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Literature summary for 1.13.12.5 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
Search for more literature for 1.13.12.5

Application

Application Comment Organism
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)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
I75A specific activity of I75A is 47% of that of the wild type enzyme, retains activity up to 50°C Renilla reniformis
N178D mutation does not affect thermostability but increases the solubility at 34°C and specific activity up to approximately 141% Renilla reniformis
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coelenterazine h + O2 Renilla reniformis
-
 excited coelenteramide h monoanion + CO2
-
 ?

Organic Solvent Stability

Organic Solvent Comment Organism
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
dimethylformamide 10%, residual activity of the mutant after treatment is 24.8%, residual activity of the wild type enzyme is 0.1% Renilla reniformis
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

Organism UniProt Comment Textmining
Renilla reniformis P27652
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Renilla reniformis

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
RLuc
-
 Renilla reniformis