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Literature summary for 1.13.12.18 extracted from
- Unravelling the mechanism of pH-regulation in dinoflagellate luciferase (2020), Int. J. Biol. Macromol., 164, 2671-2680 .
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dinoflagellate luciferin + O2 | Lingulodinium polyedra | - |
oxidized dinoflagellate luciferin + H2O + hv | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lingulodinium polyedra | O77206 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dinoflagellate luciferin + O2 | - |
Lingulodinium polyedra | oxidized dinoflagellate luciferin + H2O + hv | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
the oxidation of luciferin by Dinoflagellates luciferase only takes place at low pH. Computational tools are used to predict the open structure of the luciferase in Lingulodinium polyedra and to decipher the nature of the opening mechanism. Through accelerated molecular dynamics simulations, it is demonstrated that the closed-open conformational change likely takes place via a tilt of the pH-regulatory helix-loop-helix domain. It is proposed that the molecular basis for the transition is electrostatic repulsion between histidine-cation pairs, which destabilizes the closed conformation at low pH | Lingulodinium polyedra |
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