Structural highlights
Function
[LUCI_OPLGR] Catalytic subunit of oplophorus-luciferin 2-monooxygenase. Oxidoreductase that converts coelenterazine (the oplophorus luciferin) to coelenteramide under emission of blue light with a maximum at 454 nm. Is also active with bisdeoxycoelenterazine.[1]
Publication Abstract from PubMed
The 19 kDa protein (KAZ) of Oplophorus luciferase is a catalytic component, that oxidizes coelenterazine (a luciferin) with molecular oxygen to emit light. The crystal structure of the mutated 19 kDa protein (nanoKAZ) was determined at 1.71 A resolution. The structure consists of 11 antiparallel beta-strands forming a beta-barrel that is capped by 4 short alpha-helices. The structure of nanoKAZ is similar to those of fatty acid-binding proteins (FABPs), even though the amino acid sequence similarity was very low between them. The coelenterazine-binding site and the catalytic site for the luminescence reaction might be in a central cavity of the beta-barrel structure.
Crystal structure of nanoKAZ: The mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine.,Tomabechi Y, Hosoya T, Ehara H, Sekine S, Shirouzu M, Inouye S Biochem Biophys Res Commun. 2016 Jan 29;470(1):88-93. doi:, 10.1016/j.bbrc.2015.12.123. Epub 2015 Dec 30. PMID:26746005[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Inouye S, Watanabe K, Nakamura H, Shimomura O. Secretional luciferase of the luminous shrimp Oplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase(1). FEBS Lett. 2000 Sep 8;481(1):19-25. PMID:10984608
- ↑ Tomabechi Y, Hosoya T, Ehara H, Sekine S, Shirouzu M, Inouye S. Crystal structure of nanoKAZ: The mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine. Biochem Biophys Res Commun. 2016 Jan 29;470(1):88-93. doi:, 10.1016/j.bbrc.2015.12.123. Epub 2015 Dec 30. PMID:26746005 doi:http://dx.doi.org/10.1016/j.bbrc.2015.12.123
