Literature summary for 1.13.12.7 extracted from

Smirnova, D.V.; Ugarova, N.N.
Firefly luciferase-based fusion proteins and their applications in bioanalysis (2017), Photochem. Photobiol., 93, 436-447 .

Search for more literature for 1.13.12.7

Application

Application	Comment	Organism
molecular biology	firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling	Photinus pyralis
molecular biology	firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling	Luciola mingrelica
molecular biology	firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling	Aquatica lateralis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-firefly luciferin + O2 + ATP	Photinus pyralis	-	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?
D-firefly luciferin + O2 + ATP	Luciola mingrelica	-	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?
D-firefly luciferin + O2 + ATP	Aquatica lateralis	-	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?

Organism

Organism	UniProt	Comment	Textmining
Aquatica lateralis	Q01158	-	-
Luciola mingrelica	Q26304	-	-
Photinus pyralis	P08659	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-firefly luciferin + O2 + ATP	-	Photinus pyralis	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?
D-firefly luciferin + O2 + ATP	-	Luciola mingrelica	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?
D-firefly luciferin + O2 + ATP	-	Aquatica lateralis	firefly oxyluciferin + CO2 + AMP + diphosphate + hv	-	?

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Release 2023.1 (January 2023)