EC Number   |
Reaction |
Reference  |
|---|
    1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
- |
- |
| 1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
active site structure, reaction and kinetic mechanisms |
667700 |
| 1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
conserved residues Asp103 and Lys67 are important for catalysis in all three paralogues, kinetic mechanism of paralogue HI0607 and substrate binding site |
669328 |
| 1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
active-site base is K92. After the binding of quinate and NAD+, the oxygen of the C3-OH of quinate forms a hydrogen bond to the side chain of the conserved T88 and K92 functions as the active-site base to remove the proton on the C3-OH. Simultaneously,a hydride is transferred from C3 of quinate to NAD+ |
684153 |
| 1.1.1.25 | 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 |
-, 684670 |
| 1.1.1.25 | 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 |
685190 |
| 1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
the pro-R hydrogen of the nicotinamide C4 is 3.35 A from the C3 of shikimate. The catalytic K385 and D423 residues are proximal to the C3-hydroxyl of shikimate, which is deprotonated in the oxidation reaction. The enzyme adopts a concave architecture that places the active sites in a face-to-face arrangement |
686243 |
| 1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding, overview |
711616 |
| 1.1.1.25 | shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ |
the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids |
-, 741030 |
