Coelenteramide
Chemical compound
From Wikipedia, the free encyclopedia
Coelenteramide is the oxidized product, or oxyluciferin, of the bioluminescent reactions in many marine organisms that use coelenterazine. It was first isolated as a blue fluorescent protein from Aequorea victoria after the animals were stimulated to emit light.[2] Under basic conditions, the compound will break down further into coelenteramine and 4-hydroxyphenylacetic acid.
| |
| Names | |
|---|---|
| Preferred IUPAC name
N-[3-Benzyl-5-(4-hydroxyphenyl)pyrazin-2-yl]-2-(4-hydroxyphenyl)acetamide | |
| Other names
Coelenteramide | |
| Identifiers | |
3D model (JSmol) |
|
| ChEBI | |
| ChemSpider | |
| DrugBank | |
| KEGG | |
PubChem CID |
|
| UNII | |
CompTox Dashboard (EPA) |
|
| |
| |
| Properties | |
| C25H21N3O3 | |
| Molar mass | 411.461 g·mol−1 |
| Density | 1.26 g/cm3 |
| Absorbance | ε332.5 = 15000 M−1 cm−1 (methanol)[1] |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
| |
It is an aminopyrazine.[3]
Biosynthesis
Biosynthesis of the precursor coelenterazine in Mnemiopsis leidyi and related comb jellies starts from two molecules of tyrosine and one molecule of phenylalanine. Some researchers believe this comes in the form of a cyclized "Phe-Tyr-Tyr" (FYY) peptide,[4] but as of 2025[update] the full details of the pathway were not known.[5][6]
Bioluminescence
Enzymes such as renilla-luciferin 2-monooxygenase are responsible for the bioluminescence observed in the organisms which contain coelenterazine by catalyzing the chemical reaction
In the process, coelenterazine is oxidized with a concurrent loss of carbon dioxide, and a photon of blue light is emitted.[7]
