EC Number | Application | Comment | Organism |
---|---|---|---|
1.13.12.5 | diagnostics | Renilla Luciferase (RLuc) is a blue light emitter protein which can be applied as a valuable tool in medical diagnosis | Renilla reniformis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.12.5 | additional information | super RLuc8 is a Renilla luciferase variant in which 16 amino acids are substituted | Renilla reniformis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.5 | coelenterazine + O2 | Renilla reniformis | - |
coelenteramide + CO2 + hv | - |
? | |
1.13.12.5 | coelenterazine h + O2 | Renilla reniformis | - |
excited coelenteramide h monoanion + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.12.5 | Renilla reniformis | P27652 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.5 | coelenterazine + O2 | - |
Renilla reniformis | coelenteramide + CO2 + hv | - |
? | |
1.13.12.5 | coelenterazine h + O2 | - |
Renilla reniformis | excited coelenteramide h monoanion + CO2 | - |
? | |
1.13.12.5 | coelenterazine h + O2 | an induced-fit mechanism is proposed where ligand-binding induces conformational changes of the active site. Insights regarding the controversial properties and the mechanism of the reaction catalysis of Renilla luciferase and its red-shifted light emittingvariant (Super RLuc 8) | Renilla reniformis | excited coelenteramide h monoanion + CO2 | - |
? | |
1.13.12.5 | coelenterazine-h + O2 | substrate binding structure | Renilla reniformis | coelenteramide h + CO2 + hv | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.12.5 | ? | x * 37000, SDS-PAGE and crystallization | Renilla reniformis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.12.5 | Renilla luciferase | - |
Renilla reniformis |
1.13.12.5 | RLuc | - |
Renilla reniformis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.12.5 | additional information | enzyme active site structure and ligand-receptor interactions, molecular docking. Structure analysis using crystal structure of Renilla luciferase 8 (RLuc8), a thermostable variant of RLuc, in apo-form and incomplex with its product-coelenteramide. The enzyme has a deep tunnel made up of mostly hydrophobic residues and the catalytic triad (D120, E144 and H285) is embedded at the bottom of the tunnel. Molecular dynamic simulation and molecular docking, simulation of open conformation for docking study and of of receptor-ligand complex, with ligand/substrate coelenterazine-h (ZINC2569714), after molecular docking, overview. Evaluation of the enzymes' active site in complex with coelenterazine-h. The RMSD value is moderately higher in Super RLuc8 compared with the native variant which represents the higher motion of the ligand in Super RLuc8 | Renilla reniformis |