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<StructureSection load='1lci' size='450' side='right' background='none' scene='69/691535/Overall_structure_rainbow/4' caption='Structure of ''Photinus pyralis'' luciferase (PDB code [[1lci]])'>
<StructureSection load='1lci' size='450' side='right' background='none' scene='69/691535/Overall_structure_rainbow/4' caption='Structure of ''Photinus pyralis'' luciferase (PDB code [[1lci]])'>
=''Photinus pyralis'' Luciferase=
=''Photinus pyralis'' Luciferase=
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 acyl-CoA synthetates, non-ribosmal peptide synthetases (NRPSs), and luciferase. 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: luring prey, mating and courtship or helping to camouflage by erasing the shadow and 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> In research labs, the reporter firefly luciferase from Photinus pyralis is widely used in molecular biology and small molecule high-throughput screening (HTS) assays.<ref name=Thorne2012 /> Light production produced by this enzyme is a very sensitive analytical tool in detection and quantification of ATP, phosphate activity detection, as well as DNA sequencing. It also has applications in public health, specifically in detection of microorganisms. The use of luciferase in monitoring gene expressions, tumor growth, and metastasis has been studied more recently.<ref name=Ali2009>Riahi-Madvar, A. and Hosseinkhani, S. (2009) “Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis”, PEDS 22(11):655-663. doi:10.1093/protein/gzp047.</ref>
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 acyl-CoA synthetases, non-ribosmal peptide synthetases (NRPSs), and luciferases. 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: luring prey, mating and courtship or helping to camouflage by erasing the shadow and 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> In research labs, the reporter firefly luciferase from Photinus pyralis is widely used in molecular biology and small molecule high-throughput screening (HTS) assays.<ref name=Thorne2012 /> Light production produced by this enzyme is a very sensitive analytical tool in detection and quantification of ATP, phosphate activity detection, as well as DNA sequencing. It also has applications in public health, specifically in detection of microorganisms. The use of luciferase in monitoring gene expressions, tumor growth, and metastasis has been studied more recently.<ref name=Ali2009>Riahi-Madvar, A. and Hosseinkhani, S. (2009) “Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis”, PEDS 22(11):655-663. doi:10.1093/protein/gzp047.</ref>


== Structure ==
== Structure ==