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Literature summary extracted from

  • Hatzios, S.; Ringgaard, S.; Davis, B.; Waldor, M.
    Studies of dynamic protein-protein interactions in bacteria using renilla luciferase complementation are undermined by nonspecific enzyme inhibition (2012), PLoS ONE, 7, e43175.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.13.12.5 biotechnology split luciferase complementation is applied to study dynamic protein-protein interactions in live bacteria. Nonspecific inhibition of Rluc activity by small molecule effectors compromises the utility of this technique in measuring dynamic protein-protein interactions Renilla reniformis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.5 fragments of Renilla luciferase (Rluc) are fused to the chemotaxis-associated response regulator CheY3 and its phosphatase CheZ in the enteric pathogen Vibrio cholerae in order to demonstrate dynamic protein-protein interactions by luciferase complementation Renilla reniformis

Organism

EC Number Organism UniProt Comment Textmining
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 + O2
-
 Renilla reniformis coelenteramide + CO2 + hv
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.5 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 20
-
 assay at Renilla reniformis