By feeding experiments using deuterium labeled amino acids of l -tyrosine and l -phenylalanine, we have shown that coelenterazine can be synthesized from two molecules of l -tyrosine and one molecule of l -phenylalanine in M.
We have used electrospray ionization-ion trap-mass spectrometry to investigate whether the deep-sea luminous copepod Metridia pacifica is able to synthesize coelenterazine.
One of the most widely occurring Luciferins is Coelenterazine, this molecule is found in a number of phyla containing marine organisms (Haddock et al., 2001) including Ctenophora, Cnidaria, Mollusca, Arthropoda and many more (Shimonura et al., 1978). Although it is found in many organisms, many do not actively produce the molecule. These organisms depend on a diet of prey that include coelenterazine to successfully produce light (Haddock et al., 2001).Â Example prey items include other ctenophores and hydrozoans, which are likely to gain their coelenterazine from copepod and crustacean prey. (Haddock et al., 2001; Powers et al., 2013). Crustaceans and copepods have been reported to produce their own coelenterazine.Â Which is coded within the dna of the organisms (Haddok et al., 2010; Inouye & Sasaki 2007; Shimomura et al., 1978). The decapod shrimp family Oplophridae have been shown to accumulate coelentrazine through both diet and de novo biosynthesis (Thomson et al., 1995). In a study by Thompson et al (1995), it was found that these decapods held high concentrations of coelenterazine (2154 pmol) in the hepatopancreas and stomach. The two sites responsible for secretory bioluminescence.