Any feedback?
Literature summary for 1.13.12.5 extracted from
- Stabilization of luciferase from Renilla reniformis using random mutations (2017), Protein Eng. Des. Sel., 30, 7-13 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3) | Renilla reniformis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F116L | random mutagenesis | Renilla reniformis |
| F116L/I137V | random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type | Renilla reniformis |
| I137V | random mutagenesis | Renilla reniformis |
| additional information | overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview | Renilla reniformis |
| additional information | stabilization of luciferase from Renilla reniformis using random mutations | Renilla reniformis |
| N178D | random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type | Renilla reniformis |
| N264S | random mutagenesis | Renilla reniformis |
| N264S/S287P | random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type | Renilla reniformis |
| S287P | random mutagenesis | Renilla reniformis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| coelenterazine + O2 | Renilla reniformis | - |
coelenteramide + CO2 + hv | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Renilla reniformis | P27652 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography to over 95% purity | Renilla reniformis |
Substrates and Products (Substrate)
| 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 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| R-Luc | - |
Renilla reniformis |
| Renilla luciferase | - |
Renilla reniformis |
| RLuc | - |
Renilla reniformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Renilla reniformis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 52 | the F116L/I137V mutant shows a transition starting at 30°C, which is 5°C lower than the wild-type, and ending at 52°C, which is 5°C higher than the wild type. N178D mutant has almost the same denaturation profile | Renilla reniformis |
| 35 | 47 | purified recombinant His-tagged wild-type RLuc retains full activity up to 35°C and is inactivated at 47°C | Renilla reniformis |
| 40 | 47 | the stability of the purified recombinant His-tagged N264S/S287P mutant is maintains at a temperature that is 5°C higher than the wild-type. | Renilla reniformis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Renilla reniformis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview | Renilla reniformis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
