Renilla-luciferin 2-monooxygenase
Renilla-luciferin 2-monooxygenase, Renilla luciferase, or RLuc, is a bioluminescent enzyme found in Renilla reniformis, belonging to a group of coelenterazine luciferases. Of this group of enzymes, the luciferase from Renilla reniformis has been the most extensively studied, and due to its bioluminescence requiring only molecular oxygen, has a wide range of applications, with uses as a reporter gene probe in cell culture, in vivo imaging, and various other areas of biological research. Recently, chimeras of RLuc have been developed and demonstrated to be the brightest luminescent proteins to date, and have proved effective in both noninvasive single-cell and whole body imaging.
Renilla-luciferin 2-monooxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.13.12.5 | ||||||||
CAS no. | 61869-41-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Note that the EC record also includes other unrelated enzymes that catalyze the same reaction. An example is the calcium-dependent photoprotein aequorin: while Rluc is in the AB hydrolase superfamily, aequorin is an EF hand protein. The name does not specifically refer to Renilla, but instead refers to Renilla-luciferin, a chemical also known as coelenterazine.