Sandbox Reserved 993: Difference between revisions

Purified and characterized in 1978, ''Photinus pyralis'' luciferase (E.C. 1.13.12.7) is an enzyme found within the peroxisomes of the lantern organ located in the abdomen of the North American firefly (''Photinus pyralis'').<ref name=Conti1996>Conti E., Franks N.P., Brick P. (1996) "Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes", Structure 4(3): 287-298. doi: 10.1016/S0969-2126(96)00033-0</ref> It is a member of an ANL superfamily which is made of '''a'''cyl-CoA synthetases, '''n'''on-ribosmal peptide synthetases (NRPSs), and '''l'''uciferases. These enzymes all produce an acyl-AMP intermediate as part of their catalytic reactions.<ref name=Sundlov2012>Sundlov J.A., Fontaine D.M., Southworth T.L., Branchini B.R., and Gulick, A.M. (2012) “Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism”, Biochemistry 51(33): 6493-6495. doi: 10.1021/bi300934s</ref> Luciferases, along with a substrate luciferin, produce light by a reaction with ATP. Organisms that can do this include bacteria, fungi, algae, fish, squid, shrimp, and insects including the firefly.<ref name=Amani2012>Amani-Bayat Z., Hosseinkhani S., Jafari R., and Khajeh K. (2012) “Relationship between stability and flexibility in the most flexible region Photinus pyralis luciferase”, Biochim. Biophy. Acta 1842(2): 350-358. doi 10.1016/j.bbapap.2011.11.003</ref> Some uses of bioluminescence in nature are luring prey, mating and courtship, or helping to camouflage the organism by erasing its shadow or making it invisible from below.<ref name=Shapiro2005>Shapiro E., Lu C., and Baneyx F. (2005) “A Set of Multicolored Photinus Pyralis Luciferase Mutants for in Vivo Bioluminescence Applications”, PEDS 18(12): 581-587. doi:10.1093/protein/gzi066.</ref> ''Photinus pyralis'' luciferase is used in a variety of analytic biological tests as well.