium tuberculosis | |
shikimate | product inhibition, noncompetitive versus NADPH, competitive versus 3-dehydroshikimate | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.034 | - |
NADPH | 25°C, pH 7.3 | Mycobacterium tuberculosis | |
0.044 | - |
3-dehydroshikimate | 25°C, pH 7.3 | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | A5U5Q2 | - |
- |
Mycobacterium tuberculosis H37Rv | A5U5Q2 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ | steady-state ordered bi-bi kinetic mechanism. The hydride transferred from NADPH and protons transferred from the solvent in the catalytic cycle are not significantly rate limiting in the overall reaction. Both hydride and proton transfers are concerted, and acid/base chemistry takes place in catalysis and substrate binding | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroshikimate + NADPH | - |
Mycobacterium tuberculosis | shikimate + NADP+ | - |
? | |
3-dehydroshikimate + NADPH | - |
Mycobacterium tuberculosis H37Rv | shikimate + NADP+ | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.078 | - |
3-dehydroshikimate | 25°C, pH 7.3 | Mycobacterium tuberculosis |