Oplophorus-luciferin 2-monooxygenase

The two substrates of this enzyme are the luciferin, coelenterazine and oxygen. Its products are the oxyluciferin, coelenteramide, carbon dioxide, and a photon. It belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and initial incorporation of two atoms of oxygen into the substrate. Although the enzyme is part of the group of enzymes that act on coelenterazine, such as Renilla and Gaussia luciferases, it does not share base pair sequences with these enzymes. OpLuc catalyzes the ATP independent chemical reaction: The result of this process is loss of and emission of a photon of blue light at ~460 nm. This reaction has an optimal pH of 9, optimal salt concentration of 0.05-0.1 M, and optimal temperature of ~40 C (making it an unusually heat resistant luciferase), although because O.gracilirostris are deep sea animals living in below 20 C temperatures, luciferase is normally expressed and folded at low temperatures. == Biological function ==

When stimulated in Oplophorus gracilirostris, OpLuc is secreted from the base of legs and antennae of the deep-sea shrimp as a defense mechanism. This mechanism causes O.gracilirostris release a luminous, bright blue luciferase cloud. == Structure ==

OpLuc is a complex of two covalently bonded protein subunits: two molecules of 19 kDa and two molecules of 35 kDa components, making it a heterotetrameric molecule. 35 kDa Protein The lesser known component of the OpLuc enzyme has 320 amino acids with 11 cysteine and 5 leucine molecules. The amino terminus of the protein was experimentally concluded to begin at 39 amino acids. It is thought to stabilize 19 kDa and is not thought to be affect by substrate specificity, however its exact function is not known. == References ==