1.13.12.7: firefly luciferase
This is an abbreviated version!
For detailed information about firefly luciferase, go to the full flat file.
Word Map on EC 1.13.12.7
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1.13.12.7
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bioluminescence
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luminescence
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chemiluminescence
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emit
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renilla
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noninvasive
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luciferases
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cypridina
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photon
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lentiviral
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adenovirus
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click
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luciferase-expressing
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herpes
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engraft
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nude
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co-transfected
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cytomegalovirus
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camera
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electroporation
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simplex
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hsp70
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emitter
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replication-deficient
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excited-state
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promoter-driven
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charge-coupled
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nonviral
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nanoluc
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non-invasively
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gaussia
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luminol
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intramyocardial
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coelenterazine
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bicistronic
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yellow-green
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molecular biology
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light-emitting
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cap-independent
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aequorin
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biotechnology
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red-shifted
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dnaj
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luminometer
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grpe
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polyethylenimine
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bioimaging
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luciferase-based
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medicine
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photoproteins
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glow
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analysis
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multicolor
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brighter
- 1.13.12.7
-
bioluminescence
-
luminescence
-
chemiluminescence
-
emit
- renilla
-
noninvasive
- luciferases
- cypridina
-
photon
-
lentiviral
- adenovirus
-
click
-
luciferase-expressing
-
herpes
-
engraft
-
nude
-
co-transfected
- cytomegalovirus
-
camera
-
electroporation
- simplex
- hsp70
-
emitter
-
replication-deficient
-
excited-state
-
promoter-driven
-
charge-coupled
-
nonviral
- nanoluc
-
non-invasively
- gaussia
- luminol
-
intramyocardial
- coelenterazine
-
bicistronic
-
yellow-green
- molecular biology
-
light-emitting
-
cap-independent
- aequorin
- biotechnology
-
red-shifted
- dnaj
-
luminometer
- grpe
- polyethylenimine
-
bioimaging
-
luciferase-based
- medicine
-
photoproteins
-
glow
- analysis
-
multicolor
-
brighter
Reaction
Synonyms
AL1, AL2, beetle luciferase, CBG99luc, CBRluc, FFL, firefly luciferase, firefly luciferin luciferase, fluc, LpLuc1, LpLuc2, Luc, Luc1, Luc1-type luciferase, Luc2, Luc2-type luciferase, luciferase, luciferase (firefly luciferin), luciferase FM, luciferin, Luciola italica luciferase, lucPpe, lucPpy, orange light-producing luciferase, oxygen 4-oxidoreductase, PC3-Luc, Photinus luciferin 4-monooxygenase (ATP-hydrolyzing), Photinus pyralis luciferase, PML, PpLase, Ppy, Ppy GR-TS, Ppy RE-TS, PpyWT, PsntWT
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General Information
General Information on EC 1.13.12.7 - firefly luciferase
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evolution
two paralogous firefly luciferase genes, Luc1 and Luc2. Both gene products have luciferase activity to emit green light. Only Luc1 exhibits spectral pH-sensitivity. Phylogenetic analysis suggests that the pH-sensitivity is developed during the course of the evolution of Luc1 lineage
malfunction
physiological function
additional information
the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference
malfunction
the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference
physiological function
fatty acyl-CoA synthesis, acyl-adenylate/thioester-forming enzyme
physiological function
fatty acyl-CoA synthesis, acyl-adenylate/thioester-forming enzyme
physiological function
beetle bioluminescence is the result of two half-reactions catalyzed by a luciferase (Luc) in which the substrate D-firefly luciferin is converted into the corresponding adenylate D-firefly luciferin-AMP, followed by a multistep oxidative process that produces light via a single electron transfer process. Among the Lampyridae, one of the three families of bioluminescent beetles, light emission typically ranges from green to yellow-green in color having emission maxima (lambdamax) of about 548-568 nm
physiological function
beetle bioluminescence is the result of two half-reactions catalyzed by a luciferase (Luc) in which the substrate D-firefly luciferin is converted into the corresponding adenylate D-firefly luciferin-AMP, followed by a multistep oxidative process that produces light via a single electron transfer process. Among the Lampyridae, one of the three families of bioluminescent beetles, light emission typically ranges from green to yellow-green in color having emission maxima (lambdamax) of about 548-568 nm
physiological function
firefly luciferase from North American Photinus pyralis is a monooxygenase that performs ATP-dependent conversion of luciferin into a luciferyl-adenylate, which is oxidized in a multistep reaction to electronically excited oxyluciferin
physiological function
luciferase is the key component of light production in bioluminescence process
usage of three different methods, molecular dynamics (MD) simulation, B-FITTER and framework rigidity optimized dynamics algorithm (FRODA) to determine the flexible regions of Photinus pyralis luciferase: fragment 197-207, fragment 471-481, and fragment 487-495. Introduction of proline within most flexible regions is used to rigidify these flexible regions resulting in mutants D476P and H489P. Analysis of the relationship between stability, activity and flexibility of wild-type and mutant enzymes, molecular dynamics simulations, modelling, overview
additional information
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usage of three different methods, molecular dynamics (MD) simulation, B-FITTER and framework rigidity optimized dynamics algorithm (FRODA) to determine the flexible regions of Photinus pyralis luciferase: fragment 197-207, fragment 471-481, and fragment 487-495. Introduction of proline within most flexible regions is used to rigidify these flexible regions resulting in mutants D476P and H489P. Analysis of the relationship between stability, activity and flexibility of wild-type and mutant enzymes, molecular dynamics simulations, modelling, overview