Cloned (Comment) | Organism |
---|---|
the three intramolecularly homologous domains are separately cloned and expressed in Escherichia coli JM109 cells as fusion proteins | Lingulodinium polyedra |
Protein Variants | Comment | Organism |
---|---|---|
additional information | for each luciferase domain (D1, D2, D3) the removal of approximately 50 N-terminal amino acids results in an increase in the ratio of luciferase activity at pH 8.0 relative to that at pH 6.3. At pH 8.0, peptides D1167-486, D2535-897, and D3927-1241, lacking the first 55, 47, and 62 amino acids of their N-termini retain about 40%, 50%, and 70% of the pH 6.3 luciferase activity, respectively | Lingulodinium polyedra |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lingulodinium polyedra | - |
formerly Gonyaulax polyedra | - |
Purification (Comment) | Organism |
---|---|
glutathione-Sepharose column chromatography | Lingulodinium polyedra |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dinoflagellate luciferin + O2 | - |
Lingulodinium polyedra | oxidized dinoflagellate luciferin + H2O + hv | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.3 | - |
full-length native enzyme | Lingulodinium polyedra |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
8 | - |
the activity of the full-length native enzyme drops to near zero at pH 8.0, the activity of domain fragments also peaks at pH 6.3 but remains high at 8.0 | Lingulodinium polyedra |