Coelenteramide

Coelenteramide
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
UNII
  • InChI=1S/C25H21N3O3/c29-20-10-6-18(7-11-20)15-24(31)28-25-22(14-17-4-2-1-3-5-17)27-23(16-26-25)19-8-12-21(30)13-9-19/h1-13,16,29-30H,14-15H2,(H,26,28,31)
    Key: CJIIERPDFZUYPI-UHFFFAOYSA-N
  • C1=CC=C(C=C1)CC2=NC(=CN=C2NC(=O)CC3=CC=C(C=C3)O)C4=CC=C(C=C4)O
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).
Infobox references

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.

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 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

coelenterazine
 
O2
CO2
 
 
 
coelenteramide
+ hν
 

In the process, coelenterazine is oxidized with a concurrent loss of carbon dioxide, and a photon of blue light is emitted.[7]

References

  1. ^ Shimomura, Osamu (2012). Bioluminescence: chemical principles and methods. Singapore Hackensack, NJ: World Scientific Publishing Co. Pte. Ltd. ISBN 978-981-4366-08-3. OCLC 794263013.
  2. ^ Shimomura O, Johnson FH (1975). "Chemical Nature of Bioluminescence Systems in Coelenterates". PNAS USA. 72 (4): 1546–1549. Bibcode:1975PNAS...72.1546S. doi:10.1073/pnas.72.4.1546. PMC 432574. PMID 236561.
  3. ^ Discovery and Validation of a New Family of Antioxidants: The Aminopyrazine Derivatives. M. L. N. Dubuisson, J.-F. Rees and J. Marchand-Brynaert, Mini-Reviews in Medicinal Chemistry, 2004, 4, 159-165, doi:10.2174/1389557043403927
  4. ^ Francis, Warren R.; Shaner, Nathan C.; Christianson, Lynne M.; Powers, Meghan L.; Haddock, Steven H. D. (2015). "Occurrence of Isopenicillin-N-Synthase Homologs in Bioluminescent Ctenophores and Implications for Coelenterazine Biosynthesis". PLOS ONE. 10 (6) e0128742. doi:10.1371/journal.pone.0128742. PMC 4488382. PMID 26125183.
  5. ^ Tsarkova, Aleksandra S. (2021). "Luciferins Under Construction: A Review of Known Biosynthetic Pathways". Frontiers in Ecology and Evolution. 9 667829. doi:10.3389/fevo.2021.667829.
  6. ^ Oba, Yuichi (2025). "Copepod luminescence revisited". Plankton and Benthos Research. 20 S-P202501: s1–s11. doi:10.3800/pbr.20.s1.
  7. ^ Loening, Andreas Markus; Fenn, Timothy David; Gambhir, Sanjiv Sam (2007). "Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla reniformis". Journal of Molecular Biology. 374 (4): 1017–1028. doi:10.1016/j.jmb.2007.09.078. PMC 2700051. PMID 17980388.
  • Media related to Coelenteramide at Wikimedia Commons
This article is issued from Wikipedia. The text is available under Creative Commons Attribution-Share Alike 4.0 unless otherwise noted. Additional terms may apply for the media files.