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Literature summary extracted from

  • Ishibashi, M.; Kawanabe, R.; Amaba, N.; Arai, S.; Laksmi, F.; Komori, K.; Tokunaga, M.
    Expression and characterization of the Renilla luciferase with the cumulative mutation (2018), Protein Expr. Purif., 145, 39-44 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.13.12.5 diagnostics the enzyme is a good research tool as a reporter protein and bioimaging probes, yielding blue light using the substrate coelenterazine. However the applications are limited since RLuc is unstable under various conditions Renilla reniformis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.5 expression in Escherichia coli BL21 Star (DE3) Renilla reniformis

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.5 F116/I137V the mutant starts to denature at 30°C, and retained its activity up to 52°C with increased solubility at 34°C and specific activity up to approximately 119% Renilla reniformis
1.13.12.5 F116L/I137V/I75A/N178D/N264S/S287P the thermostability effect increases, with the mutant showing approximately 10°C higher stability. The mutant shows improved tolerance for protease digestion, e.g. trypsin and proteinase and for organic solvent. The mutant enzyme retains 100% specific activity at 45°C, while the wild type loses almost all activity, and retains activity at 55°C. The specific activity is approximately 123% higher than that of the wild type Renilla reniformis
1.13.12.5 F116L/I137V/N264S/S287P thermostability of the mutant is increased. The mutant enzyme shows denaturation at 45 to 52°C and specific activity up to approximately 150% compared with the wild type enzyme Renilla reniformis
1.13.12.5 I75A specific activity of I75A is 47% of that of the wild type enzyme, retains activity up to 50°C Renilla reniformis
1.13.12.5 N178D mutation does not affect thermostability but increases the solubility at 34°C and specific activity up to approximately 141% Renilla reniformis
1.13.12.5 N264S/S287P the mutant starts to denature at 40°C and retains its activity up to 50°C with increased solubility at 34°C and specific activity up to approximately 150% 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 h + O2 Renilla reniformis
-
excited coelenteramide h monoanion + CO2
-
?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.13.12.5 2-propanol 10%, residual activity of the mutant after treatment is 29.4%, residual activity of the wild type enzyme is 0.4% Renilla reniformis
1.13.12.5 dimethylformamide 10%, residual activity of the mutant after treatment is 24.8%, residual activity of the wild type enzyme is 0.1% Renilla reniformis
1.13.12.5 DMSO 10%, residual activity of the mutant after treatment is 91.3%, residual activity of the wild type enzyme is 24.3% Renilla reniformis

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
-
Renilla reniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.5 coelenterazine h + O2
-
Renilla reniformis excited coelenteramide h monoanion + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.5 RLuc
-
Renilla reniformis