EC Number   |
Metals/Ions |
Reference |
|---|
   1.13.12.5 | Br- |
stimulates luminescence activity |
695982 |
| 1.13.12.5 | Ca2+ |
after treatment with excess EDTA to remove Ca2+ from BFP-aq, the blue fluorescence shifts to a greenish fluorescence. This greenish fluorescent protein (GFP-aq) is identified as a non-covalent complex of apoaequorin with coelenteramide (oxyluciferin) in a molar ratio of 1:1 |
673608 |
| 1.13.12.5 | Ca2+ |
all three Ca2+-binding loops of photoproteins bind calcium ions |
677006 |
| 1.13.12.5 | Ca2+ |
Ca2+-induced interaction between calmodulin and M13 leads to intermolecular complementation of split Renilla luciferase |
695572 |
| 1.13.12.5 | Ca2+ |
clytin emits light on reacting with Ca2+. The Ca2+ sensitivity of recombinant clytin is lower than that of aequorin |
676984 |
| 1.13.12.5 | Ca2+ |
dependence of mutant and wild-type aequorin luminescence on Ca2+ concentration.Variations of luminescence kinetics, which depend on three EF hands endowed with different calcium affinities, critically determine the amplitude of aequorin responses to biological calcium signals |
676876 |
| 1.13.12.5 | Ca2+ |
the enzyme contains 3 Ca2+-binding sites |
673606 |
| 1.13.12.5 | Cl- |
stimulates luminescence activity |
695982 |
| 1.13.12.5 | Cu2+ |
strong inhibition of luminescence activity |
695982 |
| 1.13.12.5 | I- |
stimulates luminescence activity |
695982 |
