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Literature summary extracted from

  • Shigehisa, M.; Amaba, N.; Arai, S.; Higashi, C.; Kawanabe, R.; Matsunaga, A.; Laksmi, F.A.; Tokunaga, M.; Ishibashi, M.
    Stabilization of luciferase from Renilla reniformis using random mutations (2017), Protein Eng. Des. Sel., 30, 7-13 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.5 recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3) Renilla reniformis

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.5 F116L random mutagenesis Renilla reniformis
1.13.12.5 F116L/I137V random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type Renilla reniformis
1.13.12.5 I137V random mutagenesis Renilla reniformis
1.13.12.5 additional information overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview Renilla reniformis
1.13.12.5 additional information stabilization of luciferase from Renilla reniformis using random mutations Renilla reniformis
1.13.12.5 N178D random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type Renilla reniformis
1.13.12.5 N264S random mutagenesis Renilla reniformis
1.13.12.5 N264S/S287P random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type Renilla reniformis
1.13.12.5 S287P random mutagenesis Renilla reniformis

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.5 Renilla reniformis P27652
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.5 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

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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 coelenteramide h + CO2 + hv
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.5 R-Luc
-
 Renilla reniformis
1.13.12.5 Renilla luciferase
-
 Renilla reniformis
1.13.12.5 RLuc
-
 Renilla reniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.5 25
-
 assay at Renilla reniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.12.5 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
1.13.12.5 35 47 purified recombinant His-tagged wild-type RLuc retains full activity up to 35°C and is inactivated at 47°C Renilla reniformis
1.13.12.5 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.5 7.6
-
 assay at Renilla reniformis

General Information

EC Number General Information Comment Organism
1.13.12.5 additional information overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview Renilla reniformis