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Literature summary extracted from

  • Stepanyuk, G.A.; Unch, J.; Malikova, N.P.; Markova, S.V.; Lee, J.; Vysotski, E.S.
    Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase (2010), Anal. Bioanal. Chem., 398, 1809-1817.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.5 A55T/C124A/C130A/A143M/M253L/S287L/A123T/D154M/E155G/D162E/I163L/V185L sequentially introduced into the RM-Luc coding sequence using designed oligonucleotide primers and quick-change site-directed mutagenesis, the mutant RM-Y has a red-shifted bioluminescence spectrum Renilla muelleri

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.5 Renilla muelleri C9V492
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.5 coelenterazine + O2 the enzyme catalyzes the oxidative decarboxylation of coelenterazine in the presence of O2, resulting in the formation of coelenteramide in its excited state and CO2 as the reaction product Renilla muelleri coelenteramide + CO2 + hnu green bioluminescence ?
1.13.12.5 coelenterazine-v + O2 increase of substrate coelenterazine stability by ligating it to Ca2+-triggered coelenterazine-binding protein, CBP, from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The apo-CBP binds coelenterazine-v very rapidly from Ca2+ free solution, similar to that as the native coelenterazine. At low concentrations, coelenterazine-v bound within CBP generates a brighter bioluminescence signal than would free coelenterazine, thereby increasing the assay sensitivity, overview Renilla muelleri coelenteramide-v + CO2 + hnu orange bioluminescence ?
1.13.12.5 additional information free coelenterazine and its analogues are unstable in neutral aqueous solution, undergoing a slow autooxidation over several hours Renilla muelleri ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.5 Renilla muelleri luciferase
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 Renilla muelleri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.5 30
-
 assay at Renilla muelleri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.5 7
-
 assay at Renilla muelleri

General Information

EC Number General Information Comment Organism
1.13.12.5 physiological function Renilla luciferase is an enzyme that is responsible for the bioluminescence of the soft coral Renilla Renilla muelleri