KEGG   ENZYME: 1.13.12.5Help
Entry
EC 1.13.12.5                Enzyme                                 

Name
Renilla-type luciferase;
Renilla-luciferin 2-monooxygenase;
luciferase (Renilla luciferin);
Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
BRITE hierarchy
Sysname
coelenterazine h:oxygen 2-oxidoreductase (decarboxylating)
Reaction(IUBMB)
coelenterazine h + O2 = excited coelenteramide h monoanion + CO2 (over-all reaction) [RN:R03137];
(1a) coelenterazine h + O2 = coelenterazine h dioxetanone;
(1b) coelenterazine h dioxetanone = excited coelenteramide h monoanion + CO2
Reaction(KEGG)
Substrate
coelenterazine h [CPD:C00982];
O2 [CPD:C00007];
coelenterazine h dioxetanone
Product
excited coelenteramide h monoanion [CPD:C03717];
CO2 [CPD:C00011];
coelenterazine h dioxetanone
Comment
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.
History
EC 1.13.12.5 created 1976, modified 1981, modified 1982, modified 2004, modified 2017
Orthology
K18053  
renilla-luciferin 2-monooxygenase
Genes
BFO: 
CIN: 
SPU: 
TAD: 
Taxonomy
Reference
1  [PMID:4154104]
  Authors
Cormier MJ, Hori K, Anderson JM.
  Title
Bioluminescence in coelenterates.
  Journal
Biochim. Biophys. Acta. 346 (1974) 137-64.
Reference
2  [PMID:237531]
  Authors
Hori K, Anderson JM, Ward WW, Cormier MJ.
  Title
Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin.
  Journal
Biochemistry. 14 (1975) 2371-6.
Reference
3  [PMID:4149963]
  Authors
Anderson JM, Charbonneau H, Cormier MJ.
  Title
Mechanism of calcium induction of Renilla bioluminescence. Involvement of a calcium-triggered luciferin binding protein.
  Journal
Biochemistry. 13 (1974) 1195-200.
Reference
4  [PMID:236561]
  Authors
Shimomura O, Johnson FH.
  Title
Chemical nature of bioluminescence systems in coelenterates.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 1546-9.
Reference
5  [PMID:33174]
  Authors
Charbonneau H, Cormier MJ.
  Title
Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein.
  Journal
J. Biol. Chem. 254 (1979) 769-80.
Reference
6  [PMID:1674607]
  Authors
Lorenz WW, McCann RO, Longiaru M, Cormier MJ.
  Title
Isolation and expression of a cDNA encoding Renilla reniformis luciferase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 4438-42.
  Sequence
Reference
7  [PMID:17980388]
  Authors
Loening AM, Fenn TD, Gambhir SS
  Title
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis.
  Journal
J. Mol. Biol. 374 (2007) 1017-28.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
61869-41-8

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