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Enzyme Nomenclature
Information on EC 1.13.12.7 - firefly luciferase
for references in articles please use BRENDA:EC1.13.12.7
Word Map on EC 1.13.12.7
- 1.13.12.7
-
bioluminescence
-
luminescence
- viral
- renilla
-
luciferases
-
emit
-
noninvasive
- cypridina
-
chemiluminescence
-
photon
- cytomegalovirus
-
longitudinal
-
herpes
-
luciferase-expressing
- adenovirus
-
lentiviral
-
electroporation
- viruses
-
orthotopic
-
nude
- simplex
-
camera
-
engraft
-
co-transfected
-
click
-
cell-based
-
promoter-driven
-
positron
-
excited-state
-
light-emitting
- gaussia
- medicine
-
bioimaging
-
emitter
-
multicolor
- luminol
- biotechnology
-
photoproteins
- benzothiazole
-
red-shifted
-
luminometer
- aequorin
-
cap-independent
- coelenterazine
- molecular biology
- analysis
-
nonviral
-
bicistronic
-
charge-coupled
-
intramyocardial
-
luciferase-based
-
luminometric
-
dual-luciferase
-
replication-deficient
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.13.12.7
-
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RECOMMENDED NAME
GeneOntology No.
firefly luciferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-firefly luciferin + O2 + ATP = firefly oxyluciferin + CO2 + AMP + diphosphate + hnu
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Photinus (firefly) is a bioluminescent insect. The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate. The enzyme may be assayed by measurement of light emission.
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CAS REGISTRY NUMBER
COMMENTARY
61970-00-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
484825, 484826, 484827, 484828, 484829, 484830, 484831, 484832, 484833, 484834, 484835, 484836, 484837, 484838, 484839, 484840, 484841, 484842, 484843, 484844, 484845, 484846, 484847, 484848, 484849, 484850, 484851, 484852, 484853, 484854, 484855, 484856, 484857, 484858, 484859, 484860, 484862, 484863, 484864, 484865, 484866, 484867, 484868, 484869, 484870, 484873, 484874, 484875, 657787, 657942, 658085, 658193, 658219, 658709, 659958, 671309, 671781, 671869, 672578, 672992, 673086, 673531, 673618, 675214, 675322, 675811, 676320, 676934, 685746, 695557, 696465, 697750, 698315, 699453, 699955, 700619, 700623, 701048, 726696, 726775, 727009, 727075, 727160, 727630, 727631, 728433, 728712
-
-
-
484861, 658103, 658314, 672684, 697221, 698393, 744012, 744013, 744062, 744326, 744408, 745975, 746213, 746376
UniProt
-
Q27758
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
-
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
malfunction
-
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
-
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
-
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 500 sec, relative specific activity: 13%
-
-
?
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 150 sec, relative specific activity: 1.7%
-
-
?
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 5700 sec, relative specific activity: 421%
-
-
?
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 400 sec, relative specific activity: 0.4%
-
-
?
(4S)-2-(6-hydroxy-1H-indol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
-
-
-
?
5,5'-dimethylluciferin + ATP + O2
dehydroluciferin-adenylate + diphosphate
-
produces only red light, 6-amino and 4 hydroxy analogs tested
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv + ?
-
-
-
-
?
5,5-dimethylluciferin + ATP
5,5-dimethyloxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
5-methylluciferin + ATP
5-methyloxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
5-monomethyl-luciferyl-O-adenosine monophosphate + ?
5-monomethyloxyluciferin + hv + ?
-
-
-
-
?
adenosine 5'-tetraphosphate + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
0.75% light response relative to ATP
-
?
ADP
ATP + AMP
-
-
reaction inhibited by P1,P5-di(adenosine-5'-)pentaphosphate, but independent of luciferin
?
coelenterazine disulfate + ATP + O2 + H2O
coelenteramide disulfate + AMP + CO2 + diphosphate
-
-
-
?
D-5,5-dimethylluciferyl-adenylate + O2
?
-
yellow-green color of luminescence
-
-
?
D-5,5-dimethylluciferyl-adenylate + O2 + ATP
?
red color of luminescence
-
-
?
D-luciferin + ATP + O2
luciferyl-AMP + diphosphate
-
assay at pH 7.8
-
-
r
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate
-
-
-
-
?
D-luciferin + ATP + O2
oxyluciferin + CO2 + AMP + hv + diphosphate
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
r
dehydroluciferin + ATP + O2
diphosphate + dehydroluciferin-adenylate
-
-
-
?
deoxyATP + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
L-luciferin + CoA + ATP
luciferyl-CoA + AMP + diphosphate
-
L-luciferin is converted to luciferyl adenylate, and the adenyl group of luciferyl adenylate is then substituted to CoA-SH to give luciferyl-CoA. Even in presence of CoA-SH, D-luciferin is used for the light production reaction, but is not converted into luciferyl-CoA
-
-
?
P1,P5-di(adenosine-5'-)pentaphosphate + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
2.2% light response relative to ATP
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
Photinus luciferin + O2 + GTP
adenosine 5'-P1-tetraphospho-P4-5'''-guanosine
-
-
-
?
polyethylene glycol-6-amino-D-luciferin
? + hv
-
longer light emission
-
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv
-
-
-
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
Q1AG35;
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate + H2O + hv
-
-
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate + H2O + hv
-
-
-
-
r
D-luciferin + ATP + O2
oxidized D-luciferin + AMP + CO2 + diphosphate
-
-
-
-
?
D-luciferin + ATP + O2
oxidized D-luciferin + AMP + CO2 + diphosphate
-
decay time to 10%: 23 sec, relative specific activity: 100%
-
-
?
D-luciferin + ATP + O2
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
assay at 25°C, pH 7.8
-
-
?
D-luciferin + ATP + O2
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
-
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
Macrolampis sp2
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
Q27758;
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
D-luciferin is (S)-2-[6'-hydroxy-2'-benzothiazolyl]-2-thiazoline-4-carboxylic acid (S)-2-[6-hydroxybenzothiazol-2-yl]-4,5-dihydrothiazole-4-carboxylic acid
-
-
r
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
D-luciferin is (S)-2-(6-hydroxy-2-benzothiazolyl)-2-thiazoline-4-carboxylic acid
the keto form of oxidized D-luciferin produces red light in chemiluminescence and yellow-green in bioluminescence
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + CoA
-
linoleic acid concentration above 10 microM has an inhibitory effect
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
-
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
luciferase modulates emission color by controlling the resonance-based delocalization of the anionic keto form of the oxyluciferin excited state
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
luciferase modulates emission color by controlling the resonance-based deloclization of the anionic keto form of the oxyluciferin excited state
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
highly specific for ATP
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
enzyme produced in Sf9 cells requires less luciferin than mammalian or plant cells
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the true substrate is MgATP2-
-
?
additional information
?
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
-
additional information
?
-
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
-
additional information
?
-
-
analysis of reaction parameters, detailed overview
-
-
-
additional information
?
-
analysis of reaction parameters, detailed overview
-
-
-
additional information
?
-
-
analysis of reaction parameters, detailed overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coelenterazine disulfate + ATP + O2 + H2O
coelenteramide disulfate + AMP + CO2 + diphosphate
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
highly specific for ATP
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
Q1AG35
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
A0A1B3TNR9
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Mg2+
Zn2+
additional information
Cu2+
-
promotes the binding to Cibacron brilliant blue and Cibacron blue F3GA
Mg2+
-
the enzyme catalyzes the oxidation of substrate luciferin in the presence of Mg2+ (10 mM)
Mg2+
-
optimal concentration for wild-type enzyme and N-terminal domain: 10 mM
Mg2+
-
enzyme activity without 10 mM MgSO4 decreases to about 50% of that of wild type enzyme in the presence of Mg2+
Mg2+
-
the enzyme catalyzes the oxidation of substrate luciferin in the presence of Mg2+ (10 mM)
Zn2+
-
increasing concentration shifts the light wavelenghts to higher values
additional information
-
Mg2+, Ca2+, Zn2+, Ni2+, Cu2+, Fe3+, Li+, Na+, K+ not required for activity
additional information
-
activity in decreasing order: Mn2+, Mg2+, Co2+/Zn2+/Fe2+, Cd2+, Ni2+, Ca2+, Sr2+; Ba2+ inactivates and Hg2+ is inhibitor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid
-
common name indoprofen
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
-
-
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
-
common name SU4312
2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone
-
common name pifithrin-alpha
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
2-(6'-hydroxy-2'-benzothiazolyl)-4-hydroxymethylthiazole
-
competitive inhibitor
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
-
common name SCS
3,4-dichloro-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 13% inhibition
3,4-dimethoxy-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 26% inhibition
-
3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
decrease of Fluc proteolysis, 2 microM
4-((7-[4-(trifluoromethyl)benzyl]-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy)aniline
-
7% inhibition
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
-
-
4-(1-methylethoxy)-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 12% inhibition
-
4-(dimethylamino)-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 35% inhibition
4-([2-(methylsulfanyl)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
31% inhibition
4-([2-(methylsulfonyl)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
9% inhibition
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N,N-dimethylaniline
-
-
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N-methylaniline
-
-
4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(3-methylbut-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
26% inhibition
4-amino-6-[(E)-[4'-[(Z)-(8-amino-1-hydroxy-5,7-disulfonato-6,7-dihydronaphthalen-2-yl)diazenyl]-3-methylbiphenyl-4-yl]diazenyl]-5-hydroxy-2,3-dihydronaphthalene-1,3-disulfonate
-
common name Evans Blue
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
-
-
5'-O-[(N-dehydroluciferyl)-sulfamoyl]-adenosine
-
stable and potent reversibel inhibitor
5-methyl-N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
-
D-luciferin
-
inhibits CoA-ligase activity with L-luciferin, IC50: 0.135 mM against 0.1 mM L-luciferin
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
-
-
ethyl [4-(4-aminophenoxy)-7H-pyrrolo[2,3-d]pyrimidin-7-yl]acetate
-
33% inhibition
L-1-tosylamido-2-phenethyl chlorometyl ketone
-
competitive inhibitor with respect to luciferin, noncompetitive with respect to ATP
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
-
common name DCB
N,N-dimethyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N,N-dimethyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N-methyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N-methyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N-[5-(3,4-dichlorophenyl)pyridin-2-yl]benzamide
-
10 microM, 4% inhibition
N-[5-(4-tert-butylphenyl)pyridin-2-yl]benzamide
-
10 microM, 49% inhibition
N-[5-[4-(1-methylethoxy)phenyl]pyridin-2-yl]benzamide
-
10 microM, 38% inhibition
N-[5-[4-(dimethylamino)phenyl]pyridin-2-yl]benzamide
-
10 microM, 14% inhibition
N-[5-[4-(trifluoromethyl)phenyl]pyridin-2-yl]benzamide
-
10 microM, 39% inhibition
arsenate
-
lowers the flash height and extends the light emission for a given amount of ATP
ATP
-
uncomplexed ATP is a competitive inhibitor with respect to MgATP2- complex
N-tosyl-L-phenylalanine chloromethyl ketone
-
competitive inhibitor with respect to luciferin, noncompetitive with respect to ATP, pH dependent, enzyme protected by dehydroluciferin-AMP
Procion blue MX-R
-
irreversible inhibitor, enzyme protected by luciferin, ATP and MgATP2-
Procion blue MX-R
-
irreversible inhibitor, enzyme protected by luciferin, ATP and MgATP2-; time dependent
additional information
-
binding of one of the substrates ATP or luciferin to luciferase decreases the affinity of the enzyme to the other substrate
-
additional information
-
irreversible aggregation because of the exposure of its hydrophobic sites followed by structural changes leads to its further inactivation
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-synuclein
-
dose-dependent enhancement of oxyluciferin formation, maximum rate of bioluminescence independent upon ATP concentration
-
Luciferin
-
preparations supplemented with extra luciferin provide maximum light emission
Polyethyleneglycol
-
stimulates activity by promoting the dissociation of inhibitory product from the enzyme
Polyvinylpyrrolidone
-
stimulates activity by promoting the dissociation of inhibitory product from the enzyme
Triton X-100
-
stimulates activity by promoting the dissociation of inhibitory product from the enzyme
[1,1,3,3-tetramethylguanidine][acetate]
-
enzyme shows increased activity and increased thermal stability
[1,1,3,3-tetramethylguanidine][lactate]
-
increase in concentration of [1,1,3,3-tetramethylguanidine][Lac] up to 0.25 M increases enzyme activity, and at concentrations more than 0.25 M enzyme activity is decreased. Optimum temperature and thermal stability studies show more stability of luciferase only in the presence of [1,1,3,3-tetramethylguanidine][Lac]
[1,1,3,3-tetramethylguanidine][propionate]
-
in the presence of [1,1,3,3-tetramethylguanidine][propionate], enzyme activities are decreased with an increase in ionic liquid concentration
[1,1,3,3-tetramethylguanidine][trichloroacetate]
-
enzyme shows decreased activity
[1,1,3,3-tetramethylguanidine][trifluoroacetate]
-
enzyme shows unchanged activity
AMP
-
activator of yellow-green light at pH 6.5; competitive with respect to MgATP2-
CoA
-
enhances luminescent activity of the wild-type enzyme about 2fold, highest activity at 1.2 mM CoA. For the N-terminal domain the effect of CoA is modest, 1.1fold enhancement, highest activity at 0.01 mM CoA. Addition of CoA at higher concentrations inhibits the luminescence activity
additional information
-
nonionic buffers; polyethyleneglycol-nonionic micelle-forming substances, anionic, cationic and zwitterionic surfactants tested, stimulation is concentration-dependent
-
additional information
-
GMP, UMP, CMP, IMP, 3'-AMP, 3',5'-cyclic AMP, ADP and free ATP tested
-
additional information
-
several cytidine nucleotides and CoA change the light emission pattern by promoting the dissociation of the oxidized luciferin from the enzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.176
(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.07
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.061
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 9.1, temperature not specified in the publication
0.02
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.00025
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme F250S; pH 8.6, mutant enzyme G246A
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0004
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme A243G
0.0008
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme S247F
0.001
ATP
-
mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0038
ATP
-
150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.004
ATP
-
free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol
0.008
ATP
-
mutant I423L/D436G/L530R, in the presence of 0.001 mM D-luciferin
0.009
ATP
-
mutant D436G, in the presence of 0.001 mM D-luciferin; mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.029
ATP
-
recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.041
ATP
-
recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0456
ATP
-
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.047
ATP
-
mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2; mutant I423L, in the presence of 0.001 mM D-luciferin
0.0538
ATP
-
mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.054
ATP
-
mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2; mutant L530R, in the presence of 0.001 mM D-luciferin
0.06
ATP
-
recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C; recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.06
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][acetate]
0.061
ATP
-
recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.077
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][acetate]
0.0778
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][lactate]; pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][propionate]
0.093
ATP
-
recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.094
ATP
-
150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.1
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
0.1 - 1
ATP
-
pH 7.8, temperature not specified in the publication, native enzyme
0.11
ATP
-
two catalytically active sites: first site with a Km for ATP of 0.11 mM is responsible for initial flash, a second site with a Km for ATP of 0.02 mM catalyses the continuous low production of light
0.111
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.111
ATP
-
pH 7.8, temperature not specified in the publication, native enzyme
0.1125
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][lactate]
0.114
ATP
-
0.094 mM luciferin, without alpha-synuclein; 0.188 mM luciferin, in presence of alpha-synuclein
0.133
ATP
-
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.151
ATP
-
recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.16
ATP
-
recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C; recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.16
ATP
-
wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2; wild-type, in the presence of 0.001 mM D-luciferin
0.166
ATP
-
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.182
ATP
-
recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.215
ATP
-
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.283
ATP
-
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.7
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][propionate]
1.666
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
2.25
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.015
D-firefly luciferin
pH 7.8, 22°C, recombinant mutant F255Y
0.019
D-firefly luciferin
pH 7.8, 22°C, recombinant wild-type enzyme
0.001
D-luciferin
-
mutant I423L/D436G/L530R, in the presence of 0.01 mM ATP; wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0018
D-luciferin
-
mutant enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.002
D-luciferin
-
mutant D436G, in the presence of 0.01 mM ATP; mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.0037
D-luciferin
-
mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.004
D-luciferin
-
recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.004
D-luciferin
-
mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2; mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2; mutant I423L, in the presence of 0.01 mM ATP; mutant L530R, in the presence of 0.01 mM ATP
0.0043
D-luciferin
-
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.006
D-luciferin
-
recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.008
D-luciferin
-
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.009
D-luciferin
-
recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.01
D-luciferin
-
recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.01
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][acetate]; pH 7.8, temperature not specified in the publication, native enzyme
0.01
D-luciferin
-
pH 7.8, temperature not specified in the publication, native enzyme
0.011
D-luciferin
-
recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C; recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.012
D-luciferin
-
recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0125
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][lactate]
0.014
D-luciferin
-
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.015
D-luciferin
-
recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.016
D-luciferin
-
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.02
D-luciferin
-
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.02
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
0.021
D-luciferin
-
mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2; wild-type, in the presence of 0.001 mM D-luciferin
0.0211
D-luciferin
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.022
D-luciferin
-
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.024
D-luciferin
-
recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C; recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0625
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][lactate]
0.07
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.2
D-luciferin
-
25°C, pH 8.5, mutant I232R; 35°C, pH 8, mutant A296C/A326C/I232R
0.2
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][propionate]
0.5
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
1
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][acetate]
1
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][propionate]
2.5
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.008
Luciferin
-
free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol
0.016
Luciferin
-
90 microM ATP, presence of 0.1 microM of N-quinolin-2-ylbenzamide
0.053
Luciferin
-
90 microM ATP, presence of 1 microM of N-quinolin-2-ylbenzamide
0.0006
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme A243G
0.0008
luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0046
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme S247F
additional information
additional information
-
increase of the Km with increasing ionic strength
-
additional information
additional information
-
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.14 mM
-
additional information
additional information
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.24 mM
-
additional information
additional information
-
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.24 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.00063
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.0067
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 9.1, temperature not specified in the publication
0.00051
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.01
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.11
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 9.1, temperature not specified in the publication
0.03
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
5'-O-[hydroxy({[(2Z)-2-(6-oxo-1,3-benzothiazol-2(6H)-ylidene)-2,3-dihydro-1,3-thiazol-4-yl]carbonyl}oxy)phosphoryl]adenosine
0.00034
5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine
-
for luciferyl adenylate
additional information
5'-O-[hydroxy({[(2Z)-2-(6-oxo-1,3-benzothiazol-2(6H)-ylidene)-2,3-dihydro-1,3-thiazol-4-yl]carbonyl}oxy)phosphoryl]adenosine
-
value between 0.0000025-0.00125 mM
additional information
dehydroluciferyl adenylate
-
value between 0.0000025 - 0.00125 mM
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid
Photinus pyralis;
-
-
0.00021
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
Photinus pyralis;
-
-
0.0008
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
Photinus pyralis;
-
-
0.00032
2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone
Photinus pyralis;
-
-
0.0013
2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline
Photinus pyralis;
-
-
0.00041
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
Photinus pyralis;
-
-