CATH Classification

Domain Context

CATH Clusters

Superfamily alpha/beta hydrolase
Functional Family

Enzyme Information

1.13.12.5
Renilla-type luciferase.
based on mapping to UniProt P27652
Coelenterazine h + O(2) = excited coelenteramide h monoanion + CO(2).
-!- 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 catalyzes an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO(2) 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.

UniProtKB Entries (1)

P27652
LUCI_RENRE
Renilla reniformis
Coelenterazine h 2-monooxygenase

PDB Structure

PDB 2PSF
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla reniformis.
Loening, A.M., Fenn, T.D., Gambhir, S.S.
J.Mol.Biol.