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Information on EC 1.13.12.5 - Renilla-type luciferase and Organism(s) Renilla muelleri and UniProt Accession C9V492

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IUBMB Comments
This enzyme has been studied from the soft coral Renilla reniformis. Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein. Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase. Upon binding the substrate, the enzyme catalyses an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.
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Renilla muelleri
UNIPROT: C9V492
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The taxonomic range for the selected organisms is: Renilla muelleri
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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coelenterazine h
+
O2
=
excited coelenteramide h monoanion
+
CO2
+
=
+
Synonyms
aequorin, renilla luciferase, gaussia luciferase, gaussia princeps luciferase, renilla reniformis luciferase, rluc8, clytin, oplophorus luciferase, bfp-aq, gaussia-luciferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Renilla muelleri luciferase
-
aequorin
-
-
-
-
luciferase (Renilla luciferin)
-
-
-
-
Renilla luciferin 2-monooxygenase
-
-
-
-
Renilla-luciferin 2-monooxygenase
-
-
-
-
Renilla-type luciferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
coelenterazine h + O2 = excited coelenteramide h monoanion + CO2
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
coelenterazine h:oxygen 2-oxidoreductase (decarboxylating)
This enzyme has been studied from the soft coral Renilla reniformis. Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein. Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase. Upon binding the substrate, the enzyme catalyses an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.
CAS REGISTRY NUMBER
COMMENTARY hide
346421-46-3
Gaussia luciferase
61869-41-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coelenterazine + O2
coelenteramide + CO2 + hnu
show the reaction diagram
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
green bioluminescence
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
show the reaction diagram
coelenterazine is bound by coelenterazine-binding protein. In combinantion with renilla luciferase, addition of only one Ca2+-ion is sufficient to release coelenterazine as a substrate. The combination of the two proteins generates bioluminescence with higher reaction efficiency than using free coelenterazine alone
-
-
?
coelenterazine-v + O2
coelenteramide-v + CO2 + hnu
show the reaction diagram
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
orange bioluminescence
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
show the reaction diagram
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-
-
-
?
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Renilla luciferase is an enzyme that is responsible for the bioluminescence of the soft coral Renilla
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C9V492_RENMU
311
0
36097
TrEMBL
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cormier, M.J.; Hori, K.; Anderson, J.M.
Bioluminescence in coelenterates
Biochim. Biophys. Acta
346
137-164
1974
Renilla koellikeri, Renilla muelleri, Renilla reniformis
Manually annotated by BRENDA team
Titushin, M.S.; Markova, S.V.; Frank, L.A.; Malikova, N.P.; Stepanyuk, G.A.; Lee, J.; Vysotski, E.S.
Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase
Photochem. Photobiol. Sci.
7
189-196
2008
Renilla muelleri (C9V492), Renilla muelleri
Manually annotated by BRENDA team
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
Anal. Bioanal. Chem.
398
1809-1817
2010
Renilla muelleri (C9V492), Renilla muelleri
Manually annotated by BRENDA team