Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli in native and His-tagged form | Aquifex aeolicus |
Crystallization (Comment) | Organism |
---|---|
apo-enzyme and in complex with both shikimate and NADP+, which assumes the closed conformation | Aquifex aeolicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0424 | - |
NADP+ | 25°C, pH 9.0 | Aquifex aeolicus | |
0.0424 | - |
shikimate | 25°C, pH 9.0 | Aquifex aeolicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | O67049 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ | the active enzyme for dehydrogenation of shikimate contains a deprotonated K70 residue, a deprotonated D106, and a protonated Y216. The hydride transfer and the deprotonation of the 3-hydroxyl group of shikimate proceed in a concerted manner. K70 functions as a general base and becomes protonated in the dehydrogenation reaction. The proton is then transferred to the bulk solvent via the short proton-conducting wire. D106 plays a critical role in the transfer of the proton to the bulk solvent | Aquifex aeolicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
shikimate + NADP+ | - |
Aquifex aeolicus | 3-dehydroshikimate + NADPH + H+ | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
55 | - |
shikimate | 25°C, pH 9.0 | Aquifex aeolicus |