Cloned (Comment) | Organism |
---|---|
recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) | Renilla reniformis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
dimethyl sulfoxide | competitive inhibition at 16.6-66 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Seven DMSO molecules interact with amino acids onthe surface of Renilla luciferase. Two of them interact with two catalytic residues (Glu144, His285), the rest of the DMSO molecules have specific interactions with the residues in the substrate binding site including Pro220, Phe180, and Phe261 | Renilla reniformis | |
Isopropanol | compatitive inhibition at 19.3-76 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Four isopropanol molecules interact with amino acids. Most of these molecules move around the amino acidin the binding sites, and only one isopropanol molecule interacts with His285 | Renilla reniformis | |
additional information | the changes of activity of Renilla luciferase in the presence of low concentrations of small organic molecules is not associated with structural collapse or severe changes in the enzyme conformation. Molecular dynamics simulations indicate that DMSO and isopropanol, as probing molecules, aare both able to bind to the emitter site and remain with the residues of the emitter site | Renilla reniformis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | enzyme kinetics in presence of inhibitors DMSO and isopropanol, overview | Renilla reniformis | |
0.0039 | - |
coelenterazine h | pH 7.8, 25°C, recombinant His-tagged enzyme | Renilla reniformis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
coelenterazine + O2 | Renilla reniformis | - |
coelenteramide + CO2 + hv | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Renilla reniformis | P27652 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Renilla reniformis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
coelenterazine + O2 | - |
Renilla reniformis | coelenteramide + CO2 + hv | - |
? | |
coelenterazine h + O2 | - |
Renilla reniformis | coelenteramide h + CO2 + hv | - |
? | |
additional information | substrate of Renilla luciferase, coelenterazine, is a heterocyclic imidazolo-pyrazinone, which is derivatized with (4-hydroxyphenyl)methyl (R2), 4-hydroxyphenyl (R6), and phenyl-methyl (R8) moieties | Renilla reniformis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Renilla luciferase | - |
Renilla reniformis |
RLuc | - |
Renilla reniformis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Renilla reniformis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Renilla reniformis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
12.4 | - |
Isopropanol | pH 7.8, 25°C, recombinant His-tagged enzyme | Renilla reniformis | |
15.1 | - |
dimethyl sulfoxide | pH 7.8, 25°C, recombinant His-tagged enzyme | Renilla reniformis |
General Information | Comment | Organism |
---|---|---|
additional information | architecture of the emitter site in a non-binding model, overview | Renilla reniformis |