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Literature summary for 1.13.12.18 extracted from
- Constant pH accelerated molecular dynamics investigation of the pH regulation mechanism of Dinoflagellate luciferase (2018), Biochemistry, 57, 295-299 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Lingulodinium polyedra |
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 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LCF | - |
Lingulodinium polyedra |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
constant pH accelerated molecular dynamics (CpHaMD) is applied to investigate the conformational changes associated with the activation of the enzyme (LCF) upon acidification. The protonation of several residues, including the previously identifies intramolecularly conserved histidines and the H1064/H1065 dyad, correlates with a large scale conformational change in which the N-terminal domain reorganizes to allow the substrate access to the active site | Lingulodinium polyedra |
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