The origin, diversity, and structure function relationships of insect luciferases

Abstract

Luciferases are the enzymes that catalyze the reactions that produce light in bioluminescence. Whereas the oxidative mechanism which leads to light emission is similar for most luciferases, these enzymes and their substrates are evolutionarily unrelated. Among all bioluminescent groups, insects constitute one of the most diverse in terms of biochemistry. In the fungus-gnats (Mycetophilidae: Diptera), for example, bioluminescence is generated by two biochemically distinct systems. Despite the diversity, investigations on insect luciferases and biochemistry have been conducted mostly with fireflies. The luciferases from the related phengodid beetles, which can produce green to red bioluminescence using the same chemistry as firefly luciferases, have been recently investigated. Beetle luciferases originated from ancestral acyl-CoA ligases. Present data suggest that conserved motifs among this class of ligases are involved in substrate adenylation. The three-dimensional structure of firefly luciferase was recently solved and mutagenesis studies have been performed identifying putative residues involved in luciferin binding and bioluminescence color determination in several beetle luciferases. The knowledge gained through these studies is helping in the development of useful reporter gene tools for biotechnological and biomedical purposes.

Mammalian-Based Bioreporter Targets: Protein Expression for Bioluminescent and Fluorescent Detection in the Mammalian Cellular Background

“…The primary sequence of Luc shares extensive sequence similarity with the acyl-CoA ligases and this homology has been exploited to determine the location of the active site as well as the binding sites for its required co-factors (Conti et al, 1996). One interesting feature of the protein sequence is a C-terminal tag that directs it to the peroxisome (Viviani, 2002), although it does have some functional features of a membrane protein such as a tendency to associate with phospholipids (Ugarova, 1989). The Luc protein can be divided into two major domains.…”

“…The insects represent a large related group of bioluminescent organisms, with over 2500 species reported to be capable of generating light (Viviani, 2002). While the vast majority of these luminescent reactions remain unstudied, the main exception is in the order Coleoptera (beetles) where systems have been characterized for the click beetles (Fraga, 2008).…”

Microwave Induced Facile One-Pot Access to Diverse 2-Cyanobenzothiazole-A Key Intermediate for the Synthesis of Firefly Luciferin

“…Fireflies are only a part of the big family of bioluminescent insects that can emit light with wavelengths going from yellow-green (560 nm) to red (620 nm) [2]. All the enzymes use the same substrate, i.e.…”

Theoretical Study of the Relationships between Excited State Geometry Changes and Emission Energies of Oxyluciferin

“…[1][2][3][4] Interestingly, while keto-1 exhibits red fluorescence in DMSO or in aqueous solution, 2,3,[5][6][7][8][9] its bioluminescence spectra can be shifted to the green by interactions with the luciferases. [10][11][12][13][14][15][16] Several mechanisms have been proposed to explain this phenomenon. 1,2,4,6,11,12,14,[17][18][19][20][21][22][23][24][25] To the present, the detailed mechanism of the bioluminescence and its shifts in color remain unclear due to the complexity of the microenvironment in vivo.…”