Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme. Both words are derived from the Latin word Lucifer – meaning lightbearer. Luciferases are widely used in biotechnology, for microscopy and as reporter genes.
About Luciferase in brief
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. Both words are derived from the Latin word Lucifer – meaning lightbearer. Luciferases are widely used in biotechnology, for microscopy and as reporter genes, for many of the same applications as fluorescent proteins. Unlike fluorescent proteins, luciferases do not require an external light source, but do require addition ofLuciferin, the consumable substrate. A variety of organisms regulate their light production using differentLuciferases in a variety of light-emitting reactions. The majority of studied luciferased have been found in animals, including fireflies, and many marine animals such as copepods, jellyfish, and the sea pansy. However, luciserases have been studied in luminous fungi, like the Jack-O-Lantern mushroom, as well as examples in other kingdoms including luminous bacteria, and dinoflagellates.
Newer lucifer enzymes have recently been identified that are naturally secreted molecules. Some of the benefits of using a secreted reporter molecule like MetLuc is its no-lysis protocol that allows one to be able to conduct live cell assays and multiple assays on the same cell. The Metridia longa secreted lucifer enzyme gene encodes a 24 kDa protein containing an N-terminal secretory signal peptide of 17 amino acid residues. It has been suggested that this region of the luciferas may play an important role in the interaction between LBP and LBP or their interaction with the vacuolar membrane. It is thought that four histidines are important to play a role in this interaction. The structure of the dinofagellate luciferASE has been solved. The core part of the core is a 10 stranded beta barrel that is structurally similar to lipins and FABP.
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This page is based on the article Luciferase published in Wikipedia (as of Dec. 05, 2020) and was automatically summarized using artificial intelligence.
