Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.12.5 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

Application Comment Organism
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)

Cloned (Comment) Organism
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

Organism UniProt Comment Textmining
Renilla reniformis
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
luciferase
-
Renilla reniformis
RLuc
-
Renilla reniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
assay at Renilla reniformis