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Information on EC 1.13.12.5 - Renilla-type luciferase

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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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UNIPROT: P07164
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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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
aequorin
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luciferase (Renilla luciferin)
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Renilla luciferin 2-monooxygenase
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Renilla-luciferin 2-monooxygenase
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Renilla-type luciferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroperoxycoelenterazine + O2
?
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
all three Ca2+-binding loops of photoproteins bind calcium ions
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
aequorin-1 precursor
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AEQ1_AEQVI
196
0
22514
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch method is used for crystallization. The crystals of Ca2+-loaded apoaequorin are grown from 0.02 M CaCl2, 30% v/v 2-methyl-2,4-pentanediol, and 0.1 M sodium acetate (pH 4.6) during less than 1 week of incubation at 4°C. The maximum size of crystals is 0.35 * 0.3 * 0.25 mm
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deng, L.; Vysotski, E.S.; Markova, S.V.; Liu, Z.J.; Lee, J.; Rose, J.; Wang, B.C.
All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin
Protein Sci.
14
663-675
2005
Aequorea victoria (P07164)
Manually annotated by BRENDA team