Information on EC 1.13.12.7 - Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)

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The expected taxonomic range for this enzyme is: Protostomia

EC NUMBER
COMMENTARY
1.13.12.7
-
RECOMMENDED NAME
GeneOntology No.
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Photinus luciferin + O2 + ATP = oxidized Photinus luciferin + CO2 + AMP + diphosphate + hnu
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
hydrolysis
-
-
oxidation
-
-
-
-
oxidation
-
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Photinus-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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beetle luciferase
Q5USC8
-
beetle luciferase
Q2TNU5
-
beetle luciferase
Macrolampis sp2
-
-
beetle luciferase
Q9U4U7
-
beetle luciferase
Q9U4U8
-
beetle luciferase
-
-
beetle luciferase
-
-
CBG99luc
-
red-emitting luciferase, commercial preparation
CBRluc
-
green-emitting luciferase, commercial preparation
firefly luciferase
-
-
-
-
firefly luciferase
Q5USC8
-
firefly luciferase
Q9BLZ2
-
firefly luciferase
Q2TNU5
-
firefly luciferase
Q5UFR2
-
firefly luciferase
P13129
-
firefly luciferase
Q26304
-
firefly luciferase
Macrolampis sp2
-
-
firefly luciferase
P08659
-
firefly luciferase
-
-
firefly luciferase
Q9U4U7
-
firefly luciferase
Q9U4U8
-
firefly luciferase
-
-
firefly luciferin luciferase
-
-
-
-
Luc
Q2TNU5
-
luciferase
Q5USC8
-
luciferase
Q25118
-
luciferase
Q8T6U3
-
luciferase
Q27688
-
luciferase
Q5UFR2
-
luciferase
Q1WLP6
-
luciferase
Q01158
-
luciferase
-
-
luciferase
Q26304
-
luciferase
Q27757
-
luciferase
Q9U4U7
-
luciferase
Q9U4U8
-
luciferase
AF116843
-
luciferase
Q26076
-
luciferase
Q9GPF9
-
luciferase
Q717B6
-
luciferase
Q718F0
-
luciferase (firefly luciferin)
-
-
-
-
luciferase FM
-
mutant luciferase
oxygen 4-oxidoreductase
-
-
PC3-Luc
-
-
Photinus luciferin 4-monooxygenase (ATP-hydrolyzing)
-
-
-
-
Photinus pyralis luciferase
-
-
-
-
Photinus pyralis luciferase
-
-
Ppy
P08659
-
Ppy
Q27758
recombinant firefly luciferase
Ppy
Q27758
recombinant Photinus pyralis luciferase containing the additional N-terminal peptide Gly-Pro-Leu-Gly-Ser
Ppy GR-TS
Q27758
green-emitting luciferase
Ppy RE-TS
Q27758
red-emitting luciferase
CAS REGISTRY NUMBER
COMMENTARY
61970-00-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
European glow-worm
TrEMBL
Manually annotated by BRENDA team
wild-type emits green light
UniProt
Manually annotated by BRENDA team
Macrolampis sp2
-
-
-
Manually annotated by BRENDA team
naturally green-emitting luciferase at pH 7.8
UniProt
Manually annotated by BRENDA team
-
AF116843
GenBank
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
fatty acyl-CoA synthesis, acyl-adenylate/thioester-forming enzyme
physiological function
-
catalyzes visible light emission
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4'-methyl-D-luciferin + ATP + O2
?
show the reaction diagram
-
-
-
-
?
5,5'-dimethylluciferin + ATP + O2
dehydroluciferin-adenylate + diphosphate
show the reaction diagram
-
produces only red light, 6-amino and 4 hydroxy analogs tested
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv
show the reaction diagram
-
-
-
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv + ?
show the reaction diagram
-
-
-
-
?
5,5-dimethylluciferin + ATP
5,5-dimethyloxyluciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
5-methylluciferin + ATP
6-methyloxyluciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
5-methylluciferin + ATP + O2
?
show the reaction diagram
-
-
-
-
?
5-monomethyl-luciferyl-O-adenosine monophosphate + ?
5-monomethyloxyluciferin + hv + ?
show the reaction diagram
-
-
-
-
?
6'-amino-D-luciferin + ATP
? + hv
show the reaction diagram
-
-
-
-
?
6'-amino-D-luciferin + ATP + O2
?
show the reaction diagram
-
-
-
-
?
8-anilino-1-naphthalene-sulfonate + ?
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-tetraphosphate + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
0.75% light response relative to ATP
-
?
ADP
ATP + AMP
show the reaction diagram
-
-
reaction inhibited by P1,P5-di(adenosine-5'-)pentaphosphate, but independent of luciferin
?
arachidonic acid + ATP + CoA
arachidonoyl-CoA + ?
show the reaction diagram
-
-
-
-
?
arachidonic acid + ATP + CoA
arachidonoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + O2 + oxyluciferin
?
show the reaction diagram
-
assay at pH 7.5, 24-27C
-
-
?
coelenterazine disulfate + ATP + O2 + H2O
coelenteramide disulfate + AMP + CO2 + diphosphate
show the reaction diagram
-
-
-
?
D-5,5-dimethylluciferyl-adenylate + O2
?
show the reaction diagram
-
yellow-green color of luminescence
-
-
?
D-5,5-dimethylluciferyl-adenylate + O2 + ATP
?
show the reaction diagram
Q718F0
red color of luminescence
-
-
?
D-aminoluciferin + ATP + O2
?
show the reaction diagram
-
assay at 37C. 5 min
-
-
?
D-luciferin + ATP
diphosphate + luciferyl-adenylate
show the reaction diagram
-
-
-
-
r
D-luciferin + ATP + O2
?
show the reaction diagram
-
assay at pH 7.5, 24-27C
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate
show the reaction diagram
P08659
-
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate
show the reaction diagram
-
-
-
-
r
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate + H2O + hv
show the reaction diagram
-
-
-
-
r
D-luciferin + ATP + O2
luciferyl-AMP + diphosphate
show the reaction diagram
-
assay at pH 7.8
-
-
r
D-luciferin + ATP + O2
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q5UFR2
assay at 25C, pH 7.8
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate
show the reaction diagram
-
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + ATP + O2
oxyluciferin + CO2 + AMP + hv + diphosphate
show the reaction diagram
-
-
-
-
?
D-luciferin + O2
?
show the reaction diagram
-
10 microM, assay at pH 7.5
-
-
?
D-luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q5USC8
-
-
-
-
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q27758
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q9U4U8
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q9U4U7
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q9BLZ2
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q5UFR2
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
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
show the reaction diagram
-
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
oxyluciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
r
D-luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
?
D-luciferyl-adenylate + O2
oxyluciferin + CO2 + AMP + hv
show the reaction diagram
-
-
-
-
ir
D-luciferyl-AMP + O2
dehydroluciferyl-AMP + H2O2
show the reaction diagram
-
-
-
-
ir
D-luciferyl-O-adenosine monophosphate + ?
?
show the reaction diagram
-
-
-
-
?
D-naphthylluciferin + ATP + O2
?
show the reaction diagram
-
-
-
-
?
D-quinolylluciferin + ATP + O2
?
show the reaction diagram
-
-
-
-
?
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
show the reaction diagram
P13129
-
-
-
?
dehydroluciferin + ATP
dehydroluciferyl-AMP + diphosphate
show the reaction diagram
-
-
-
-
r
dehydroluciferin + ATP + O2
diphosphate + dehydroluciferin-adenylate
show the reaction diagram
-
-
-
?
dehydroluciferin + CoA
dehydroluciferyl-CoA
show the reaction diagram
-
-
-
-
?
dehydroluciferyladenylate + CoA
dehydroluciferyl-CoA + ?
show the reaction diagram
-
-
-
-
?
deoxyATP + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
fatty acid + ATP + CoA
fatty acyl-CoA + AMP
show the reaction diagram
-
-
-
-
?
L-luciferin + CoA + ATP
luciferyl-CoA + AMP + diphosphate
show the reaction diagram
-
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
-
-
?
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
show the reaction diagram
P13129
-
-
-
?
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + CoA
show the reaction diagram
-
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + CoA
show the reaction diagram
-
linoleic acid concentration above 10 microM has an inhibitory effect
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
linolenic acid + ATP + CoA
linolenoyl-CoA + AMP + CoA
show the reaction diagram
-
-
-
-
?
linolenic acid + ATP + CoA
linolenoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
luciferin + ATP + O2
diadenosine 5',5''-P1,P4-tetraphosphate
show the reaction diagram
-
-
-
r
luciferin + ATP + O2
?
show the reaction diagram
-
assay at 25C, pH 7.8
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
Q26304
-
-
-
?
luciferin + ATP + O2
oxyluciferin + AMP + CO2 + diphosphate
show the reaction diagram
-
-
-
-
?
luciferin + MgATP2-
AMP + diphosphate
show the reaction diagram
-
-
-
-
-
luciferin + MgATP2-
AMP + diphosphate
show the reaction diagram
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
-
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
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
show the reaction diagram
-
-
luciferase modulates emission color by controlling the resonance-based deloclization of the anionic keto form of the oxyluciferin excited state
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
?
show the reaction diagram
-
assay at pH 7.8
-
-
?
luciferyl adenylate + O2
dehydroluciferyl adenylate + ?
show the reaction diagram
-
-
-
-
?
luciferyl-adenylate
oxyluciferin + hnu
show the reaction diagram
P08659
-
-
-
-
luciferyl-adenylate + O2
oxyluciferin + AMP + CO2 + hv
show the reaction diagram
-
-
-
-
ir
luciferyl-AMP + O2
oxyluciferin + hv + CO2 + AMP + diphosphate
show the reaction diagram
-
-
-
-
r
luciferyl-O-adenosine monophosphate + ?
?
show the reaction diagram
-
-
-
-
?
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
show the reaction diagram
P13129
-
-
-
?
oleic acid + ATP + CoA
oleoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
P1,P5-di(adenosine-5'-)pentaphosphate + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
2.2% light response relative to ATP
-
?
palmitic acid + ATP + CoA
palmitoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
P08659
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
highly specific for ATP
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
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
show the reaction diagram
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + GTP
adenosine 5'-P1-tetraphospho-P4-5'''-guanosine
show the reaction diagram
-
-
-
?
polyethylene glycol-6-amino-D-luciferin
? + hv
show the reaction diagram
-
longer light emission
-
-
?
R-COOH + ATP
R-CO-AMP + diphosphate
show the reaction diagram
-
-
-
-
r
luciferyl-O-adenosine monophosphate + CoA
luciferyl-CoA + AMP
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
12 nucleoside triphosphates examined
-
-
-
additional information
?
-
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
-
additional information
?
-
P13129
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
coelenterazine disulfate + ATP + O2 + H2O
coelenteramide disulfate + AMP + CO2 + diphosphate
show the reaction diagram
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
highly specific for ATP
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
necessary
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
influences the interaction with triazine dyes
Cu2+
-
promotes the binding to Cibacron brilliant blue and Cibacron blue F3GA
Fe2+
-
influences the interaction with triazine dyes
Mg2+
-
activator with optimum concentration at 0.1 mM
Mg2+
-
concentration 5 mM, MgSO4, MgCl2, Mg(O2CCH3)2 equally suitable salts
Mg2+
-
necessary for the activation step
Mg2+
-
influences the interaction with triazine dyes
Mg2+
-
optimal concentration for wild-type enzyme and N-terminal domain: 10 mM
Mg2+
-
required
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)
Mg2+
-
required for activity
Mg2+
-
10 mM, required
Mg2+
Q5UFR2
required
Mg2+
Q718F0
essential
Ni2+
-
influences the interaction with triazine dyes
Zn2+
-
increasing concentration shifts the light wavelenghts to higher values
Zn2+
-
prevents dye inactivation and enhances activity
Mn2+
-
influences the interaction with triazine dyes
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid
-
common name indoprofen
(2Z)-1-(4-chlorophenyl)-3-(pyridin-2-ylamino)prop-2-en-1-one
-
-
(2Z)-3-[(2-bromophenyl)amino]-1-pyridin-2-ylprop-2-en-1-one
-
-
(2Z)-3-[(4-fluorophenyl)amino]-1-furan-2-ylprop-2-en-1-one
-
-
(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
1-phenyl-3-(5-phenylpyridin-2-yl)urea
-
10 microM, 20% inhibition
1-[3-(6-ethoxy-1,3-benzothiazol-2-yl)thiophen-2-yl]urea
-
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
-
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
-
-
2-(2-amino-3-methoxyphenyl)-4H-chromen-4-one
-
common name PD98059
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
-
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone
-
common name pifithrin-alpha
2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
-
-
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(3-fluorophenyl)-1,3-benzothiazole
-
-
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-chlorophenyl)-1,3-benzothiazole
-
-
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline
-
-
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-naphthalen-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(6'-hydroxy-2'-benzothiazolyl)-4-hydroxymethylthiazole
-
competitive inhibitor
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
-
common name SCS
2-methyl-6-(phenylethynyl)pyridine
-
common name MPEB
2-methyl-6-[(Z)-2-phenylethenyl]pyridine
-
common name SIB1893
2-phenylbenzothiazole
-
-
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
2-[5-(3,4-dichlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
2-[5-(3-chloro-4-methylphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
2-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
2-[5-(5-bromofuran-2-yl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
3',5'-cyclic AMP
-
competitive inhibitor
3',5'-cyclic AMP
-
-
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-diphenyl-1,2,4-oxadiazole
-
-
3-(2-hydroxyphenyl)-1H-benzo[f]chromen-1-one
-
common name flavonoid
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
-
-
3-chloro-N-(5-phenylpyridin-2-yl)benzamide
-
-
3-methyl-2-[(E)-phenyldiazenyl]phenol
-
-
-
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
-
-
3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
decrease of Fluc proteolysis, 2 microM
3-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-(3-methoxyphenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-(4-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-[2-(trifluoromethyl)phenyl]-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-[4-(trifluoromethyl)phenyl]-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
4-(1,3-benzothiazol-2-yl)benzonitrile
-
-
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-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
-
-
4-(dimethylamino)-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 35% 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-amino-N-(5-phenylpyridin-2-yl)benzamide
-
-
4-chloro-N-(5-phenylpyridin-2-yl)benzamide
-
-
4-methoxy-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 28% inhibition
4-methoxy-N-[(4-methylpyridin-2-yl)carbamoyl]benzamide
-
-
4-methyl-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 18% inhibition
4-methyl-N-(phenylmethyl)benzenesulfonamide
-
-
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
-
-
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
-
-
4-[5-(2-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
-
-
4-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-[5-(3-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
5'-O-[(N-dehydroluciferyl)-sulfamoyl]-adenosine
-
stable and potent reversibel inhibitor
5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine
-
competitive inhibitor
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
5-(2-bromophenyl)-3-(4-methylphenyl)-1,2,4-oxadiazole
-
-
5-(2-chloro-4-methylphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
-
-
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
-
-
5-anilino-1-naphthalene sulfonate
-
-
5-anilino-1-naphthalene sulfonate
-
competitive inhibitor
5-methyl-N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
-
5-naphthalen-2-yl-3-phenyl-1,2,4-oxadiazole
-
-
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
6-methyl-2-[(Z)-phenyldiazenyl]pyridin-3-ol
-
common name SIB1757
6-toluidino-2-naphthalene sulfonate
-
-
6-toluidino-2-naphthalene sulfonate
-
competitive inhibitor
arachidonic acid
-
concentration above 10 microM
arsenate
-
reversible inhibition
arsenate
-
lowers the flash height and extends the light emission for a given amount of ATP
ATP
-
mechanism
ATP
-
noncompetitive inhibitor
ATP
-
uncomplexed ATP is a competitive inhibitor with respect to MgATP2- complex
Bovine serum albumin
-
inhibition when present in large excess
-
CoA
-
above 0.1 mM, N-terminal domain
D-luciferin
-
inhibits CoA-ligase activity with L-luciferin, IC50: 0.135 mM against 0.1 mM L-luciferin
dehydroluciferin
-
competitive inhibitor
dehydroluciferin
-
-
dehydroluciferin
-
-
dehydroluciferyl adenylate
-
IC50: 6 nM
dehydroluciferyl adenylate
-
-
dehydroluciferyl-adenylate
-
tight-binding competitive inhibitor
dehydroluciferyl-CoA
-
IC50: 0.005 mM
diphosphate
-
depending on conditions
dithiothreitol
-
-
dodecanoic acid
-
competitive
Dodecanol
-
mixed-type inhibitor
dodecylamine
-
noncompetitive inhibitor
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
-
-
ethyl-2-benzothiazole sulfonate
-
competitive inhibitor
-
geneticin
-
induces nonsense suppression
gentamicin
-
induces nonsense suppression
Halothane
-
non-competitive inhibitor
iodoacetamide
-
-
L-1-tosylamido-2-phenethyl chlorometyl ketone
-
competitive inhibitor with respect to luciferin, noncompetitive with respect to ATP
Limulus amebocyte lysate
-
decreased luminescence intensity to 10%
-
linoleic acid
-
concentration above 10 microM
lipoic acid
-
-
Luciferin
-
noncompetitive inhibitor
Luciferin
-
inhibition if concentration is higher than 0.05 mM
myristic acid
-
-
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
-
common name DCB
N-(4-ethoxyphenyl)-2-methoxybenzamide
-
-
N-(5-methylpyridin-2-yl)benzamide
-
-
N-(5-phenylpyridin-2-yl)benzamide
-
; 10 microM, 27% inhibition
N-(5-phenylpyridin-2-yl)butanamide
-
10 mciroM, 22% inhibition
N-(5-phenylpyridin-2-yl)cyclohexanecarboxamide
-
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
-
-
N-(6-methoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
-
-
N-(6-methoxy-1,3-benzothiazol-2-yl)-3-methylthiophene-2-carboxamide
-
-
N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide
-
-
N-(6-phenylpyridin-2-yl)benzamide
-
10 microM, 30% inhibition
N-benzyl-5-phenylpyridin-2-amine
-
10 microM, 20% inhibition
N-pyridin-2-ylbenzamide
-
-
N-quinolin-2-ylbenzamide
-
-
N-tosyl-L-lysine chloromethyl ketone
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
competitive inhibitor with respect to luciferin, noncompetitive with respect to ATP, pH dependent, enzyme protected by dehydroluciferin-AMP
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
N-[5-(3,4-dichlorophenyl)pyridin-2-yl]benzamide
-
10 microM, 4% inhibition
N-[5-(3-chlorophenyl)pyridin-2-yl]benzamide
-
10 microM, 38% inhibition
N-[5-(4-chlorophenyl)pyridin-2-yl]benzamide
-
-
N-[5-(4-methoxyphenyl)pyridin-2-yl]benzamide
-
-
N-[5-(4-methylphenyl)pyridin-2-yl]benzamide
-
10 microM, 51% inhibition
N-[5-(4-tert-butylphenyl)pyridin-2-yl]benzamide
-
10 microM, 49% inhibition
N-[5-[(2,2-dimethylpropanoyl)amino]pyridin-2-yl]-3-hydroxybenzamide
-
-
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
N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
-
oleic acid
-
concentration above 10 microM
oxyluciferin
-
competitive inhibitor
p-mercuribenzoate
-
-
phenyl (5-phenylpyridin-2-yl)carbamate
-
-
-
pifithrin-alpha
-
20 microM, above 95% inhibiton
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
resveratrol
-
resveratrol is 3,5,4'-trihydroxystilbene, potent inhibitor
Ribose-5-phosphate
-
-
additional information
-
binding of one of the substrates ATP or luciferin to luciferase decreases the affinity of the enzyme to the other substrate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
alpha-synuclein
-
dose-dependent enhancement of oxyluciferin formation, maximum rate of bioluminescence independent upon ATP concentration
-
AMP
-
activator of yellow-green light at pH 6.5
AMP
-
activator of yellow-green light at pH 6.5; competitive with respect to MgATP2-
ATP
-
essential for luminescence reaction
ATP
-
essential for luminescence reaction, initiates luminescence reaction
ATP
Q718F0
essential for luminescence reaction
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
CoA
-
prevents rapid decay of light emission
diphosphate
-
stimulates light production under some conditions
Luciferin
-
preparations supplemented with extra luciferin provide maximum light emission
molecular oxygen
-
essential for luminescence reaction
-
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
Triphosphate
-
stimulates light production under some conditions
Triton X-100
-
stimulates activity by promoting the dissociation of inhibitory product from the enzyme
molecular oxygen
Q718F0
essential for luminescence reaction
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0.00015
-
ATP
-
; immobilized on activated Sepharose
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
0.002
-
ATP
-
immobilized enzyme
0.003
-
ATP
-
150 microM luciferin, two-site binding model
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 enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
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 25C
0.04
-
ATP
-
mutant E354K/ins356K
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 25C
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
0.0485
-
ATP
-
addition of luciferin 30 min after ATP
0.05
-
ATP
-
mutant E354Q/ins356K
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
0.0594
-
ATP
-
addition of luciferin 30 min before ATP
0.06
-
ATP
-
adenylate kinase activity
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 25C; recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
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 25C
0.063
-
ATP
-
mutant E354K
0.071
-
ATP
-
wild-type luciferase
0.086
-
ATP
-
0.094 mM luciferin, in presence of alpha-synuclein
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 25C
0.094
-
ATP
-
150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.095
-
ATP
-
mutant E354R/ins356K
0.0955
-
ATP
-
in 50 mM Tricine-NaOH buffer with 10 mM MgSO4, at pH 7.8
0.1
-
ATP
P08659
mutant ins356R
0.105
-
ATP
P08659
mutant ins356E; mutant ins356Q
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
0.11
-
ATP
-
soluble and immobilized enzyme
0.11
-
ATP
P08659
mutant ins356K
0.114
-
ATP
-
0.094 mM luciferin, without alpha-synuclein; 0.188 mM luciferin, in presence of alpha-synuclein
0.115
-
ATP
-
mutant E354R
0.12
-
ATP
P08659
wild-type luciferase
0.125
-
ATP
-
tricine buffer
0.133
-
ATP
-
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
0.133
-
ATP
-
wild-type luciferase
0.135
-
ATP
Q5UFR2
wild-type luciferase
0.138
-
ATP
-
150 microM luciferin, two-site binding model
0.14
-
ATP
-
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.15
-
ATP
-
mutant R213M
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 25C
0.157
-
ATP
-
0.188 mM luciferin, without alpha-synuclein
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 25C; recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
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
0.1602
-
ATP
-
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.166
-
ATP
-
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
0.168
-
ATP
Q5UFR2
mutant H245N
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 25C
0.1872
-
ATP
Q5UFR2
mutant H431Y
0.2
-
ATP
-
phosphate buffer
0.2
-
ATP
-
mutant R213E
0.215
-
ATP
-
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
0.23
-
ATP
-
wild-type enzyme
0.2484
-
ATP
Q5UFR2
mutant S284T
0.283
-
ATP
-
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
0.285
-
ATP
-
glycylglycine buffer
0.35
-
ATP
-
mutant Q338P
0.5
-
ATP
-
crude extract
0.5
-
ATP
-
mutant R337Q
6.9
-
ATP
-
N-terminal domain
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
0.0023
-
D-luciferin
-
mutant enzyme K443A
0.0024
-
D-luciferin
-
native luciferase
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 25C
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
0.0042
-
D-luciferin
-
mutant enzyme G246A
0.0043
-
D-luciferin
-
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.0047
-
D-luciferin
-
recombinant luciferase
0.006
-
D-luciferin
-
mutant enzyme G446I; mutant enzyme Q448A
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 25C
0.006
-
D-luciferin
P08659
mutant ins356E
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 25C
0.0089
-
D-luciferin
-
mutant enzyme K445Q
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 25C
0.009
-
D-luciferin
P08659
mutant ins356K
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 25C
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 25C; recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
0.011
-
D-luciferin
P08659
wild-type luciferase
0.011
-
D-luciferin
-
mutant E354K/ins356K
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 25C
0.012
-
D-luciferin
-
mutant E354Q/ins356K
0.013
-
D-luciferin
-
mutant E354K
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 25C
0.014
-
D-luciferin
-
mutant E354R/ins356K
0.015
-
D-luciferin
-
mutant enzyme H245A; wild-type enzyme
0.015
-
D-luciferin
-
wild-type enzyme
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 25C
0.015
-
D-luciferin
P08659
mutant ins356R
0.015
-
D-luciferin
-
-
0.0157
-
D-luciferin
-
mutant enzyme F250G
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 25C
0.016
-
D-luciferin
-
mutant E354R
0.01612
-
D-luciferin
Q5UFR2
wild-type luciferase
0.018
-
D-luciferin
-
mutant enzyme F247Y; mutant enzyme G316A
0.018
-
D-luciferin
P08659
mutant ins356Q
0.02
-
D-luciferin
-
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
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
-
mutant enzyme F250S
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 25C
0.023
-
D-luciferin
Q5UFR2
mutant H245N
0.023
-
D-luciferin
-
wild-type luciferase
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 25C; recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25C
0.026
-
D-luciferin
Q5UFR2
mutant H431Y
0.03
-
D-luciferin
-
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.03
-
D-luciferin
Q5UFR2
mutant S284T
0.06
-
D-luciferin
-
mutant enzyme G341A
0.067
-
D-luciferin
-
mutant enzyme K443A/K529A
0.085
-
D-luciferin
-
mutant enzyme I351A
0.099
-
D-luciferin
-
mutant enzyme T343A
0.124
-
D-luciferin
-
mutant enzyme F247L
0.13
-
D-luciferin
-
mutant enzyme L342A
0.133
-
D-luciferin
-
mutant enzyme A348V
0.17
-
D-luciferin
-
mutant enzyme S347A
0.2
-
D-luciferin
-
mutant enzyme G315A
0.23
-
D-luciferin
-
mutant enzyme F247A; mutant enzyme K529A
0.23
-
D-luciferin
-
mutant enzyme K529A
0.301
-
D-luciferin
-
mutant enzyme R218A
0.311
-
D-luciferin
-
mutant enzyme T251A
0.00038
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K443A
0.00055
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K443A/K529A
0.0015
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme G446I
0.0022
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme Q448A
0.0039
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K445Q
0.0047
-
D-luciferyl-O-adenosine monophosphate
-
wild-type enzyme
0.0126
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K529A
0.0149
-
dehydroluciferyl-adenylate
-
-
0.0982
-
L-luciferin
-
-
0.00741
-
lauric acid
-
-
0.0163
-
lauric acid
-
-
0.0136
-
linoleic acid
-
-
0.0136
-
linolenic acid
-
-
0.0072
-
Luciferin
-
wild-type enzyme
0.0079
-
Luciferin
-
addition of luciferin 30 min before ATP
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
0.0083
-
Luciferin
-
addition of luciferin 30 min after ATP
0.01
-
Luciferin
-
mutant R213M
0.012
-
Luciferin
-
immobilized on activated Sepharose
0.012
-
Luciferin
-
90 microM ATP
0.012
-
Luciferin
-
wild-type luciferase
0.013
-
Luciferin
-
mutant Q338P
0.014
-
Luciferin
-
mutant R213E
0.015
-
Luciferin
-
-
0.015
-
Luciferin
-
-
0.016
-
Luciferin
-
90 microM ATP, presence of 0.1 microM of N-quinolin-2-ylbenzamide
0.018
-
Luciferin
-
mutant R337Q
0.02
-
Luciferin
-
-
0.026
-
Luciferin
-
N-terminal domain
0.03
-
Luciferin
-
-
0.042
-
Luciferin
-
phosphate buffer
0.053
-
Luciferin
-
90 microM ATP, presence of 1 microM of N-quinolin-2-ylbenzamide
0.055
-
Luciferin
-
glycylglycine buffer
0.074
-
Luciferin
-
0.5 mM ATP, in presence of alpha-synuclein
0.088
-
Luciferin
-
0.2 mM ATP, in presence of alpha-synuclein
0.134
-
Luciferin
-
0.15 mM ATP, in presence of alpha-synuclein
0.188
-
Luciferin
-
0.15 mM ATP, without alpha-synuclein
0.189
-
Luciferin
-
0.5 mM ATP, without alpha-synuclein
0.192
-
Luciferin
-
0.2 mM ATP, without alpha-synuclein
0.197
-
Luciferin
-
0.1 mM ATP, without alpha-synuclein
0.218
-
Luciferin
-
0.1 mM ATP, in presence of alpha-synuclein
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
0.0077
-
luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0114
-
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme F250S
0.0127
-
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme G246A
0.025
-
MgATP2-
-
-
0.029
-
MgATP2-
-
mutant enzyme G246A
0.0486
-
MgATP2-
-
mutant enzyme K443A
0.069
-
MgATP2-
-
mutant enzyme K445Q
0.073
-
MgATP2-
-
mutant enzyme G446I
0.08
-
MgATP2-
-
mutant enzyme F247Y
0.107
-
MgATP2-
-
mutant enzyme G316A
0.133
-
MgATP2-
-
mutant enzyme F250S
0.16
-
MgATP2-
-
-
0.16
-
MgATP2-
-
wild-type enzyme
0.166
-
MgATP2-
-
mutant enzyme F250G
0.2
-
MgATP2-
-
mutant enzyme G341A
0.226
-
MgATP2-
-
mutant enzyme F247L
0.24
-
MgATP2-
-
mutant enzyme H245A
0.285
-
MgATP2-
-
mutant enzyme I351A
0.341
-
MgATP2-
-
mutant enzyme Q448A
0.344
-
MgATP2-
-
mutant enzyme S347A
0.56
-
MgATP2-
-
mutant enzyme K443A/K529A
0.857
-
MgATP2-
-
mutant enzyme T343A
1.038
-
MgATP2-
-
mutant enzyme A348V
1.2
-
MgATP2-
-
mutant enzyme G315A; mutant enzyme K529A; mutant enzyme L342A
1.2
-
MgATP2-
-
mutant enzyme K529A
2
-
MgATP2-
-
mutant enzyme T251A
3.5
-
MgATP2-
-
mutant enzyme F247A
0.0147
-
oxyluciferin
-
-
6.2
-
MgATP2-
-
mutant enzyme R218A
additional information
-
additional information
-
increase of the Km with increasing ionic strength
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000000157
-
D-luciferin
-
mutant enzyme K443A/K529A
0.0000629
-
D-luciferin
-
mutant enzyme K443A
0.0001
-
D-luciferin
-
mutant enzyme K529A
0.0002
-
D-luciferin
-
mutant enzyme G315A; mutant enzyme G341A
0.00025
-
D-luciferin
-
mutant enzyme K529A
0.001
-
D-luciferin
-
mutant enzyme T343A
0.004
-
D-luciferin
-
mutant enzyme R218A
0.007
-
D-luciferin
-
mutant enzyme F247A
0.013
-
D-luciferin
-
mutant enzyme F250G
0.02
-
D-luciferin
-
mutant enzyme G446I
0.03
-
D-luciferin
-
mutant enzyme S347A
0.036
-
D-luciferin
-
mutant enzyme F250S
0.041
-
D-luciferin
-
mutant enzyme H245A
0.043
-
D-luciferin
-
mutant enzyme T251A
0.049
-
D-luciferin
-
mutant enzyme G316A
0.06
-
D-luciferin
-
mutant enzyme G246A
0.064
-
D-luciferin
-
mutant enzyme A348V
0.0875
-
D-luciferin
-
mutant enzyme Q448A
0.098
-
D-luciferin
-
mutant enzyme F247Y
0.106
-
D-luciferin
-
mutant enzyme L342A
0.116
-
D-luciferin
-
mutant enzyme F247L
0.125
-
D-luciferin
-
wild-type enzyme
0.167
-
D-luciferin
-
wild-type enzyme
0.19
-
D-luciferin
-
mutant enzyme I351A
0.24
-
D-luciferin
-
mutant enzyme K445Q
0.0000311
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K443A/K529A
0.000101
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K443A
0.021
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme G446I
0.095
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme Q448A
0.175
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K529A
0.23
-
D-luciferyl-O-adenosine monophosphate
-
wild-type enzyme
0.32
-
D-luciferyl-O-adenosine monophosphate
-
mutant enzyme K445Q
0.278
-
lauric acid
-
-
0.651
-
lauric acid
-
-
0.13
-
linolenic acid
-
-
1.6
-
Luciferin
-
-
0.000000157
-
MgATP2-
-
mutant enzyme K443A/K529A
0.0000629
-
MgATP2-
-
mutant enzyme K443A
0.00025
-
MgATP2-
-
mutant enzyme K529A
0.02
-
MgATP2-
-
mutant enzyme G446I
0.0875
-
MgATP2-
-
mutant enzyme Q448A
0.167
-
MgATP2-
-
wild-type enzyme
0.24
-
MgATP2-
-
mutant enzyme K445Q
additional information
-
additional information
-
kinetic of light emission
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0006
-
2-(6'-hydroxy-2'-benzothiazolyl)-4-hydroxymethylthiazole
-
-
0.9
-
3',5'-cyclic AMP
-
-
0.0014
-
4-[5-(2-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
0.03
-
4-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
0.000034
-
5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine
-
for D-luciferin
0.000041
-
5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine
-
for MgATP2-
0.00034
-
5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine
-
for luciferyl adenylate
0.23
-
5-anilino-1-naphthalene sulfonate
-
-
0.0059
-
6-toluidino-2-naphthalene sulfonate
-
-
0.00001
-
dehydroluciferin
-
-
0.003
0.004
L-luciferin
-
-
0.25
-
L-tosylamido-2-phenethyl chloromethyl ketone
-
-
-
0.000026
-
lipoic acid
-
-
1
-
MgATP2-
-
-
0.00053
-
myristic acid
-
-
0.73
-
N-tosyl-L-lysine chloromethyl ketone
-
-
0.0005
-
oxyluciferin
-
-
0.3
-
phosphate
-
-
0.002
-
resveratrol
-
-
0.34
-
Ribose-5-phosphate
-
-
0.00034
-
5'-O-[(N-dehydroluciferyl)-sulfamoyl]-adenosine
-
-
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
0.001
-
dehydroluciferin
-
-
additional information
-
dehydroluciferyl adenylate
-
value between 0.0000025 - 0.00125 mM
0.0000038
-
dehydroluciferyl-adenylate
-
-
additional information
-
L-luciferin
-
value between 0.003-0.004 mM
0.25
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
-
additional information
-
oxyluciferin
-
value between 0.0005-0.002 mM
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0002
-
(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid
-
-
0.002
-
(2Z)-1-(4-chlorophenyl)-3-(pyridin-2-ylamino)prop-2-en-1-one
-
-
0.00008
-
(2Z)-3-[(2-bromophenyl)amino]-1-pyridin-2-ylprop-2-en-1-one
-
-
0.001
-
(2Z)-3-[(4-fluorophenyl)amino]-1-furan-2-ylprop-2-en-1-one
-
-
0.00021
-
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
-
-
0.0008
-
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
-
-
0.0006
-
1-[3-(6-ethoxy-1,3-benzothiazol-2-yl)thiophen-2-yl]urea
-
-
0.00008
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
-
-
0.0062
-
2-(2-amino-3-methoxyphenyl)-4H-chromen-4-one
-
-
0.0049
-
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
-
0.0054
-
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
-
0.0005
-
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0006
-
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.00032
-
2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone
-
-
0.0077
-
2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
0.0113
-
2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
0.0019
-
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
-
-
0.0032
-
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
-
-
0.0028
-
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0038
-
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0078
-
2-(3-fluorophenyl)-1,3-benzothiazole
-
-
0.0242
-
2-(3-fluorophenyl)-1,3-benzothiazole
-
-
0.0011
-
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0015
-
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0014
-
2-(4-chlorophenyl)-1,3-benzothiazole
-
-
0.0045
-
2-(4-chlorophenyl)-1,3-benzothiazole
-
-
0.0035
-
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0038
-
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0013
-
2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline
-
-
0.00041
-
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
0.00086
-
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.0013
-
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
0.00036
-
2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
0.001
-
2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
0.004
-
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
0.000038
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.00008
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0001
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0013
-
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0171
-
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0001
-
2-(5-naphthalen-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0019
-
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0144
-
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0008
-
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
-
-
0.0047
-
2-methyl-6-(phenylethynyl)pyridine
-
-
0.0043
-
2-methyl-6-[(Z)-2-phenylethenyl]pyridine
-
-
0.00008
-
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
0.0028
-
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
0.00084
-
2-[5-(3,4-dichlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
0.00022
-
2-[5-(3-chloro-4-methylphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
0.0005
-
2-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
0.0032
-
2-[5-(5-bromofuran-2-yl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
0.00005
-
3-(2-hydroxyphenyl)-1H-benzo[f]chromen-1-one
-
-
0.0006
-
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
-
-
0.0083
-
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
-
-
0.00016
-
3-chloro-N-(5-phenylpyridin-2-yl)benzamide
-
-
0.00004
-
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
-
-
0.0014
-
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
-
-
0.0002
-
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
0.00032
-
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
0.0021
-
4-(1,3-benzothiazol-2-yl)benzonitrile
-
-
0.0063
-
4-(1,3-benzothiazol-2-yl)benzonitrile
-
-
0.0007
-
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
-
-
0.0024
-
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.024
-
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
0.0007
-
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
0.0027
-
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
0.0057
-
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
-
-
0.0061
-
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
-
-
0.0017
-
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
-
-
0.0012
-
4-amino-N-(5-phenylpyridin-2-yl)benzamide
-
-
0.00041
-
4-methoxy-N-[(4-methylpyridin-2-yl)carbamoyl]benzamide
-
-
0.0003
-
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
-
-
0.0048
-
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
-
-
0.024
-
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
-
-
0.00032
-
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
-
-
0.0005
-
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
-
-
0.000054
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
0.00015
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
0.0002
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
0.001
-
5-(2-bromophenyl)-3-(4-methylphenyl)-1,2,4-oxadiazole
-
-
0.00015
-
5-(2-chloro-4-methylphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
0.0003
-
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
-
-
0.0028
-
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
-
-
0.00058
-
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
-
-
0.0017
-
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
-
-
0.0011
-
5-methyl-N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
-
0.00041
-
5-naphthalen-2-yl-3-phenyl-1,2,4-oxadiazole
-
-
0.0032
-
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
0.0056
-
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
0.00067
-
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
-
-
0.0015
-
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
-
-
0.0022
-
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
0.0041
-
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
0.0043
-
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
0.0089
-
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
0.0134
-
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
0.03
-
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
0.0045
-
6-methyl-2-[(Z)-phenyldiazenyl]pyridin-3-ol
-
-
0.135
-
D-luciferin
-
inhibits CoA-ligase activity with L-luciferin, IC50: 0.135 mM against 0.1 mM L-luciferin
0.000006
-
dehydroluciferyl adenylate
-
IC50: 6 nM
0.0000074
-
dehydroluciferyl-adenylate
-
2.5 nM D-luciferin
0.0000085
-
dehydroluciferyl-adenylate
-
5 nM D-luciferin
0.0000103
-
dehydroluciferyl-adenylate
-
10 nM D-luciferin
0.0000132
-
dehydroluciferyl-adenylate
-
20 nM D-luciferin
0.000022
-
dehydroluciferyl-adenylate
-
40 nM D-luciferin
0.005
-
dehydroluciferyl-CoA
-
IC50: 0.005 mM
0.0009
-
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
-
-
0.00005
-
lipoic acid
-
-
0.00068
-
myristic acid
-
-
0.0045
-
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
-
-
0.0006
-
N-(4-ethoxyphenyl)-2-methoxybenzamide
-
-
0.0064
-
N-(5-methylpyridin-2-yl)benzamide
-
-
0.000069
-
N-(5-phenylpyridin-2-yl)benzamide
-
-
0.0024
-
N-(5-phenylpyridin-2-yl)cyclohexanecarboxamide
-
-
0.00065
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
-
-
0.0012
-
N-(6-methoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
-
-
0.0005
-
N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide
-
-
0.000069
-
N-pyridin-2-ylbenzamide
-
-
0.007
-
N-quinolin-2-ylbenzamide
-
-
0.0019
-
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
0.0029
-
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
0.003
-
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
0.0031
-
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
0.00056
-
N-[5-(4-chlorophenyl)pyridin-2-yl]benzamide
-
-
0.00031
-
N-[5-(4-methoxyphenyl)pyridin-2-yl]benzamide
-
-
0.0007
-
N-[5-[(2,2-dimethylpropanoyl)amino]pyridin-2-yl]-3-hydroxybenzamide
-
-
0.0011
-
N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
detection of activity in light units/mg of protein; luminometer measures in Escherichia coli, Rhizobium melioti, Medicago sativa; quantum yield 0.88 with respect to luciferin
additional information
-
-
assay method
additional information
-
-
28000 light units/mg after crystallization
additional information
-
-
quantum yield 0.88 with respect to luciferin
additional information
-
-
-
additional information
-
-
relative specific activity is 30% lower at pH 8.7 than at pH 7.8
additional information
-
-
enzyme from crude extract shows a specific activity of 6100000 relative light units per mg, purified enzyme shows a specific activity of 104000000 relative light units per mg
additional information
-
-
41 relative luminescence units
additional information
-
Q5UFR2
11500000000000 relative light units/mg, mutant H245N; 15000000000000 relative light units/mg, wild-type luciferase; 2500000000000 relative light units/mg, mutant H431Y; 3600000000000 relative light units/mg, mutant S284T
additional information
-
-
lower luminescence activity when another substrate than D-luciferin is used: only 10% luminescence activity with 6'-amino-D-luciferin, only 5% luminescence activity with 4'-methyl-D-luciferin, only 7% luminescence activity with D-quinolylluciferin, only 1.5% luminescence activity with D-naphthylluciferin, only 16% luminescence activity with D-5,5-dimethylluciferyl-adenylate
additional information
-
-
12000000000 relative light units/s/mg, mutant E354Q/ins356K; 15000000000 relative light units/s/mg, wild-type luciferase; 18000000000 relative light units/s/mg, mutant E354K/ins356K; 19000000000 relative light units/s/mg, mutant E354K; 20000000000 relative light units/s/mg, mutant E354R; 23000000000 relative light units/s/mg, mutnat E354R/ins356K
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
6
-
red emitted light
5.4
-
-
red emitted light
5.5
-
P08659
shift of emission spectra to red region
6.9
-
-
in vivo detection
7
-
-
emission at 562 nm
7.3
-
-
mutant R337Q
7.4
-
-
optimum for binding to triazine dyes
7.5
7.8
-
yellow-green emitted light
7.5
-
-
assay at
7.6
-
-
tricine buffer
7.6
-
-
yellow-green emitted light
7.8
-
-
purified enzyme
7.8
-
-
phosphate buffer
7.8
-
-
different recombinant mutants
7.8
-
Q5UFR2
assay at
7.8
-
-
assay at, shift in bioluminescence spectra to red region by increase in temperature to 42C
7.8
-
P08659
-
7.8
-
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at
8
-
Q5UFR2
wild-type luciferase, mutant S284T
8.5
-
Q5UFR2
mutant H245N and H431Y
8.6
-
-
reaction with 5,5-dimethyl-luciferyl-O-adenosine monophosphate
additional information
-
-
pH 7.8 crude extract
additional information
-
-
pH 7.5
additional information
-
-
pH 7.3 with immobilized enzyme; pH 7.8 soluble enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.8
-
bioluminescence spectra independent from pH, for mutants Y35N, Y35H and F16L/A40S
6.5
8.5
-
pH 6.5: about 45% of activity maximum, pH 8.5: about 35% of activity maximum
7.5
8
-
pH up to 8 red light occurs instead of yellow-green light
7.5
8
-
pH below 7.5 emission shifts to longer wavelengths; pH up to 8 red light occurs instead of yellow-green light
7.5
8.5
-
peak emission at 560 nm
7.5
8.5
-
-
7.5
8.5
-
depending on mutation
additional information
-
-
buffers with pKa from 7.2 to 8.4 tested and no relationship with activity found
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
purified
24
-
Q5UFR2
wild-type luciferase, mutant H245N and H431Y
25
-
Q5UFR2
assay at
25
-
-
assay at
30
-
Q5UFR2
mutant S284T
30
-
-
in presence of sucrose, proline or sorbitol
37
-
-
assay at
additional information
-
-
shift in bioluminescence spectra to red region by increase in temperature to 42C
additional information
-
-
shift of emission to red emitting light
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
27
-
assay at
25
35
-
depending on mutation
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
-
calculation from amino acid sequence
6
-
-
isoelectric focusing
6.2
-
-
calculated with ExPASy Compute pI/MW tool
7.2
-
-
His10-tagged wild type enzyme
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
chromophore organs at the end of ventral arms
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
localized in peroxisomes when expressed in mammalian, plant and yeast cells
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
52000
-
high speed equilibrium sedimentation after 5 M guanidine hydrochloride
50000
52000
-
gel filtration
50000
-
-
minimum molecular weight, gel filtration, high-speed sedimentation equilibrium ultracentrifugation and combination of sedimentation and diffusion coefficients
53600
-
-
sedimentation velocity
60750
-
-
-
61160
-
-
calculated from sequence of cDNA
62000
-
P08659
SDS-PAGE
62000
-
-
SDS-PAGE
65500
-
-
calculated from amino acid sequence
89000
91000
-
low speed equilibrium sedimentation
92000
95000
-
high speed equilibrium sedimentation
100000
-
-
from sedimentation velocity of the crystalline form
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 49000, N-terminal domain, SDS-PAGE; x * 61200, wild-type enzyme, SDS-PAGE
dimer
-
2 * 50000 not separated
dimer
-
2 * 500000 sedimentation equilibrium study of guanidine hydrochloride-treated enzyme; two non identical subunits
dimer
-
1 * alpha (catalytic subunit) + 1 * beta; two non identical subunits
dimer
-
2 * 48000-53000, various methods
dimer
-
only one subunit is enzymatically active
dimer
-
two non identical subunits
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallization was achieved using the micro batch technique under oil at 4C, 2 A resolution structure was determined at -173C, using isomorphous replacement, the protein is folded into two compact domains. The large N-terminal domain consists of a beta-barrel and two beta-sheets. The sheets are flanked by alpha-helices to form a layered structure, the C-terminal portion forms a distinct domain, separated from the N-terminal domain by a wide cleft
-
extraction, 2 gel elutions, 5 crystallizations
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
all spectra undergo a red-shift when cells are assayed under acidic conditions, whereas a blue-shift is observed at pH 8.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
40
Q5UFR2
at 35C native luciferase completely inactive, mutant H245N still 80% residual activity, mutant S284T and H431Y about 20% residual activity
25
45
-
activity starts to decrease above 25C and is almost completely lost at 45C
32
-
-
mutant E354R, E354K, E354R/ins356Arg with greater thermostability than wild-type luciferase
35
-
-
about 70% loss of activity within 10 min, no residual activity after 60 min, in presence of osmolytes higher residual activity after 60 min: 90% with 1.5 M sucrose, 50% with 1.5 M sorbitol, 35% with 1.5 M proline
37
-
-
half-life: 3.06 min for wild-type enzyme,8.5 min for mutant enzyme E345K/T214A, 15.5 min for E345K/I232A/T214A, 7.36 min for E345K/A215L, 72.4 min for E345K/I232A/T214A/F295L/S420T, 82.1 min for E345K/A215L/I232A/T214A/F295L, 75.1 min for E345K/A215L/I232A/T214A
40
-
-
at 40C for 45 min the activity of the enzyme decreased to less than 1% of control
40
-
-
immobilized enzyme forms are stable for 1 min at 40C and then lose their activities
40
-
P08659
complete inactivation, mutant ins356Q still 20% residual activity
42
-
-
50% decrease in activity after 6.9 min for wild-type luciferase, for mutant S118C after 13.4 min
45
-
-
1 h, less than 10% loss of activity mutant enzyme E356R/V368A
45
-
-
mutant enzymes F14R, L35Q, V182K, I232K and F465R are stable up to 45C
additional information
-
-
higher stability in frozen state than in refrigerated
additional information
-
-
a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases is more stable than the wild type enzyme, retaining 75% of the activity after 10 min at 50C
additional information
-
-
10 min at 50C decreases activity by 90%
additional information
-
-
no activity at 40C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
activity loss at 42C is reverted at 4C
-
stability increases 1000fold with immobilization on CNBr-Sepharose 4B, pH 7.5 at 25C
-
stabilized by immobilization on polysaccharide carriers
-
bovine serum albumin stabilizes
-
decrease of remaining activity after trypsin hydrolysis at 23 and 37C, mutants R213M and R337Q are more stable than the wild-type luciferase
-
dithiothreitol stabilizes
-
EDTA stabilizes
-
EDTA, 2-mercaptoethanol, dithiothreitol and bovine serum albumin used as stabilizers
-
enzyme is stable for several days adsorbed on polystyrene
-
immobilization on hexyl-Sepharose reduces the specific activity to 35%, immobilization on octyl-Sepharose reduces the specific activity to 26%
-
inactivation inhibited by sodium azide
-
more stable in phosphate buffer than in Tricine buffer
-
mutant R337Q still 26% remaining activity after 15 min trypsin hydrolysis at 37C
-
sorbitol, proline and sucrose with strong stabilizing effect on firefly luciferase activity at 35C
-
stability in crude solutions varies
-
stabilized by immobilization on polysaccharide carriers
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 50 mM Tris-HCl (pH 7.0) containing 150 mM NaCl, 1 mM EDTA, and 1 mM dithiothreitol, up to 6 months, 10% loss of activity
-
4C, in 50 mM Tris-HCl, 1 mM EDTA, 150 mM NaCl, 1 mM DTT and 0.8 M ammonium sulfate pH 8.0
-
4C, pH 7.0, 0.1 M phosphate, 1 mM 2-mercaptoethanol, immobilized, 3 weeks
-
4C, pH 7.5, ammonium sulfate, EDTA, as 10 mg protein/ml slurry, several months
-
4C, wild-type and mutant enzymes remain fully active for up to 6 months
-
5C, pH 7.2, ammonium sulfate, EDTA, glycerol, several weeks
-
4C, 20% loss of activity after 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA Sepharose
Q5UFR2
Ni-NTA Sepharose column chromatography
-
Ni-NTA sepharose, 95% purity
-
ammonium sulfate precipitation, gel filtration, hydroxyapatite HPLC
-
ammonium sulfate precipitation, gel filtration, hydroxyapatite HPLC
Q01158
chromatography on DEAE-cellulose
-
gel filtration
-
affinity chromatography
-
alkyl-substituted Sepharose 4B affinity chromatography
-
ammonium sulfate fractionation and gel filtration of the wild-type and several mutants
-
ammonium sulfate fractionation and ion-exchange chromatography of the wild-type and several mutants
-
gel filtration, affinity chromatography
-
glutathione Sepharose 4B affinity chromatography
-
immobilization with Procion blue and other tiazine dyes as a purification method
-
immobilized ion affinity chromatography was used to purify a polyhistidine tagged recombinant enzyme
-
Ni-chelate affinity chromatography
-
Ni-NTA agarose column chromatography
-
Ni-NTA Sepharose column chromatography
-
Ni-NTA Sepharose, yield of 95%
-
Ni-NTA spin column
-
Ni-Sepharose 6 Fast Flow column chromatography
-
Ni2+-nitrilotriacetate agarose column chromatography
-
Ni2+-Sepharose column chromatography
-
purification of a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases by ammonium sulfate precipitation, gel filtration and hydroxyapatite column chromatography
-
recombinant mutants purified using ammonium sulfate precipitation and Sephacryl S-200 column chromatography
-
several chromatographic and non chromatographic methods
-
agarose-Ni2+ column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli XL1-Blue cells
-
expressed in HepG2 cells
Q9BLZ2
expressed in Escherichia coli strains XL1-Blue and BL21
-
expression in Escherichia coli BL21
-
a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases expressed in Escherichia coli
-
expression of the wild type and three mutants in Escherichia coli
-
expressed in Escherichia coli strain LE 392
-
expression in Escherichia coli BL21 and XL1blue
-
complete nucleotide sequence, expression in mammalian cells
-
expressed in Candida albicans strain CAI4
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli JM109 cells and Bacillus subtilis strain NBRC13719; into pET28a vector
-
expressed in Escherichia coli strain BL21
-
expressed in Escherichia coli strain HMS174(DE3)
-
expressed in Escherichia coli strain JM109
-
expressed in Escherichia coli strains XL1-Blue and BL21
-
expressed in Escherichia coli Top10 cells
-
expressed in Escherichia coli XL10-Gold cells
-
expression in Drosophila; expression in mouse cells
-
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21 and DH5alpha, transfection in CHO-cells
-
expression in Escherichia coli, transfection in human glioma cells and in quadriceps muscles of mice
-
expression in Escherichia coli; firefly lantern cDNA library
-
expression in Escherichia coli; gene expression in vegetative and symbiotic Rhizobium melioti and other gram-negative bacteria
-
expression in HEK-293 cells or Grip-Tite 293 MSR cells
-
expression in HEK-293T cells
-
expression in L16 derived from CV-1 monkey kidney cells
-
expression in PC3 cells
-
expression in Spodoptera frugiperda clone 9-cells, expression in insect cells using a baculovirus vector
-
expression of a polyhystidine tagged enzyme in Trichoplusia
-
expression of a recombinant enzyme containing a protein kinase A recognition site
-
expression of a recombinant luciferase-ubiquitin enzyme in Saccharomyces cerevisiae
-
mutant enzymes,R218A, H245A, G246A, F247A, F247L, F247Y, F250G, F250S, T251A, G315A, G316A, G341A, L342A, T343A, S347A, A348V, I351A and K529A
-
Nn-terminal domain, expression in Escherichia coli
-
wild-type and mutant enzymes are expressed as GST-fusion proteins
-
wild-type and mutant enzymes expressed as glutathione-S-transferase-fusion proteins containing the additional N-terminal peptide Gly-Pro-Leu-Gly-SER, which remains after PreScission protease cleavage from GST, expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli
-
wild-type and mutant enzymes are expressed as GST-fusion proteins
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F227Y
-
the mutation causes dramatic redshift and temporal shift
F260L
-
the mutation results in a much less pH-sensitive enzyme displaying only a 10 nm redshift and broadening of the spectra at pH 6
I226A
-
the mutation causes dramatic redshift and temporal shift
E356R/V368A
-
mutant enzyme with significantly improved thermostability, more than 90% of the activity remains after incubation for 1 h at 45C. Unlike the wild-type enzyme the mutant enzyme shows no change in the emission maximum of 568 nm even at pH 6.3
E353Q/ins356R
-
emission of red and green light at pH 7.8, 20% less activity
E354K
-
emission of red and green light at pH 7.8, 26% higher activity
E354K/ins356R
-
emission of red and green light at pH 7.8, 20% higher activity
E354R
-
emission of red and green light at pH 7.8, 33% higher activity
E354R/ins356R
-
emission of red light at pH 7.8 compared to green emitted light by wild-type luciferase, 53% higher activity compared to wild-type luciferase
H245N
Q5UFR2
red- and green-emitting luciferase, increase in thermostability, about 25% decrease in relative activity
H431Y
Q5UFR2
red- and green-emitting luciferase, about 85% decrease in relative acitivity
S284T
Q5UFR2
red-emitting luciferase, about 75% decrease in relative activity
S286N
-
red bioluminescence
F16L
-
lower pH-dependence of bioluminescence spectra, about 40% decrease in specific activity
F16L/A40S
-
bioluminescence spectra independent from pH in range of pH 6.0-7.8, about 80% decrease in specific activity
H433Y
-
higher affinity to monomethyloxyluciferin and dimethyloxyluciferin compared to the wild type enzyme
S118C
-
increased thermostability, about 30% increase in specific activity
Y35H
-
bioluminescence spectra independent from pH in range of pH 6.0-7.8, about 40% decrease in specific activity
Y35N
-
bioluminescence spectra independent from pH in range of pH 6.0-7.8, about 30% decrease in specific activity
F227Y
Macrolampis sp2
-
the mutation results in a unique time-dependent shift from red to yellow-green
G228A
Macrolampis sp2
-
the mutation results in a large redshift
Y227A
Macrolampis sp2
-
the substitution results in a weak and unstable red mutant
A348V
-
Km-value for D-luciferin is 8.9fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 6.5fold higher compared to the Km-value of the wild-type enzyme
AC571TG
-
nonsense mutation
D436A
-
3.4fold increased activity compared to the wild type enzyme
D436E
-
50% activity compared to the wild type enzyme
D436G
-
8.5fold increased activity compared to the wild type enzyme
D436G
-
exhibits 8.5fold higher luciferase activity than the wild type enzyme; shows 8.5fold increase in luminescence intensity
D436N
-
50% activity compared to the wild type enzyme
D436S
-
2.2fold increased activity compared to the wild type enzyme
D436V
-
2% activity compared to the wild type enzyme
DELTA438-550
-
the purified N-terminal domain 1-437 has luminescence activity by itself, and binds to substrates ATP and luciferin with reduced affinity
E345K/A215L
-
half-life at 37C is 7.36 min, compared to 3.06 min for the wild-type enzyme
E345K/A215L/I232A/T214A
-
half-life at 37C is 75.1 min, compared to 3.06 min for the wild-type enzyme
E345K/A215L/I232A/T214A/F295L
-
half-life at 37C is 82.1 min, compared to 3.06 min for the wild-type enzyme
E345K/I232A/T214A
-
half-life at 37C is 15.5 min, compared to 3.06 min for the wild-type enzyme
E345K/I232A/T214A/F295L/S420T
-
half-life at 37C is 72.4 min, compared to 3.06 min for the wild-type enzyme
E345K/T214A
-
half-life at 37C is 8.5 min, compared to 3.06 min for the wild-type enzyme
F14R
-
improved pH tolerance and stability up to 45C, no decrease in specific activity relative to the recombinant wild type enzyme
F14R/L35Q/V182K/I232K/F465R
-
improved pH tolerance and stability up to 45C, no decrease in specific activity relative to the recombinant wild type enzyme
F247A
-
Km-value for D-luciferin is 15.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 17.9fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 21.9fold higher compared to the Km-value of the wild-type enzyme
F247L
-
Km-value for D-luciferin is 8.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is nearly identical to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.4fold higher compared to the Km-value of the wild-type enzyme
F247Y
-
Km-value for D-luciferin is 1.2fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 128fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 2fold lower compared to the Km-value of the wild-type enzyme
F250G
-
Km-value for D-luciferin is neraly identical to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 9.6fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is nearly identical to the Km-value of the wild-type enzyme
F250G
-
23% specific activity at pH 7.8 compared to the wild type enzyme
F250S
-
Km-value for D-luciferin is 1.5fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 3.5fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.2fold lower compared to the Km-value of the wild-type enzyme
F250S
-
bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 546 nm compared to 552 nm for the wild-type enzyme, bioluminescence emission maxima with 5,5-dimethyl-luciferyl-O-adenosine monophosphate are 631 nm and 552 nm compared to 560 nm for the wild-type enzyme
F250S
-
49% specific activity at pH 7.8 compared to the wild type enzyme
F250T
-
37% specific activity at pH 7.8 compared to the wild type enzyme
F465R
-
improved pH tolerance and stability up to 45C, no decrease in specific activity relative to the recombinant wild type enzyme
G246A
-
Km-value for D-luciferin is 3.6fold lower compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2.1fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 5.5fold lower compared to the Km-value of the wild-type enzyme
G246A
-
bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 548 nm compared to 552 nm for the wild-type enzyme, bioluminescence emission maximum with 5,5-dimethyl-luciferyl-O-adenosine monophosphate is 578 nm compared to 560 nm for the wild-type enzyme
G246A
-
104% specific activity at pH 7.8 compared to the wild type enzyme
G246A/F250G
-
33% specific activity at pH 7.8 compared to the wild type enzyme
G246A/F250S
-
42% specific activity at pH 7.8 compared to the wild type enzyme
G246A/F250T
-
40% specific activity at pH 7.8 compared to the wild type enzyme
G315A
-
Km-value for D-luciferin is 13.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 625fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 7.5fold higher compared to the Km-value of the wild-type enzyme
G316A
-
Km-value for D-luciferin is 1.2fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2.6fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.5fold lower compared to the Km-value of the wild-type enzyme
G341A
-
Km-value for D-luciferin is 4fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 625fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.3fold higher compared to the Km-value of the wild-type enzyme
G446I
-
turnover number is 8.4fold lower compared to wild-type value, KM-value for D-luciferin is 1.5fold lower compared to wild-type value, KM-value for MgATP2- is 2.2fold lower compared to wild-type value, the bioluminescence emission maximum is 554 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 5.1fold lower compared to wild-type value
H245A
-
Km-value for D-luciferin is identical to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 3fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.5fold higher compared to the Km-value of the wild-type enzyme
H245D
-
longest rise time known among single point mutants
I147A
-
30% activity compared to the wild type enzyme
I147E
-
4% activity compared to the wild type enzyme
I147F
-
1.2fold increased activity compared to the wild type enzyme
I147G
-
3% activity compared to the wild type enzyme
I147K
-
4% activity compared to the wild type enzyme
I147L
-
4.7fold increased activity compared to the wild type enzyme
I147M
-
3.4fold increased activity compared to the wild type enzyme
I147Q
-
70% activity compared to the wild type enzyme
I147R
-
1% activity compared to the wild type enzyme
I147S
-
7% activity compared to the wild type enzyme
I147V
-
1.3fold increased activity compared to the wild type enzyme
I232K
-
improved pH tolerance and stability up to 45C, no decrease in specific activity relative to the recombinant wild type enzyme
I351A
-
Km-value for D-luciferin is 5.7fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 1.5fold higher compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.8fold higher compared to the Km-value of the wild-type enzyme
I423L
-
exhibits 4.7fold higher luciferase activity than the wild type enzyme; shows 4.7fold increase in luminescence intensity
I423L/D436G/L530R
-
combining the mutations results in a combined mutant luciferase with higher luminescence intensity than any of the single mutant luciferases, generates more than 12.5fold higher luminescence intensity than the wild-type enzyme. The combined mutant luciferase detects ATP at 10-18 mol, whereas wild-type luciferase is unable to detect below 10-17 mol ATP; exhibits 12.5fold higher luciferase activity than the wild type enzyme
ins356E
P08659
green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 97% increase in specific activity
ins356K
P08659
green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 18% decrease in specific activity
ins356Q
P08659
at pH 5.5 red-emitting luciferase, increase in thermostability, 6% decrease in specific activity
ins356R
P08659
green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 12% decrease in specific activtiy
K443A
-
turnover number is 2655 fold lower compared to wild-type value, KM-value for D-luciferin is 6.5fold lower compared to wild-type value, KM-value for MgATP2- is 3.3fold lower compared to wild-type value, the bioluminescence emission maximum is identical to the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 181fold lower compared to wild-type value
K443A/K529A
-
turnover number is 1063700fold lower compared to wild-type value, KM-value for D-luciferin is 4.5fold higher compared to wild-type value, KM-value for MgATP2- is 3.5fold higher compared to wild-type value, the bioluminescence emission maximum is 596 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 858fold lower compared to wild-type value
K445Q
-
turnover number is 1.4fold higher compared to wild-type value, KM-value for D-luciferin is 1.7fold lower compared to wild-type value, KM-value for MgATP2- is 2.3fold lower compared to wild-type value, the bioluminescence emission maximum is 556 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 1.7fold higher compared to wild-type value
K529A
-
Km-value for D-luciferin is 15.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 1250fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 7.5fold higher compared to the Km-value of the wild-type enzyme
K529A
-
turnover number is 668fold lower compared to wild-type value, KM-value for D-luciferin is 15.3fold higher compared to wild-type value, KM-value for MgATP2- is 7.5fold higher compared to wild-type value, the bioluminescence emission maximum is 562 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 3.5fold lower compared to wild-type value
K529A
-
similar rise time compared to wild type enzyme
L287I
-
orange light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
L342A
-
Km-value for D-luciferin is 8.7fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 1.2fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 7.5fold higher compared to the Km-value of the wild-type enzyme
L35Q
-
improved pH tolerance and stability up to 45C, no decrease in specific activity relative to the recombinant wild type enzyme
L530A
-
20% activity compared to the wild type enzyme
L530D
-
1% activity compared to the wild type enzyme
L530F
-
10% activity compared to the wild type enzyme
L530H
-
1.4fold increased activity compared to the wild type enzyme
L530I
-
shows wild type enzyme activity
L530K
-
3.2fold increased activity compared to the wild type enzyme
L530R
-
5.1fold increased activity compared to the wild type enzyme
L530R
-
exhibits 5.1fold higher luciferase activity than the wild type enzyme; shows 5.1fold increase in luminescence intensity
L530S
-
1% activity compared to the wild type enzyme
L530V
-
50% activity compared to the wild type enzyme
Q283R
-
red light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
Q338P
-
about 50% decrease in specific activity compared to wild-type luciferase
Q448A
-
turnover number is 1.9fold lower compared to wild-type value, KM-value for D-luciferin is 2.5fold lower compared to wild-type value, KM-value for MgATP2- is 2.1fold higher compared to wild-type value, the bioluminescence emission maximum is 557 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 1.1fold lower compared to wild-type value
R213E
-
same activity like wild-type luciferase
R213M
-
3fold activity compared to wild-type luciferase
R218A
-
Km-value for D-luciferin is 20fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 31.3fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 38.8fold higher compared to the Km-value of the wild-type enzyme
R337Q
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only 60% relative specific activity compared to wild-type luciferase, higher light stability, most stable luciferase mutant against trypsin hydrolysis at 23 and 37C
S184T
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red-emitting luciferase with a bioluminescence maximum of 615 nm
S284G
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red light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
S284T
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red-emitting mutant, about 75% decrease of activitiy in vitro, in vivo more efficient light production
S293P
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orange light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
S347A
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Km-value for D-luciferin is 11.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 4.2fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 2.2fold higher compared to the Km-value of the wild-type enzyme
T251A
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Km-value for D-luciferin is 20.7fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2.9fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 12.5fold higher compared to the Km-value of the wild-type enzyme
T343A
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Km-value for D-luciferin is 6.6fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 125fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 5.4fold higher compared to the Km-value of the wild-type enzyme
V182K
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improved pH tolerance and stability up to 45C, no decrease in specific activity relative to the recombinant wild type enzyme
V241I
-
136% specific activity at pH 7.8 compared to the wild type enzyme
V241I/F250G
-
13% specific activity at pH 7.8 compared to the wild type enzyme
V241I/F250S
-
32% specific activity at pH 7.8 compared to the wild type enzyme
V241I/F250T
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64% specific activity at pH 7.8 compared to the wild type enzyme
V241I/G246A/F250S
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73% specific activity at pH 7.8 compared to the wild type enzyme
V241I/G246A/F250T
-
83% specific activity at pH 7.8 compared to the wild type enzyme
Y227A
-
mutant shows enzymatic behaviour similar to the wild type enzyme
G228A
-
the mutation results in a large redshift
Y227A
-
the mutation causes dramatic red- and time-dependent shifts
L260F
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mutation results in a 20 nm redshift without affecting pH-insensitivity
V227A
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mutant displays a small redshift
V227F
-
mutation results in a 60 nm redshift
V227I
-
mutant displays a small redshift
V227S
-
mutant displays a small redshift
A243G
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bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 599 nm compared to 549 nm for the wild-type enzyme, bioluminescence emission maxima with 5,5-dimethyl-luciferyl-O-adenosine monophosphate are 610 nm and 557 nm compared to 624 nm for the wild-type enzyme
S247F
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bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 597 nm compared to 549 nm for the wild-type enzyme, bioluminescence emission maximum with 5,5-dimethyl-luciferyl-O-adenosine monophosphate is 612 nm compared to 624 nm for the wild-type enzyme
L530Y
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2% activity compared to the wild type enzyme
additional information
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mutants with changes in V241I, G246A, and F250S show emission maximum blue-shifted to 549 nm
additional information
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a chimeric protein with the N-terminal domain of firefly luciferase and the C-terminal domain of the firefly luciferase homolog from Drosophila melanogaster CG6178 shows approximately 4% of the activity of wild type firefly luciferase
additional information
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10fold higher luminescence intensity of mutant enzyme luciferase FM compared to wild-type luciferase
additional information
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chimeric protein with fatty acyl-CoA synthetase, EC 6.2.1.3, 4% of luminescence activity from wild-tpe luciferase activity
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
renaturation is initiated by diluting the denaturant in 50 mM HEPES-KOH, pH 7.5, 10 mM Mg(OAc)2, 70 mM KOAc, 50 mM imidazole, and 1 mM dithiothreitol without urea, refolding of firefly luciferase from a denatured state is a slow process, its rate and productivity depend on molecular chaperones of the Hsp70 family, Hsp70-dependent refolding restores 55% of the initial enzymatic activity, immobilization leads to a higher refolding yield owing to the prevention of intermolecular aggregation
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
Q5UFR2
imaging technology
analysis
-
luminescence-based assays for ATP measurement in clinical chemistry and hygiene monitoring
analysis
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optical bioluminescence-based molecular imaging
analysis
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analytical assay of metabolites like ATP, CoA, pyrophosphate, AMP
biotechnology
-
molecular biology studies with luciferase as reproter gene, bioimaging
medicine
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luciferase gene is a useful reporter gene in vivo, allowing noninvasive imaging of tumor growth, metastasis, gene transfer, drug treatment, and gene expression. The use of thermostabilized luciferases may allow monitoring of micro-metastses and the early stages of tumor growth
medicine
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use in endotoxin detection method
medicine
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observing tumours
additional information
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the combined mutant luciferase, which has high luminescence intensity, will be useful for detecting bacteria with high sensitivity in production safety tests