Literature summary for 1.13.12.5 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.

Search for more literature for 1.13.12.5

Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Renilla muelleri	C9V492	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?
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	?
additional information	free coelenterazine and its analogues are unstable in neutral aqueous solution, undergoing a slow autooxidation over several hours	Renilla muelleri	?	-	?

Synonyms

Synonyms	Comment	Organism
Renilla muelleri luciferase	-	Renilla muelleri

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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

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Release 2023.1 (January 2023)