Information on EC 1.13.12.7 - firefly luciferase and Organism(s) Photinus pyralis and UniProt Accession P08659

-

-

?

5-methylluciferin + ATP + O2

?

-

-

?

6'-amino-D-luciferin + ATP + O2

?

-

-

?

D-5,5-dimethylluciferyl-adenylate + O2

?

yellow-green color of luminescence

-

?

D-firefly luciferin + O2 + ATP

firefly oxyluciferin + CO2 + AMP + diphosphate + hv

10 entries

D-luciferin + ATP

diphosphate + luciferyl-adenylate

-

698393

-

r

D-luciferin + ATP + O2

luciferyl-adenylate + diphosphate

-

-

?

D-luciferin + ATP + O2

luciferyl-adenylate + diphosphate + H2O + hv

-

-

r

D-luciferin + O2 + ATP

oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv

-

-

?

D-luciferin + O2 + ATP

oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv

-

-

?

D-luciferyl-adenylate + O2

oxyluciferin + CO2 + AMP + hv

-

698393

-

ir

D-luciferyl-O-adenosine monophosphate + ?

?

-

-

?

D-naphthylluciferin + ATP + O2

?

-

-

?

D-quinolylluciferin + ATP + O2

?

-

-

?

decanoic acid + ATP + CoA

decanoyl-CoA + AMP + diphosphate

-

-

?

dehydroluciferin + ATP

dehydroluciferyl-AMP + diphosphate

-

-

r

fatty acid + ATP + CoA

fatty acyl-CoA + AMP

-

-

?

lauric acid + ATP + CoA

lauroyl-CoA + AMP + diphosphate

-

658314, 697221

-

?

linoleic acid + ATP + CoA

linoleoyl-CoA + AMP + diphosphate

linoleic acid concentration above 10 microM has an inhibitory effect

-

?

luciferin + MgATP2-

AMP + diphosphate

-

-

?

luciferyl-adenylate

oxyluciferin + hnu

-

-

?

luciferyl-adenylate + O2

oxyluciferin + AMP + CO2 + hv

-

-

ir

luciferyl-O-adenosine monophosphate + CoA

luciferyl-CoA + AMP

-

-

?

myristic acid + ATP + CoA

myristoyl-CoA + AMP + diphosphate

-

-

?

Photinus luciferin + O2 + ATP

oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv

-

-

?

R-COOH + ATP

R-CO-AMP + diphosphate

-

-

r

(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2

?

-

decay time to 10%: 500 sec, relative specific activity: 13%

-

?

(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2

?

-

decay time to 10%: 150 sec, relative specific activity: 1.7%

-

?

(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2

?

-

decay time to 10%: 5700 sec, relative specific activity: 421%

-

?

(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2

?

-

decay time to 10%: 400 sec, relative specific activity: 0.4%

-

?

(4S)-2-(6-hydroxy-1H-indol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2

?

-

-

?

5,5'-dimethylluciferin + ATP + O2

dehydroluciferin-adenylate + diphosphate

-

produces only red light, 6-amino and 4 hydroxy analogs tested

-

?

5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?

5,5-dimethyloxyluciferin + hv

-

-

?

6'-amino-D-luciferin + ATP

? + hv

-

-

?

8-anilino-1-naphthalene-sulfonate + ?

?

-

-

?

adenosine 5'-tetraphosphate + Photinus luciferin

oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv

-

0.75% light response relative to ATP

-

?

ADP

ATP + AMP

-

484869

reaction inhibited by P1,P5-di(adenosine-5'-)pentaphosphate, but independent of luciferin

484869

?

arachidonic acid + ATP + CoA

arachidonoyl-CoA + AMP + diphosphate

-

-

?

ATP + O2 + oxyluciferin

?

-

assay at pH 7.5, 24-27°C

-

?

D-aminoluciferin + ATP + O2

?

-

assay at 37°C. 5 min

-

?

D-luciferin + ATP + O2

?

D-luciferin + ATP + O2

luciferyl-adenylate + diphosphate + H2O + hv

-

-

?

D-luciferin + ATP + O2

oxidized D-luciferin + AMP + CO2 + diphosphate

D-luciferin + ATP + O2

oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv

-

726696, 728433

-

?

D-luciferin + ATP + O2

oxidized luciferin + AMP + CO2 + diphosphate

-

-

?

D-luciferin + ATP + O2

oxidized luciferin + AMP + CO2 + diphosphate + hv

-

-

?

D-luciferin + ATP + O2

oxyluciferin + CO2 + AMP + hv + diphosphate

-

697750

-

?

D-luciferin + dATP + O2

?

-

-

?

D-luciferin + O2

?

-

10 microM, assay at pH 7.5

-

?

D-luciferin + O2 + ATP

oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv

8 entries

D-luciferin + O2 + ATP

oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv

-

-

?

D-luciferin + O2 + ATP

oxyluciferin + AMP + diphosphate + CO2 + light

-

685746

-

?

D-luciferin + O2 + ATP

oxyluciferin + CO2 + H2O + AMP + diphosphate + hv

-

-

r

D-luciferyl-AMP + O2

dehydroluciferyl-AMP + H2O2

-

673086

-

ir

dehydroluciferin + ATP + O2

diphosphate + dehydroluciferin-adenylate

-

-

?

dehydroluciferin + CoA

dehydroluciferyl-CoA

-

-

?

dehydroluciferyladenylate + CoA

dehydroluciferyl-CoA + ?

-

-

?

deoxyATP + Photinus luciferin

oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv

-

-

?

L-luciferin + CoA + ATP

luciferyl-CoA + AMP + diphosphate

-

L-luciferin is converted to luciferyl adenylate, and the adenyl group of luciferyl adenylate is then substituted to CoA-SH to give luciferyl-CoA. Even in presence of CoA-SH, D-luciferin is used for the light production reaction, but is not converted into luciferyl-CoA

-

?

linoleic acid + ATP + CoA

linoleoyl-CoA + AMP + diphosphate

-

-

?

linolenic acid + ATP + CoA

linolenoyl-CoA + AMP + diphosphate

-

-

?

luciferin + ATP + O2

?

-

assay at 25°C, pH 7.8

-

?

luciferin + ATP + O2

oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv

luciferin + MgATP2-

AMP + diphosphate

luciferin + O2 + ATP

?

-

assay at pH 7.8

-

?

luciferin + O2 + ATP

oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv

luciferin + O2 + ATP

oxyluciferin + AMP + diphosphate + CO2 + light

-

-

ir

luciferyl adenylate + O2

dehydroluciferyl adenylate + ?

-

-

?

luciferyl-O-adenosine monophosphate + ?

?

-

-

?

oleic acid + ATP + CoA

oleoyl-CoA + AMP + diphosphate

-

-

?

P1,P5-di(adenosine-5'-)pentaphosphate + Photinus luciferin

oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv

-

2.2% light response relative to ATP

-

?

palmitic acid + ATP + CoA

palmitoyl-CoA + AMP + diphosphate

-

-

?

Photinus luciferin + O2 + ATP

oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv

45 entries

Photinus luciferin + O2 + GTP

adenosine 5'-P1-tetraphospho-P4-5'''-guanosine

-

484834

-

484834

?

polyethylene glycol-6-amino-D-luciferin

? + hv

-

longer light emission

-

?

additional information

?

-

D-firefly luciferin + O2 + ATP

firefly oxyluciferin + CO2 + AMP + diphosphate + hv

9 entries

luciferin + O2 + ATP

oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv

-

the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism

-

?

luciferin + O2 + ATP

oxyluciferin + AMP + diphosphate + CO2 + light

-

-

ir

Photinus luciferin + O2 + ATP

oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv

-

highly specific for ATP

-

?

ATP

CoA

-

ATP

-

necessary

Mg2+

Co2+

-

influences the interaction with triazine dyes

484834, 484855

Cu2+

Fe2+

-

influences the interaction with triazine dyes

484855

Mg2+

11 entries

Mn2+

-

influences the interaction with triazine dyes

484834, 484853, 484855

Ni2+

-

influences the interaction with triazine dyes

484855

Zn2+

additional information

(2E)-1-(1-benzofuran-2-yl)-3-(4-methylphenyl)prop-2-en-1-one

-

-

(2E)-1-(1-benzofuran-2-yl)-3-phenylprop-2-en-1-one

-

-

(2E)-1-(2-hydroxyphenyl)-3-(4-methylphenyl)prop-2-en-1-one

-

-

(2E)-1-(5-chlorothiophen-2-yl)-3-(4-methylphenyl)prop-2-en-1-one

-

-

(2E)-1-(5-chlorothiophen-2-yl)-3-phenylprop-2-en-1-one

-

-

(2E)-2-benzylidene-3,4-dihydronaphthalen-1(2H)-one

-

(2E)-2-[(2-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(2-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(2-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(2-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(2-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(3-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(3-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(3-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(3-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(3-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-ethoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-ethylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-fluorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-hydroxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(4-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[(pyridin-3-yl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(benzyloxy)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(diethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-6-methoxy-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-7-methoxy-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-8-methoxy-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(methylsulfanyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-2-[[4-(trifluoromethyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-5-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-6-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-7-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(2E)-8-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

-

(6E)-6-[(3-carboxy-4-hydroxyphenyl)methylidene]-5-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid

-

-

(7E)-7-[(4-methylphenyl)methylidene]-8-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid

-

-

2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide

non-competitive inhibitor

2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole

luciferin competitor

2-benzylidene-1H-indene-1,3(2H)-dione

-

-

2-hydroxy-5-[(E)-(1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]benzoic acid

-

-

2-phenylbenzothiazole

-

2-[(4-methylphenyl)methylidene]-1H-indene-1,3(2H)-dione

-

-

2-[(4-methylphenyl)methyl]-3,4-dihydronaphthalen-1(2H)-one

-

-

2-[[4-(dimethylamino)phenyl]methyl]-3,4-dihydronaphthalen-1(2H)-one

-

-

3-(4-methylphenyl)-4,5-dihydro-2H-benzo[g]indazole

-

-

3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid

-

4-(4-methylphenyl)-5,6-dihydrobenzo[h]quinazolin-2-amine

-

-

5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine

competitive inhibitor

5'-O-[[2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazole-4-carbonyl]sulfamoyl]adenosine

non-competitive inhibitor

-

5-(ethanesulfonyl)-2-(naphthalen-2-yl)-1,3-benzoxazole

non-competitive inhibitor

-

5-[(2E)-4-(4-bromophenyl)-4-oxobut-2-en-1-yl]-2-hydroxybenzoic acid

luciferin competitor

-

5-[(E)-(6-bromo-1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]-2-hydroxybenzoic acid

-

-

AMP

-

arachidonic acid

concentration above 10 microM

ATP

-

bromoform

-

dehydroluciferin

dehydroluciferyl adenylate

-

diphosphate

Halothane

non-competitive inhibitor

L-AMP

a potent luciferase inhibitor

L-luciferin

-

linoleic acid

concentration above 10 microM

lipoic acid

-

myristic acid

-

N-pyridin-2-ylbenzamide

-

NFkappaBAI4

non-competitive inhibitor

-

oleic acid

concentration above 10 microM

oxyluciferin

pifithrin-alpha

20 microM, above 95% inhibition

resveratrol

SMT C1100

non-competitive inhibitor, utrophin modulator, phase II clinical compound SMT C1100 for the treatment of Duchenne muscular dystrophy

-

[2-(4-ethoxyphenyl)quinolin-4-yl][4-(pyridin-2-yl)piperazin-1-yl]methanone

ATP competitor

-

[4-(6-methoxynaphthalen-2-yl)phenyl]acetic acid

luciferin competitor

-

(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-[3-(6-ethoxy-1,3-benzothiazol-2-yl)thiophen-2-yl]urea

-

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-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-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

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-[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

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-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

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-((7-[4-(trifluoromethyl)benzyl]-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy)aniline

-

7% inhibition

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-(4-aminophenoxy)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine

-

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-(7H-pyrrolo[2,3-d]pyrimidin-4-yloxy)aniline

-

19% inhibition

4-([2-(methylsulfanyl)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

31% inhibition

4-([2-(methylsulfonyl)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

9% inhibition

4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N,N-dimethylaniline

-

4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N-methylaniline

-

4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

4-([7-(2-methylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

4-([7-(3-methylbut-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

4-([7-(3-methylbutyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

4-([7-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

26% inhibition

4-([7-(prop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

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-methoxy-N-[(4-methylpyridin-2-yl)carbamoyl]benzamide

-

4-methyl-N-(phenylmethyl)benzenesulfonamide

-

4-[(7-benzyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

-

46% inhibition

4-[(7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

-

4-[(7-ethenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

-

4-[(7-ethyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

-

4-[(7-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

-

48% inhibition

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

672578

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-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

arsenate

ATP

bovine serum albumin

-

inhibition when present in large excess

484836

-

butanoic acid

-

IC50: 13.6 mM

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

dAMP

-

dATP

-

Decanoic acid

-

IC50: 0.0132 mM

dehydroluciferin

dehydroluciferyl adenylate

-

IC50: 6 nM

dehydroluciferyl-adenylate

-

tight-binding competitive inhibitor

dehydroluciferyl-CoA

-

IC50: 0.005 mM

diphosphate

-

dithiothreitol

-

dodecanoic acid

Dodecanol

-

mixed-type inhibitor

658219

dodecylamine

-

noncompetitive inhibitor

EDTA

-

ethanol

-

ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate

-

ethyl [4-(4-aminophenoxy)-7H-pyrrolo[2,3-d]pyrimidin-7-yl]acetate

-

33% inhibition

ethyl-2-benzothiazole sulfonate

-

competitive inhibitor

geneticin

-

induces nonsense suppression

gentamicin

-

induces nonsense suppression

hexadecanoic acid

-

IC50: 0.00067 mM

hexanoic acid

-

IC50: 3.4 mM

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%

-

Luciferin

MgATP2-

-

N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide

common name DCB

N,N-dimethyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

N,N-dimethyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

N-(4-ethoxyphenyl)-2-methoxybenzamide

-

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-ethylmaleimide

-

484831, 484849, 484854

N-methyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

N-methyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

-

N-tosyl-L-lysine chloromethyl ketone

-

N-tosyl-L-phenylalanine chloromethyl ketone

N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide

-

N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide

-

N-[5-[(2,2-dimethylpropanoyl)amino]pyridin-2-yl]-3-hydroxybenzamide

-

N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide

-

octadecanoic acid

-

IC50: 0.00063 mM

octanoic acid

-

IC50: 2.9 mM

oxyluciferin

-

competitive inhibitor

p-mercuribenzoate

-

phosphate

-

Procion blue MX-R

resveratrol

-

resveratrol is 3,5,4'-trihydroxystilbene, potent inhibitor

ribose-5-phosphate

-

tetradecanoic acid

-

IC50: 0.00068 mM

additional information

-

ATP

essential for luminescence reaction, initiates luminescence reaction

CoA

prevents rapid decay of light emission

diphosphate

stimulates light production under some conditions

molecular oxygen

essential for luminescence reaction

Triphosphate

stimulates light production under some conditions

alpha-synuclein

-

dose-dependent enhancement of oxyluciferin formation, maximum rate of bioluminescence independent upon ATP concentration

696465

-

AMP

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

Luciferin

-

preparations supplemented with extra luciferin provide maximum light emission

MS-275

-

Polyethyleneglycol

-

stimulates activity by promoting the dissociation of inhibitory product from the enzyme

Polyvinylpyrrolidone

-

stimulates activity by promoting the dissociation of inhibitory product from the enzyme

Triton X-100

-

stimulates activity by promoting the dissociation of inhibitory product from the enzyme

[1,1,3,3-tetramethylguanidine][acetate]

-

enzyme shows increased activity and increased thermal stability

[1,1,3,3-tetramethylguanidine][lactate]

-

increase in concentration of [1,1,3,3-tetramethylguanidine][Lac] up to 0.25 M increases enzyme activity, and at concentrations more than 0.25 M enzyme activity is decreased. Optimum temperature and thermal stability studies show more stability of luciferase only in the presence of [1,1,3,3-tetramethylguanidine][Lac]

[1,1,3,3-tetramethylguanidine][propionate]

-

in the presence of [1,1,3,3-tetramethylguanidine][propionate], enzyme activities are decreased with an increase in ionic liquid concentration

[1,1,3,3-tetramethylguanidine][trichloroacetate]

-

enzyme shows decreased activity

[1,1,3,3-tetramethylguanidine][trifluoroacetate]

-

enzyme shows unchanged activity

additional information

-

0.04 - 0.16

ATP

18 entries

0.00076 - 0.1421

D-firefly luciferin

16 entries

0.0023 - 0.23

D-luciferin

15 entries

0.00038 - 0.0126

D-luciferyl-O-adenosine monophosphate

0.00741

lauric acid

-

658314, 697221

0.0136

linoleic acid

-

0.0486 - 1.2

MgATP2-

0.176

(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.07

(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.061

(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 9.1, temperature not specified in the publication

0.02

(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.00025 - 0.0003

5,5-dimethyl-luciferyl-O-adenosine monophosphate

0.001 - 6.9

ATP

70 entries

0.001 - 2.5

D-luciferin

67 entries

0.0149

dehydroluciferyl-adenylate

-

0.0982

L-luciferin

-

0.0136

linolenic acid

-

0.0072 - 0.218

Luciferin

22 entries

0.0077 - 0.0127

luciferyl-O-adenosine monophosphate

0.025 - 6.2

MgATP2-

21 entries

0.0147

oxyluciferin

-

additional information

-

0.000000157 - 0.24

D-luciferin

0.0000311 - 0.32

D-luciferyl-O-adenosine monophosphate

0.278

lauric acid

-

0.000000157 - 0.24

MgATP2-

0.0018

(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.00063

(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.0067

(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 9.1, temperature not specified in the publication

0.00051

(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.0001 - 0.19

D-luciferin

20 entries

0.13

linolenic acid

-

1.6

Luciferin

-

484860

additional information

-

kinetic of light emission

484845

-

0.01

(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.01

(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

0.11

(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 9.1, temperature not specified in the publication

0.03

(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

-

pH 8.5, temperature not specified in the publication

6.78

D-luciferin

-

pH 8.2, temperature not specified in the publication

0.00034

3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid

pH and temperature not specified in the publication

0.000034 - 0.00034

5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine

0.0005

dehydroluciferin

pH 7.8, 25°C

0.0000038

dehydroluciferyl adenylate

pH and temperature not specified in the publication

0.0000038

L-AMP

pH 7.8, 25°C

0.003 - 0.004

L-luciferin

-

0.000026

lipoic acid

-

0.00053

myristic acid

-

0.0005

oxyluciferin

pH 7.8, 25°C

0.00012

[4-(6-methoxynaphthalen-2-yl)phenyl]acetic acid

pH and temperature not specified in the publication

-

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

-

0.00034

5'-O-[(N-dehydroluciferyl)-sulfamoyl]-adenosine

-

672578

0.23

5-anilino-1-naphthalene sulfonate

-

0.0059

6-toluidino-2-naphthalene sulfonate

-

0.9

dAMP

-

0.7

dATP

-

0.00001 - 0.001

dehydroluciferin

0.0000038

dehydroluciferyl-adenylate

-

0.25

L-tosylamido-2-phenethyl chloromethyl ketone

-

1

MgATP2-

-

0.73

N-tosyl-L-lysine chloromethyl ketone

-

0.25

N-tosyl-L-phenylalanine chloromethyl ketone

-

0.0005

oxyluciferin

-

0.3

phosphate

-

0.002

resveratrol

-

671781

0.34

ribose-5-phosphate

-

additional information

5'-O-[hydroxy({[(2Z)-2-(6-oxo-1,3-benzothiazol-2(6H)-ylidene)-2,3-dihydro-1,3-thiazol-4-yl]carbonyl}oxy)phosphoryl]adenosine

0.0004

(2E)-1-(1-benzofuran-2-yl)-3-(4-methylphenyl)prop-2-en-1-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0018

(2E)-1-(1-benzofuran-2-yl)-3-phenylprop-2-en-1-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00007

(2E)-1-(2-hydroxyphenyl)-3-(4-methylphenyl)prop-2-en-1-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0011

(2E)-1-(5-chlorothiophen-2-yl)-3-(4-methylphenyl)prop-2-en-1-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00041

(2E)-1-(5-chlorothiophen-2-yl)-3-phenylprop-2-en-1-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000088

(2E)-2-benzylidene-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

0.0002

(2E)-2-[(2-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00009

(2E)-2-[(2-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0005

(2E)-2-[(2-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00044

(2E)-2-[(2-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0013

(2E)-2-[(2-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0006

(2E)-2-[(3-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0014

(2E)-2-[(3-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000034

(2E)-2-[(3-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0015

(2E)-2-[(3-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0011

(2E)-2-[(3-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000007

(2E)-2-[(4-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00006

(2E)-2-[(4-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000007

(2E)-2-[(4-ethoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0000012

(2E)-2-[(4-ethylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000031

(2E)-2-[(4-fluorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one, (2E)-2-[(4-hydroxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0000012

(2E)-2-[(4-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0000005

(2E)-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000056

(2E)-2-[(4-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0109

(2E)-2-[(pyridin-3-yl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00013

(2E)-2-[[4-(benzyloxy)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000049

(2E)-2-[[4-(diethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0000005

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0002

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-6-methoxy-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0012

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-7-methoxy-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.007

(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-8-methoxy-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000012

(2E)-2-[[4-(methylsulfanyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00026

(2E)-2-[[4-(trifluoromethyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00014

(2E)-5-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.000159

(2E)-6-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00286 - 122

(2E)-7-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

-

0.000106

(2E)-8-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00000025

(6E)-6-[(3-carboxy-4-hydroxyphenyl)methylidene]-5-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid

Photinus pyralis

pH and temperature not specified in the publication

-

0.002

(7E)-7-[(4-methylphenyl)methylidene]-8-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid

Photinus pyralis

pH and temperature not specified in the publication

-

0.0005

2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

pH and temperature not specified in the publication

0.00016

2-benzylidene-1H-indene-1,3(2H)-dione

Photinus pyralis

pH and temperature not specified in the publication

-

0.00056

2-hydroxy-5-[(E)-(1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]benzoic acid

Photinus pyralis

pH and temperature not specified in the publication

-

0.000063

2-[(4-methylphenyl)methylidene]-1H-indene-1,3(2H)-dione

Photinus pyralis

pH and temperature not specified in the publication

-

0.0024

2-[(4-methylphenyl)methyl]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.0018

2-[[4-(dimethylamino)phenyl]methyl]-3,4-dihydronaphthalen-1(2H)-one

Photinus pyralis

pH and temperature not specified in the publication

-

0.00058

3-(4-methylphenyl)-4,5-dihydro-2H-benzo[g]indazole

Photinus pyralis

pH and temperature not specified in the publication

-

0.0059

4-(4-methylphenyl)-5,6-dihydrobenzo[h]quinazolin-2-amine

Photinus pyralis

pH and temperature not specified in the publication

-

0.000033

5'-O-[[2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazole-4-carbonyl]sulfamoyl]adenosine

Photinus pyralis

pH and temperature not specified in the publication

-

0.0003

5-(ethanesulfonyl)-2-(naphthalen-2-yl)-1,3-benzoxazole

Photinus pyralis

pH and temperature not specified in the publication

-

0.0002

5-[(2E)-4-(4-bromophenyl)-4-oxobut-2-en-1-yl]-2-hydroxybenzoic acid

Photinus pyralis

pH and temperature not specified in the publication

-

0.00044

5-[(E)-(6-bromo-1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]-2-hydroxybenzoic acid

Photinus pyralis

pH and temperature not specified in the publication

-

0.00005

lipoic acid

Photinus pyralis

-

0.00068

myristic acid

Photinus pyralis

-

0.000069

N-pyridin-2-ylbenzamide

Photinus pyralis

-

0.001

NFkappaBAI4

Photinus pyralis

pH and temperature not specified in the publication

-

0.0019 - 0.002

resveratrol

0.0005

[2-(4-ethoxyphenyl)quinolin-4-yl][4-(pyridin-2-yl)piperazin-1-yl]methanone

Photinus pyralis

pH and temperature not specified in the publication

-

0.0002

(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid

Photinus pyralis

-

0.002

(2Z)-1-(4-chlorophenyl)-3-(pyridin-2-ylamino)prop-2-en-1-one

Photinus pyralis

-

0.00008

(2Z)-3-[(2-bromophenyl)amino]-1-pyridin-2-ylprop-2-en-1-one

Photinus pyralis

-

0.001

(2Z)-3-[(4-fluorophenyl)amino]-1-furan-2-ylprop-2-en-1-one

Photinus pyralis

-

0.00021

(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one

Photinus pyralis

-

0.0008

(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one

Photinus pyralis

-

0.0006

1-[3-(6-ethoxy-1,3-benzothiazol-2-yl)thiophen-2-yl]urea

Photinus pyralis

-

0.00008

2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide

Photinus pyralis

-

0.0062

2-(2-amino-3-methoxyphenyl)-4H-chromen-4-one

Photinus pyralis

-

0.0054

2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

-

-

0.0006

2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

-

0.00032

2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone

Photinus pyralis

-

0.0113

2-(2-methoxyphenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0032

2-(3,4-dimethoxyphenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0028

2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

-

0.0242

2-(3-fluorophenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0015

2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

-

0.0045

2-(4-chlorophenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0035

2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

-

0.0013

2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline

Photinus pyralis

-

0.00041

2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline

Photinus pyralis

-

0.0013

2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole

Photinus pyralis

-

0.001

2-(4-methoxyphenyl)-1,3-benzothiazole

Photinus pyralis

-

0.004

2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline

Photinus pyralis

-

0.00008 - 0.0001

2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine

0.0171

2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine

Photinus pyralis

-

0.0001

2-(5-naphthalen-2-yl-1,2,4-oxadiazol-3-yl)pyridine

Photinus pyralis

-

0.0144

2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine

Photinus pyralis

-

0.0073

2-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.0008

2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide

Photinus pyralis

-

0.0047

2-methyl-6-(phenylethynyl)pyridine

Photinus pyralis

-

0.0043

2-methyl-6-[(Z)-2-phenylethenyl]pyridine

Photinus pyralis

-

0.0028

2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine

Photinus pyralis

-

0.00084

2-[5-(3,4-dichlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine

Photinus pyralis

-

0.00022

2-[5-(3-chloro-4-methylphenyl)-1,2,4-oxadiazol-3-yl]pyridine

Photinus pyralis

-

0.0005

2-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine

Photinus pyralis

-

0.0032

2-[5-(5-bromofuran-2-yl)-1,2,4-oxadiazol-3-yl]pyridine

Photinus pyralis

-

0.00005

3-(2-hydroxyphenyl)-1H-benzo[f]chromen-1-one

Photinus pyralis

-

0.0083

3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole

Photinus pyralis

-

0.01471

3-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.0014

3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate

Photinus pyralis

-

0.0002

4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline

Photinus pyralis

-

0.0063

4-(1,3-benzothiazol-2-yl)benzonitrile

Photinus pyralis

-

0.0007

4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline

Photinus pyralis

-

0.01076

4-(4-aminophenoxy)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine

Photinus pyralis

-

pH 7.8, 20°C

0.024

4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine

Photinus pyralis

-

0.0007

4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline

Photinus pyralis

-

0.0057

4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile

Photinus pyralis

-

0.00012

4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N,N-dimethylaniline

Photinus pyralis

-

pH 7.8, 20°C

0.00007

4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N-methylaniline

Photinus pyralis

-

pH 7.8, 20°C

0.00008

4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00012

4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00031

4-([7-(2-methylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00753

4-([7-(3-methylbut-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00646

4-([7-(3-methylbutyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00224

4-([7-(prop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00036

4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

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

Photinus pyralis

-

0.00041

4-methoxy-N-[(4-methylpyridin-2-yl)carbamoyl]benzamide

Photinus pyralis

-

0.00029

4-[(7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00943

4-[(7-ethenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00351

4-[(7-ethyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline

Photinus pyralis

-

pH 7.8, 20°C

0.0003

4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol

Photinus pyralis

-

0.024

4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine

Photinus pyralis

-

0.0005

4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline

Photinus pyralis

-

0.00015 - 0.0002

5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole

0.001

5-(2-bromophenyl)-3-(4-methylphenyl)-1,2,4-oxadiazole

Photinus pyralis

-

0.00015

5-(2-chloro-4-methylphenyl)-3-phenyl-1,2,4-oxadiazole

Photinus pyralis

-

0.0028

5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole

Photinus pyralis

-

0.0017

5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole

Photinus pyralis

-

0.0011

5-methyl-N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide

Photinus pyralis

-

0.00041

5-naphthalen-2-yl-3-phenyl-1,2,4-oxadiazole

Photinus pyralis

-

0.0032

6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0015

6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0022

6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole

Photinus pyralis

-

0.0089

6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole

Photinus pyralis

-

-

0.0134

6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole

Photinus pyralis

-

-

0.0045

6-methyl-2-[(Z)-phenyldiazenyl]pyridin-3-ol

Photinus pyralis

-

13.6

butanoic acid

Photinus pyralis

-

IC50: 13.6 mM

0.135

D-luciferin

Photinus pyralis

-

inhibits CoA-ligase activity with L-luciferin, IC50: 0.135 mM against 0.1 mM L-luciferin

0.0132

Decanoic acid

Photinus pyralis

-

IC50: 0.0132 mM

0.000006

dehydroluciferyl adenylate

Photinus pyralis

-

IC50: 6 nM

0.0000074 - 0.000022

dehydroluciferyl-adenylate

5 entries

0.005

dehydroluciferyl-CoA

Photinus pyralis

-

IC50: 0.005 mM

0.0012

dodecanoic acid

Photinus pyralis

-

IC50: 0.0012 mM

0.0009

ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate

Photinus pyralis

-

0.00067

hexadecanoic acid

Photinus pyralis

-

IC50: 0.00067 mM

3.4

hexanoic acid

Photinus pyralis

-

IC50: 3.4 mM

0.0045

N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide

Photinus pyralis

-

0.00009

N,N-dimethyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00018

N,N-dimethyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.0006

N-(4-ethoxyphenyl)-2-methoxybenzamide

Photinus pyralis

-

0.00065

N-(6-ethoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide

Photinus pyralis

-

0.0012

N-(6-methoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide

Photinus pyralis

-

0.0005

N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide

Photinus pyralis

-

0.00006

N-methyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.00013

N-methyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline

Photinus pyralis

-

pH 7.8, 20°C

0.0029

N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide

Photinus pyralis

-

0.003

N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide

Photinus pyralis

-

0.0007

N-[5-[(2,2-dimethylpropanoyl)amino]pyridin-2-yl]-3-hydroxybenzamide

Photinus pyralis

-

0.0011

N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide

Photinus pyralis

-

0.00063

octadecanoic acid

Photinus pyralis

-

IC50: 0.00063 mM

2.9

octanoic acid

Photinus pyralis

-

IC50: 2.9 mM

0.00068

tetradecanoic acid

Photinus pyralis

-

IC50: 0.00068 mM

additional information

5 - 6

red emitted light

5.4

red emitted light

5.5

shift of emission spectra to red region

7.5 - 7.8

yellow-green emitted light

7.5 - 8

7.6

yellow-green emitted light

7.8

8

8.1

-

8.5

wild-type enzyme, mutant enzymes H461D, H489K, H489D and H489M

9

recombinant circular enzyme

6.9

-

in vivo detection

7

7.2

-

assay at

7.3

-

mutant R337Q

7.4

-

optimum for binding to triazine dyes

7.5

7.6

-

tricine buffer

7.8

8

8.2

-

substrate: D-luciferin

8.5

8.6

-

reaction with 5,5-dimethyl-luciferyl-O-adenosine monophosphate

9.1

-

substrate: (4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid

additional information

2.5 - 10.5

pH activity range, recombinant circular enzyme

4 - 10

pH activity range, recombinant wild-type enzyme

7.5 - 8.5

-

6.5 - 8.5

-

pH 6.5: about 45% of activity maximum, pH 8.5: about 35% of activity maximum

7 - 8

-

7.5 - 8

7.5 - 8.5

-

peak emission at 560 nm

484827

8.2 - 9.1

-

additional information

-

buffers with pKa from 7.2 to 8.4 tested and no relationship with activity found

10

mutant enzyme H461D

20

mutant enzyme H489M

22

25

30

35

recombinant circular enzyme

37

assay at

20

23

-

purified

25

30

37

43

-

additional information

10 - 60

temperature activity range, recombinant wild-type enzyme and recombinant circular enzyme

22 - 28

-

24 - 27

-

assay at

37 - 45

-

6.2

calculated with ExPASy Compute pI/MW tool

6

isoelectric focusing

7.2

-

His10-tagged wild type enzyme

-

-

associated to

-

-

additional information

-

localized in peroxisomes when expressed in mammalian, plant and yeast cells

-

malfunction

the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference

physiological function

5 entries

additional information

P08659 pBLAST

LUCI_PHOPY

550

0

60745

Swiss-Prot

Show Sequence

other Location (Reliability: 2)

62000

SDS-PAGE

65500

calculated from amino acid sequence

100000

-

from sedimentation velocity of the crystalline form

484831, 484832, 484833, 484841

49000

-

x * 49000, N-terminal domain, SDS-PAGE

50000

50000 - 52000

500000

-

2 * 500000 sedimentation equilibrium study of guanidine hydrochloride-treated enzyme

53600

-

sedimentation velocity

60750

-

61160

-

calculated from sequence of cDNA

671309

61200

-

x * 61200, wild-type enzyme, SDS-PAGE

62000

89000 - 91000

-

low speed equilibrium sedimentation

92000 - 95000

-

high speed equilibrium sedimentation

484831, 484833

?

x * 61000, recombinant wild-type enzyme, SDS-PAGE, x * 80000, recombinant cyclized enzyme SpyCatcher-LUC-SpyTag, SDS-PAGE

?

dimer

monomer

-

484825, 484826, 484857

-

crystallization was achieved using the micro batch technique under oil at 4°C, 2 A resolution structure was determined at -173°C, 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

-

484864

extraction, 2 gel elutions, 5 crystallizations

-

D476P

site-directed mutagenesis, the mutant shows decreased thermostability compared to the wild-type

E311Q

site-directed mutagenesis, the mutant shows 65% specific activity compared to the wild-type

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

H461D

relative specific activity is 57.6% as compared to wild-type enzyme. Mutation decreases ATP binding affinity, reduces the melting temperature of protein by around 25°C and shifts its optimum temperature of activity to 10°C

H489D

relative specific activity is 112% as compared to wild-type enzyme. Mutation introduces a new salt bridge between the C-terminal and N-terminal domains and increases protein rigidity but only slightly improves its thermal stability

H489K

relative specific activity is 115% as compared to wild-type enzyme. Mutation increases protein rigidity but only slightly improves its thermal stability

H489M

relative specific activity is 103% as compared to wild-type enzyme

H489P

site-directed mutagenesis, the mutant shows improved thermostability while maintaining its catalytic efficiency compared to that of wild-type luciferase, the overall rigidity and local rigidity of H489Pmutant are greatly strengthened

I423L/D436G/L530R

the mutant shows a lower apparent Km value of 0.00076 mM than that of the wild-type enzyme

ins356E

green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 97% increase in specific activity

ins356K

green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 18% decrease in specific activity

ins356Q

at pH 5.5 red-emitting luciferase, increase in thermostability, 6% decrease in specific activity

ins356R

green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 12% decrease in specific activtiy

K329I

point mutation does not affect the orientation of critical residues in bioluminescence color determination. Thermostability and Km value for luciferin are decreased as compared to wild type enzyme. Intrinsic fluorescence and far-UV CD intensity in K329I mutant is decreased. Realative activity as compared to wild-type enzyme is 32%

764596

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

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

N229T

site-directed mutagenesis, the mutant shows 63% specific activity compared to the wild-type

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

R213K/T214N

site-directed mutagenesis, residues K213 and/or N214 are largely responsible for the 1.55fold increase in specific activity of the variant

R218Q

site-directed mutagenesis, the mutant shows 125% specific activity compared to the wild-type

R330Q

point mutation does not affect the orientation of critical residues in bioluminescence color determination. Thermostability and Km value for luciferin are decreased as compared to wild type enzyme. Increase in tryptophan fluorescence intensity and secondary structure content for R330Q as compared with wild type. Realative activity as compared to wild-type enzyme is 23%

764596

R337Q

site-directed mutagenesis, the mutant shows 26% specific activity compared to the wild-type

S284T

site-directed mutagenesis, a red-emitting mutant variant, the mutant shows 25% specific activity compared to the wild-type

S307P/H489P

site-directed mutagenesis, the mutation is randomly chosen outside the flexible regions as a control. The mutant has decreased kinetic stability and enhanced thermodynamic stability compared to the wild-type

T214A/A215L/I232A/F295L/E345K

the mutant enzyme displays high thermostability, retaining about 60% activity after 120 min at 45°C. Although the mutant shows higher maximum activity at high D-luciferin concentrations, its activity at low D-luciferin concentrations (below 0.004 mM) lags behind that of the mutantI423L/D436G/L530R

T214A/A215L/I232A/F295L/E345K/I423L/D436G/L530R

the mutant enzyme exhibits both improved thermostability and brighter luminescence at low luciferin concentrations, it may be useful for reporter gene applications

Y255F

site-directed mutagenesis, the mutant shows 71% specific activity compared to the wild-type

A296C/A326C

-

specific activity 676% (compared to wild-type 100%), Km (ATP) decreased compared to wild-type, Km (D-luciferin) decreased compared to wild-type, optimal temperature 35° (wild-type 25°C), optimal pH 8.5 (wild-type pH 8), activity remains 54% at 40°C for 5 min (compared to wild-type 0%), t1/2: 40 min at 35°C (compared to wild-type 5 min)

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

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

D474K

-

D476N mutation does not have any significant effect

D476N

-

D474K mutation destabilizes the protein. Flexibility analysis using dynamic quenching and limited proteolysis demonstrates that D474K mutation is much more flexible than wild-type

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 37°C is 7.36 min, compared to 3.06 min for the wild-type enzyme

E345K/A215L/I232A/T214A

-

half-life at 37°C is 75.1 min, compared to 3.06 min for the wild-type enzyme

E345K/A215L/I232A/T214A/F295L

-

half-life at 37°C is 82.1 min, compared to 3.06 min for the wild-type enzyme

E345K/I232A/T214A

-

half-life at 37°C is 15.5 min, compared to 3.06 min for the wild-type enzyme

E345K/I232A/T214A/F295L/S420T

-

half-life at 37°C is 72.4 min, compared to 3.06 min for the wild-type enzyme

E345K/T214A

-

half-life at 37°C is 8.5 min, compared to 3.06 min for the wild-type enzyme

F14R

-

improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme

F14R/L35Q/V182K/I232K/F465R

-

improved pH tolerance and stability up to 45°C, 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

F250S

F250T

37% specific activity at pH 7.8 compared to the wild type enzyme

F465R

-

improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme

G246A

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

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 45°C, no decrease in specific activity relative to the recombinant wild type enzyme

I232R

-

specific activity 75% (compared to wild-type 100%), Km (ATP) increased compared to wild-type, Km (D-luciferin) increased compared to wild-type, optimal temperature 25° (wild-type 25°C), optimal pH 8.5 (wild-type pH 8), activity remains 4% at 40°C for 5 min (compared to wild-type 0%), t1/2: 20 min at 35°C (compared to wild-type 5 min)

I232R/A296C/A326C

-

specific activity 358% (compared to wild-type 100%), Km (ATP) increased compared to wild-type, Km (D-luciferin) increased compared to wild-type, optimal temperature 35° (wild-type 25°C), optimal pH 8 (wild-type pH 8), activity remains 28% at 40°C for 5 min (compared to wild-type 0%), t1/2: 10 min at 35°C (compared to wild-type 5 min)

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

I423L/D436G/L530R

K529A

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 45°C, 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

L530S

1% activity compared to the wild type enzyme

L530V

50% activity compared to the wild type enzyme

L530Y

2% 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

R213E

-

same activity like wild-type luciferase

R213M

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

S184T

-

red-emitting luciferase with a bioluminescence maximum of 615 nm

671309

S284G

-

red light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase

S284T

-

red-emitting mutant, about 75% decrease of activitiy in vitro, in vivo more efficient light production

S293P

-

orange light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase

S347A

-

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

S440P/S456Y

-

mutant shows improved specificity and reactivity for ATP compared to wild-type

S440R/S456A

-

mutant shows improved specificity and reactivity for ATP compared to wild-type

S440R/S456V

-

mutant shows improved specificity for ATP compared to wild-type

T251A

-

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

-

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

-

improved pH tolerance and stability up to 45°C, 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

64% specific activity at pH 7.8 compared to the wild type enzyme

V241I/G246A/F250S

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

additional information

17 entries

8 - 10

recombinant circular LUC is stable at a pH range of 8.0-10.0, maintaining nearly 100% activity after incubation in various pH buffers for 30 min. Recombinant wild-type LUC maintains only 80% of its original activity after incubating at pH 10.0 for 30 min

746213

8

-

all spectra undergo a red-shift when cells are assayed under acidic conditions, whereas a blue-shift is observed at pH 8.0

676934

16.7

Tm value of recombinant wild-type LUC

25

t1/2: 17 min (wild-type enzyme), 9.5 min (mutant enzyme H461D), 12.6 min (mutant enzyme H489K), 20.2 min (mutant enzyme H489D) and 24.4 min (mutant enzyme H489M)

30

t1/2: 10.5 min (wild-type enzyme), 6.9 min (mutant enzyme H461D), 8.3 min (mutant enzyme H489K), 11.1 min (mutant enzyme H489D) and 9.5 min (mutant enzyme H489M)

35

35 - 45

free enzyme shows 65% remaning activity after 10 min at 35°C, inactivation after 4 min at 35°C, inactivation at 45°C

744062

37

thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 47 min

37.4

T50 for recombinant wild-type LUC

40

complete inactivation, mutant ins356Q still 20% residual activity

40.3

T1/2 value of recombinant cyclized LUC

42

thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 50 s

45

47.5

T50 for recombinant cyclized LUC

49.2

T50 value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein

51.4

T1/2 value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein

53.5

Tm value of recombinant wild-type LUC

55

complete inactivation

765519

70.2

Tm value of recombinant cyclized LUC

73.1

Tm value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein

15 - 45

-

when native and mutants are incubated 5 min at temperatures ranging from 15 to 45°C, D474K mutant is inactivated faster than native and D476N at all temperatures

20

-

after 20 min only 5% activity in the absence of ionic liquids but less than 1% in the presence of [1,1,3,3-tetramethylguanidine][lactate] and [1,1,3,3-tetramethylguanidine][propionate]

23

-

stability remains constant upon 120 min

727631

25 - 45

activity starts to decrease above 25°C and is almost completely lost at 45°C

30

32

-

after 20 min at 32°C wild-type and mutant D476N retain 24% original activity whereas mutant D474K shows only 2% remaining activity

35

37

40

45

-

mutant enzymes F14R, L35Q, V182K, I232K and F465R are stable up to 45°C

additional information

bovine serum albumin stabilizes

-

484833, 484836, 484843

decrease of remaining activity after trypsin hydrolysis at 23 and 37°C, 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

-

484833, 484836

enzyme is stable for several days adsorbed on polystyrene

-

484856

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

-

484837

more stable in phosphate buffer than in Tricine buffer

-

484836, 484843

mutant R337Q still 26% remaining activity after 15 min trypsin hydrolysis at 37°C

-

sorbitol, proline and sucrose with strong stabilizing effect on firefly luciferase activity at 35°C

-

stability in crude solutions varies

-

484830

stabilized by immobilization on polysaccharide carriers

-

5°C, pH 7.2, ammonium sulfate, EDTA, glycerol, several weeks

484861

4°C, 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

4°C, in 50 mM Tris-HCl, 1 mM EDTA, 150 mM NaCl, 1 mM DTT and 0.8 M ammonium sulfate pH 8.0

-

4°C, pH 7.0, 0.1 M phosphate, 1 mM 2-mercaptoethanol, immobilized, 3 weeks

-

484847

4°C, pH 7.5, ammonium sulfate, EDTA, as 10 mg protein/ml slurry, several months

-

484830

4°C, wild-type and mutant enzymes remain fully active for up to 6 months

-

-

gel filtration, affinity chromatography

Ni-chelate affinity chromatography

Ni-NTA Sepharose, yield of 95%

recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) pLysS by glutathione affinity chromatography

recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

recombinant mutants purified using ammonium sulfate precipitation and Sephacryl S-200 column chromatography

484861

recombinant secreted enzyme from Nicotiana benthamiana BY-2 cell medium by ultrafiltration, buffer exchange gel filtration, anion exchange chromatography, and dialysis

-

-

658085, 671309, 695557, 699453

a more efficient method for the purification and concentration of luciferase using aqueous two-phase extraction (ATPE) is designed. Downstream processing of luciferase from Photinus pyralis is carried out using polymer/salt aqueous two phase system (ATPS) at 4°C. The enzyme is observed to preferentially partition to the polyethylene glycol (PEG) rich top phase. The best results of purification (13.69 fold) and enzyme activity recovery (118.34%) are observed in the system containing 4.0% (w/w) PEG (1500) and 20.5% (w/w) (NH4)2SO4 with a phase volume ratio of 0.21

-

728712

affinity chromatography

-

alkyl-substituted Sepharose 4B affinity chromatography

-

676320

ammonium sulfate fractionation and gel filtration of the wild-type and several mutants

-

484865

ammonium sulfate fractionation and ion-exchange chromatography of the wild-type and several mutants

-

484867

glutathione Sepharose 4B affinity chromatography

immobilization with Procion blue and other tiazine dyes as a purification method

-

484858

immobilized ion affinity chromatography was used to purify a polyhistidine tagged recombinant enzyme

-

484863

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

688898

purification of a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases by ammonium sulfate precipitation, gel filtration and hydroxyapatite column chromatography

-

484870

several chromatographic and non chromatographic methods

-

484830, 484832, 484833

using Ni-NTA chromatography

-

727075, 727630, 727631, 728433

-

698393, 764010

expressed in Escherichia coli

expressed in Escherichia coli BL21(DE3)

expression in Escherichia coli

484861, 697221

expression in Escherichia coli BL21

gene luc, DNA and amino acid sequence determination and analysis, sequence comparisons of Photinus pyralis and Photinus scintillans luciferases, the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) pLysS, recombinant Luc contains the N-terminal peptide GlyProLeuGlySer-

recombinant coexpression of the luciferase with fused cyclization proteins SpyCatcher at the N-terminus and SpyTag at the C-terminus (pyCatcher-LUC-SpyTag) in Escherichia coli strain BL21(DE3)

recombinant expression from vector p35SHSPG in Nicotiana benthamiana BY-2 cells with intracellular enzyme localization, recombinant expression of the enzyme in Arabidopsis thaliana roots with enzyme localization around the nucleus, outside of the central vacuole and in the protoplasm

746376

recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)

recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS

744012

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

-

-

cloning of the cDNA encoding the destabilized enzyme into an adenoviral expression plasmid and transfection of Vero, Hep-2, Chang, A-549, COS-1, and HeLa cells, luciferase expression is linear with respect to viral multiplicity of infection, protein synthesis inhibiting drugs, e.g. shiga toxins of Escherichia coli, diphtheria toxin, Pseudomonas exotoxin A and the plant toxin ricin A, and cycloheximide, reduce bioluminescence respresenting the antiviral activity

-

675322

complete nucleotide sequence, expression in mammalian cells

-

484827

expressed in Candida albicans strain CAI4

-

675811

expressed in Escherichia coli as a His-tagged fusion protein

-

727075, 727630, 728433

expressed in Escherichia coli BL21 (DE3) cells

688898

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

685746

expressed in Escherichia coli strain BL21

expressed in Escherichia coli strain HMS174(DE3)

expressed in Escherichia coli strain JM109

689390

expressed in Escherichia coli strains XL1-Blue and BL21

expressed in Escherichia coli Top10 cells

-

expressed in Escherichia coli XL10-Gold cells

-

expressed in Saccharomyces cerevisiae

-

expression in Drosophila

-

484835

expression in Escherichia coli

-

484826, 484828, 484829

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 HEK-293 cells or Grip-Tite 293 MSR cells

-

expression in HEK-293T cells

-

697750

expression in L16 derived from CV-1 monkey kidney cells

-

expression in mouse cells

-

484835

expression in PC3 cells

-

expression in Spodoptera frugiperda clone 9-cells, expression in insect cells using a baculovirus vector

-

484825

expression in transfected Leishmania amazonensis strain LV79 amastigotes, transfection by electroporation

-

672992

expression of a polyhystidine tagged enzyme in Trichoplusia

-

484863

expression of a recombinant enzyme containing a protein kinase A recognition site

-

484873

expression of a recombinant luciferase-ubiquitin enzyme in Saccharomyces cerevisiae

-

484862

firefly lantern cDNA library

-

484828

gene expression in vegetative and symbiotic Rhizobium melioti and other gram-negative bacteria

-

into pET28a vector

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

-

overexpressed in Escherichia coli BL-21

-

727631

wild-type and mutant enzymes are expressed as GST-fusion proteins

-

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

analysis

biotechnology

industry

the enzyme is widely used in academia and industry due to its excellent sensitivity and dynamic range, and its ease of use

molecular biology

analysis

medicine

additional information

Matsuki, H.; Suzuki, A.; Kamaya, H.; Ueda, I.

Specific and non-specific binding of long-chain fatty acids to firefly luciferase: cutoff at octanate

Biochim. Biophys. Acta

1426

143-150

1999

Photinus pyralis

9878713

484825

Hasmain, S.E.; Nakhai, B.H.

Expression of the gene encoding firefly luciferase in insect cells using a baculovirus vector

Gene

91

135-138

1990

Photinus pyralis

2205537

484826

Palomares J.P.; DeLuca M.A.Helinski D.R.

Firefly luciferase enzyme for measuring gene expression in vegetative and symbiotic Rhizobium meliloti and other gram-negative bacteria

Gene

81

155-64

1989

Photinus pyralis

-

484827

De Wet, J.R.; Wood, K.V.; DeLuca, M.; Helinski, D.R.; Subramani, S.

Firefly luciferase gene: structure and expression in mammalian cells

Mol. Cell. Biol.

7

725-737

1987

Photinus pyralis

3821727

484828

De Wet, J.R.; Wood, K.V.; Helinski, D.R.; DeLuca, M.

Cloning firefly luciferase

Methods Enzymol.

133

3-14

1986

Photinus pyralis

3547031

484829

De Wet, J.R.; Wood, K.V.; Helinski, D.R.; DeLuca, M.

Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli

Proc. Natl. Acad. Sci. USA

82

7870-7873

1985

Photinus pyralis

3906652

484830

DeLuca M.; McElroy, W.D.

Purification and properties of firefly luciferase

Methods Enzymol.

57

3-15

1978

Photinus pyralis

-

DeLuca, M.

Firefly luciferase

Adv. Enzymol. Relat. Areas Mol. Biol.

44

37-68

1976

Photinus pyralis

775940

484832

Rajgopal S; Vijayalakshmi M.A.

Firefly luciferase: purification and immobilization

Enzyme Microb. Technol.

6

482-490

1984

Luciola mingrelica, Photinus pyralis

-

Leach F.R.

ATP determination with firefly luciferase

J. Appl. Biochem.

3

473-517

1981

Luciola mingrelica, Photinus pyralis

-

484834

Guranowski, A.; Sillero, M.A.G.; Sillero, A.

Firefly luciferase synthesizes P1,P4-bis(5-adenosyl)tetraphosphate (Ap4A) and other dinucleoside polyphosphates

FEBS Lett.

271

215-218

1990

Photinus pyralis

2172002

484835

Nguyen V.T; Morange M.; Bensaude O.

Protein denaturation during heat shock and related stress

J. Biol. Chem.

264

10487-10492

1989

Photinus pyralis

2499580

484836

Leach, F.R.; Webster, J.J.

Commercially available firefly luciferase reagents

Methods Enzymol.

133

51-70

1986

Photinus pyralis

3821551

484837

Thompson, A.; Nigro, J.; Seliger, H.H.

Efficient singlet oxygen inactivation of firefly luciferase

Biochem. Biophys. Res. Commun.

140

888-894

1986

Photinus pyralis

3778490

484838

Rajgopal S.; Vijayalakshmi M.A.

Studies on the interaction of firefly luciferase with triazine dyes

J. Chromatogr.

18

201-210

1986

Photinus pyralis

-

484839

DeLuca M.; McElroy, W.D.

Two kinetically distinguishable ATP sites in firefly luciferase

Biochem. Biophys. Res. Commun.

123

764-770

1984

Photinus pyralis

6487312

484840

Moye,r J.D.; Henderson, J.F.

Nucleoside triphosphate specificity of firefly luciferase

Anal. Biochem.

131

187-189

1983

Photinus pyralis

6614450

Kricka, L.J.; DeLuca, M.

Effect of solvents on the catalytic activity of firefly luciferase

Arch. Biochem. Biophys.

217

674-681

1982

Photinus pyralis

7138032

484842

Nichols, W.W.; Curtis, G. D.W.; Johnston, H.H.

Choice of buffer anion for the assay of adenosine 5'-triphosphate using firefly luciferase

Anal. Biochem.

114

396-397

1981

Photinus pyralis

7304931

484843

Webster, J.J.; Leach, F.R.

Optimization of the firefly luciferase assay for ATP

J. Appl. Biochem.

2

469-479

1980

Photinus pyralis

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484844

Webster, J.J.; Chang, J.C.; Manley, E.R.; Spivey, H.O.; Leach ,F.R.

Buffer effects on ATP analysis by firefly luciferase

Anal. Biochem.

106

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1980

Photinus pyralis

7191217

484845

DeLuca, M.; Wannlund, J.; McElroy, W.D.

Factors affecting the kinetics of light emission from crude and purified firefly luciferase

Anal. Biochem.

95

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1979

Photinus pyralis

495953

Momsen, G.

Firefly luciferase reacts with p1,p5-di(adenosine-5'-)pentaphosphate and adenosine-5'-tetraphosphate

Biochem. Biophys. Res. Commun.

84

816-822

1978

Photinus pyralis

718719

484847

Lee, Y.; Jablonski, I.; DeLuca, M.

Immobilization of firefly luciferase on glass rods: properties of the immobilized enzyme

Anal. Biochem.

80

496-501

1977

Photinus pyralis

18948

484848

Lemaster,s J.J.; Jackenbroc, C.R.

Kinetics of product inhibition during firefly luciferase luminiscense

Biochemistry

16

445-447

1977

Photinus pyralis

836795

Lee, R.; McElroy, W.D.

Role and reactivity of sulfhydryl groups in firefly luciferase

Biochemistry

8

130-135

1969

Photinus pyralis

5777315

484850

Lee, R.; McElroy, W.D.

Effects of 5'-adenylic acid on firefly luciferase

Arch. Biochem. Biophys.

145

78-84

1971

Photinus pyralis

5123147

484851

Denburg, J.L.; McElroy, W.D.

Catalytic subunit of firefly luciferase

Biochemistry

9

4619-4625

1970

Photinus pyralis

5482267

484852

Denburg, J.L.; McElroy, W.D.

Anion inhibition of firefly luciferase

Arch. Biochem. Biophys.

141

668-675

1970

Photinus pyralis

5497150

Lee, R.T.; Denburg, J.L.; McElroy, W.D.

Substrate-binding properties of firefly luciferase. II. ATP-binding site

Arch. Biochem. Biophys.

141

38-52

1970

Photinus pyralis

5480123

484854

Lee, R.T.; Denbur,g J.L.; McElroy, W.D.

Substrate-binding properties of firefly luciferase. I. Luciferin-binding site

Arch. Biochem. Biophys.

134

381-394

1969

Photinus pyralis

5354768

484855

Rajgopal S.; Vijayalakshmi M.A.

Role of metal ions in triazine dye affinity chromatography: the metal mediated interaction of triazine dyes with firefly luciferase

Enzyme Microb. Technol.

6

555-559

1984

Photinus pyralis

-

484856

Kricka L.

Clinical and biochemical applications of luciferases and luciferines

Anal. Biochem.

175

14-21

1988

Photinus pyralis

3072882

Gould, S.J.; Subraman,i S.

Firefly luciferase as a tool in molecular and cell biology

Anal. Biochem.

175

5-13

1988

Photinus pyralis

3072883

484858

Rajgopal S.; Vijayalakshmi M.A.

Interaction of firefly luciferase with triazine dyes

J. Chromatogr.

280

77-84

1983

Photinus pyralis

-

484859

Lembert, N.; Idahl, L.A.

Regulatory effects of ATP and luciferin on firefly luciferase activity

Biochem. J.

305

929-933

1995

Photinus pyralis

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484860

Branchini, B.; Magyar, R.; Murtiashaw, M.; Anderson, S.; Helgerson, L.; Zimmer, M.

Site-directed mutagenesis of firefly luciferase active site amino acids: a proposed model for bioluminiscence color

Biochemistry

38

13223-13230

1999

Photinus pyralis

10529195

484861

Thompson, J.F.; Geoghegan, K.F.; Lloyd, D.B.; Lanzetti, A.J.; Magyar, R.A.; Anderson, S.M.; Branchini, B.R.

Mutation of protease-sensitive region in firefly luciferase alters light emission properties

J. Biol. Chem.

272

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1997

Photinus pyralis (P08659), Photinus pyralis

9228050

484862

Worley, C.K.; Ling, R.; Callis, J.

Engineering in vivo instability of firefly luciferase and Escherichia coli beta-glucuronidase in higher plants using recognition elements from the ubiquitin pathway

Plant Mol. Biol.

37

337-347

1998

Photinus pyralis

9617805

484863

Michel, P.; Torkkeli, T.; Karp, M.; Oker-Blom, C.

Expression and purification of polyhistidine-tagged firefly luciferase in insect cells--a potential alternative for process scale-up

J. Biotechnol.

85

49-56

2001

Photinus pyralis

11164962

484864

Conti, E.; Franks, N.P.; Brick, P.

Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes

Structure

4

287-298

1996

Photinus pyralis

8805533

484865

Waud, J.P.; Sala-Newby, G.B.; Matthews, S.B.; Campbell, A.K.

Engineering the C-terminus of firefly luciferase as an indicator of covalent modification of proteins

Biochim. Biophys. Acta

1292

89-98

1996

Photinus pyralis

8547353

484866

Sala-Newby, G.B.; Campbell, A.K.

Stepwise removal of the C-terminal 12 amino acids of firefly luciferase results in graded loss of activity

Biochim. Biophys. Acta

1206

155-160

1994

Photinus pyralis

8186245

484867

Wang, Xi.; Yang, J.; Huang, W.; He, L.; Yu, J.; Lin, Q.; Li, W.; Zhou, H.

Effects of removal of the N-terminal amino acid residues on the activity and conformation of firefly luciferase

Int. J. Biochem. Cell Biol.

34

983-991

2002

Photinus pyralis

12007636

484868

Lundovskikh, I.; Dementieva, E.; Ugarova, N.

Recombinant firefly luciferase in Escherichia coli

Appl. Biochem. Biotechnol.

88

127-135

2000

Luciola mingrelica, Photinus pyralis

-

484869

Min, K.; Steghens, J.

ADP is produced by firefly luciferase but its synthesis is independent of the light emitting properties

Biochimie

83

523-528

2001

Photinus pyralis

11506897

484870

Hirokawa, K.; Kajiyama, N.; Murakami, S.

Improved practical usefulness of firefly luciferase by gene chimerization and random mutagenesis

Biochim. Biophys. Acta

1597

271-279

2002

Luciola cruciata, Photinus pyralis

12044905

484873

Sala-Newby, G.; Campbell, A.K.

Engineering firefly luciferase as an indicator of cyclic AMP-dependent protein kinase in living cells

FEBS Lett.

307

241-244

1992

Photinus pyralis

1322831

484874

Ford, S.R.; Hall, M.S.; Leach, F.R.

Enhancement of firefly luciferase activity by cytidine nucleotides

Anal. Biochem.

204

283-291

1992

Photinus pyralis

1332531

484875

Lundin, A.

Use of firefly luciferase in ATP-related assays of biomass, enzymes and metabolites

Methods Enzymol.

305

346-370

2000

Photinus pyralis

10812612

Nakamura, M.; Maki, S.; Amano, Y.; Ohkita, Y.; Niwa, K.; Hirano, T.; Ohmiya, Y.; Niwa, H.

Firefly luciferase exhibits bimodal action depending on the luciferin chirality

Biochem. Biophys. Res. Commun.

331

471-475

2005

Photinus pyralis

15850783

Branchini, B.R.; Southworth, T.L.; Murtiashaw, M.H.; Boije, H.; Fleet, S.E.

A mutagenesis study of the putative luciferin binding site residues of firefly luciferase

Biochemistry

42

10429-10436

2003

Photinus pyralis

12950169

Branchini, B.R.; Southworth, T.L.; Murtiashaw, M.H.; Magyar, R.A.; Gonzalez, S.A.; Ruggiero, M.C.; Stroh, J.G.

An alternative mechanism of bioluminescence color determination in firefly luciferase

Biochemistry

43

7255-7262

2004

Photinus pyralis, Pyrophorus plagiophthalamus

15182171

Branchini, B.R.; Southworth, T.L.; Murtiashaw, M.H.; Wilkinson, S.R.; Khattak, N.F.; Rosenberg, J.C.; Zimmer, M.

Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain

Biochemistry

44

1385-1393

2005

Photinus pyralis (P08659), Photinus pyralis

15683224

Zako, T.; Ayabe, K.; Aburatani, T.; Kamiya, N.; Kitayama, A.; Ueda, H.; Nagamune, T.

Luminescent and substrate binding activities of firefly luciferase N-terminal domain

Biochim. Biophys. Acta

1649

183-189

2003

Photinus pyralis

12878037

658219

Takehara, K.; Kamaya, H.; Ueda, I.

Inhibition of firefly luciferase by alkane analogues

Biochim. Biophys. Acta

1721

124-129

2005

Photinus pyralis

15652187

Oba, Y.; Sato, M.; Ojika, M.; Inouye, S.

Enzymatic and genetic characterization of firefly luciferase and Drosophila CG6178 as a fatty acyl-CoA synthetase

Biosci. Biotechnol. Biochem.

69

819-828

2005

Photinus pyralis (P08659), Luciola cruciata (P13129)

15849423

Oba, Y.; Ojika, M.; Inouye, S.

Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase

FEBS Lett.

540

251-254

2003

Luciola cruciata, Photinus pyralis

12681517

Baggett, B.; Roy, R.; Momen, S.; Morgan, S.; Tisi, L.; Morse, D.; Gillies, R.J.

Thermostability of firefly luciferases affects efficiency of detection by in vivo bioluminescence

Mol. Imaging

3

324-332

2004

Photinus pyralis

15802049

671309

Branchini, B.R.; Ablamsky, D.M.; Murtiashaw, M.H.; Uzasci, L.; Fraga, H.; Southworth, T.L.

Thermostable red and green light-producing firefly luciferase mutants for bioluminescent reporter applications

Anal. Biochem.

361

253-262

2007

Photinus pyralis

17181991

671781

Bakhtiarova, A.; Taslimi, P.; Elliman, S.J.; Kosinski, P.A.; Hubbard, B.; Kavana, M.; Kemp, D.M.

Resveratrol inhibits firefly luciferase

Biochem. Biophys. Res. Commun.

351

481-484

2006

Photinus pyralis

17064666

Law, G.H.; Gandelman, O.A.; Tisi, L.C.; Lowe, C.R.; Murray, J.A.

Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance

Biochem. J.

397

305-312

2006

Photinus pyralis

16551268

672578

Branchini, B.R.; Murtiashaw, M.H.; Carmody, J.N.; Mygatt, E.E.; Southworth, T.L.

Synthesis of an N-acyl sulfamate analog of luciferyl-AMP: a stable and potent inhibitor of firefly luciferase

Bioorg. Med. Chem. Lett.

15

3860-3864

2005

Photinus pyralis

15990297

Oba, Y.; Tanaka, K.; Inouye, S.

Catalytic properties of domain-exchanged chimeric proteins between firefly luciferase and Drosophila fatty acyl-CoA synthetase CG6178

Biosci. Biotechnol. Biochem.

70

2739-2744

2006

Photinus pyralis (P08659), Photinus pyralis

17090919

672992

Lang, T.; Goyard, S.; Lebastard, M.; Milon, G.

Bioluminescent Leishmania expressing luciferase for rapid and high throughput screening of drugs acting on amastigote-harbouring macrophages and for quantitative real-time monitoring of parasitism features in living mice

Cell. Microbiol.

7

383-392

2005

Photinus pyralis

15679841

673086

Fraga, H.; Fernandes, D.; Novotny, J.; Fontes, R.; Esteves da Silva, J.C.

Firefly luciferase produces hydrogen peroxide as a coproduct in dehydroluciferyl adenylate formation

Chembiochem

7

929-935

2006

Photinus pyralis

16642538

Fraga, H.; Fernandes, D.; Fontes, R.; Esteves da Silva, J.C.

Coenzyme A affects firefly luciferase luminescence because it acts as a substrate and not as an allosteric effector

FEBS J.

272

5206-5216

2005

Photinus pyralis

16218952

Ayabe, K.; Zako, T.; Ueda, H.

The role of firefly luciferase C-terminal domain in efficient coupling of adenylation and oxidative steps

FEBS Lett.

579

4389-4394

2005

Photinus pyralis

16061229

675214

Harrison, E.M.; Garden, O.J.; Ross, J.A.; Wigmore, S.J.

Firefly luciferase terminally degraded by mild heat exposure: implications for reporter assays

J. Immunol. Methods

310

182-185

2006

Photinus pyralis

16443236

675322

Zhao, L.; Haslam, D.B.

A quantitative and highly sensitive luciferase-based assay for bacterial toxins that inhibit protein synthesis

J. Med. Microbiol.

54

1023-1030

2005

Photinus pyralis

16192432

675811

Doyle, T.C.; Nawotka, K.A.; Purchio, A.F.; Akin, A.R.; Francis, K.P.; Contag, P.R.

Expression of firefly luciferase in Candida albicans and its use in the selection of stable transformants

Microb. Pathog.

40

69-81

2006

Photinus pyralis

16427765

676320

Venkatesh, B.; Arifuzzaman, M.; Mori, H.; Suzuki, S.; Taguchi, T.; Ohmiya, Y.

Use of GFP tags to monitor localization of different luciferases in E. coli

Photochem. Photobiol.

4

740-743

2005

Photinus pyralis

16121286

Shapiro, E.; Lu, C.; Baneyx, F.

A set of multicolored Photinus pyralis luciferase mutants for in vivo bioluminescence applications

Protein Eng. Des. Sel.

18

581-587

2005

Photinus pyralis

16243898

Mortazavi, M.; Hosseinkhani, S.; Khajeh, K.; Ranjbar, B.; Emamzadeh, A.R.

Spectroscopic and functional characterization of Lampyris turkestanicus luciferase: a comparative study

Acta Biochim. Biophys. Sin. (Shanghai)

40

365-374

2008

Photinus pyralis (Q27758), Photinus pyralis, Lampyris turkestanicus (Q5UFR2), Lampyris turkestanicus

18465021

Fujii, H.; Noda, K.; Asami, Y.; Kuroda, A.; Sakata, M.; Tokida, A.

Increase in bioluminescence intensity of firefly luciferase using genetic modification

Anal. Biochem.

366

131-136

2007

Photinus pyralis (Q27758), Photinus pyralis

17540326

Branchini, B.R.; Ablamsky, D.M.; Rosenman, J.M.; Uzasci, L.; Southworth, T.L.; Zimmer, M.

Synergistic mutations produce blue-shifted bioluminescence in firefly luciferase

Biochemistry

46

13847-13855

2007

Photinus pyralis (Q27758), Photinus pyralis

17994766

685746

Noda, K.; Matsuno, T.; Fujii, H.; Kogure, T.; Urata, M.; Asami, Y.; Kuroda, A.

Single bacterial cell detection using a mutant luciferase

Biotechnol. Lett.

30

1051-1054

2008

Photinus pyralis, Photinus pyralis (Q27758)

18224280

Yousefi-Nejad, M.; Hosseinkhani, S.; Khajeh, K.; Ranjbar, B.

Expression, purification and immobilization of firefly luciferase on alkyl-substituted Sepharose 4B

Enzyme Microb. Technol.

40

740-746

2007

Photinus pyralis (Q27758)

-

687295

Nakatani, N.; Hasegawa, J.Y.; Nakatsuji, H.

Red light in chemiluminescence and yellow-green light in bioluminescence: color-tuning mechanism of firefly, Photinus pyralis, studied by the symmetry-adapted cluster-configuration interaction method

J. Am. Chem. Soc.

129

8756-8765

2007

Photinus pyralis (Q27758), Photinus pyralis

17585760

Auld, D.S.; Southall, N.T.; Jadhav, A.; Johnson, R.L.; Diller, D.J.; Simeonov, A.; Austin, C.P.; Inglese, J.

Characterization of chemical libraries for luciferase inhibitory activity

J. Med. Chem.

51

2372-2386

2008

Photinus pyralis (Q27758)

18363348

688898

Svetlov, M.S.; Kolb, V.A.; Spirin, A.S.

Folding of the firefly luciferase polypeptide chain with the immobilized C terminus

Mol. Biol.

41

86-92

2007

Photinus pyralis (Q27758)

-

689390

Michelini, E.; Cevenini, L.; Mezzanotte, L.; Ablamsky, D.; Southworth, T.; Branchini, B.R.; Roda, A.

Combining intracellular and secreted bioluminescent reporter proteins for multicolor cell-based assays

Photochem. Photobiol. Sci.

7

212-217

2008

Pyrophorus plagiophthalamus, Photinus pyralis (Q27758), Photinus pyralis, Gaussia princeps (Q9BLZ2), Gaussia princeps

18264589

Noda, K.; Goto, H.; Murakami, Y.; Ahmed, A.B.; Kuroda, A.

Endotoxin assay by bioluminescence Using mutant firefly luciferase

Anal. Biochem.

397

152-155

2010

Photinus pyralis

19850001

Moradi, A.; Hosseinkhani, S.; Naderi-Manesh, H.; Sadeghizadeh, M.; Alipour, B.S.

Effect of charge distribution in a flexible loop on the bioluminescence color of firefly luciferases

Biochemistry

48

575-582

2009

Photinus pyralis (P08659), Photinus pyralis

19119851

696465

Kim, J.; Moon, C.H.; Jung, S.; Paik, S.R.

alpha-Synuclein enhances bioluminescent activity of firefly luciferase by facilitating luciferin localization

Biochim. Biophys. Acta

1794

309-314

2009

Photinus pyralis

19028608

Inouye, S.

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Cell. Mol. Life Sci.

67

387-404

2010

Pyrearinus termitilluminans (AF116843), Photinus pyralis (P08659), Luciola cruciata (P13129), Aquatica lateralis (Q01158), Lampyroidea maculata (Q1WLP6), Luciola parvula (Q25118), Pyrocoelia miyako (Q26076), Luciola mingrelica (Q26304), Lampyris noctiluca (Q27688), Photuris pensylvanica (Q27757), Lampyris turkestanicus (Q5UFR2), Cratomorphus distinctus (Q5USC8), Pyrophorus mellifluus (Q717B6), Pyrophorus plagiophthalamus (Q718F0), Hotaria unmunsana (Q8T6U3), Pyrocoelia rufa (Q9GPF9), Phrixothrix hirtus (Q9U4U7), Phrixothrix vivianii (Q9U4U8)

19859663

697750

Berger, F.; Paulmurugan, R.; Bhaumik, S.; Gambhir, S.S.

Uptake kinetics and biodistribution of 14C-D-luciferin--a radiolabeled substrate for the firefly luciferase catalyzed bioluminescence reaction: impact on bioluminescence based reporter gene imaging

Eur. J. Nucl. Med. Mol. Imaging

35

2275-2285

2008

Photinus pyralis

18661130

Mehrabi, M.; Hosseinkhani, S.; Ghobadi, S.

Stabilization of firefly luciferase against thermal stress by osmolytes

Int. J. Biol. Macromol.

43

187-191

2008

Photinus pyralis

18555523

698393

Marques, S.M.; Esteves da Silva, J.C.

Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions

IUBMB Life

61

6-17

2009

Photinus pyralis (P08659), Photinus pyralis

18949818

Auld, D.S.; Zhang, Y.Q.; Southall, N.T.; Rai, G.; Landsman, M.; Maclure, J.; Langevin, D.; Thomas, C.J.; Austin, C.P.; Inglese, J.

A basis for reduced chemical library inhibition of firefly luciferase obtained from directed evolution

J. Med. Chem.

52

1450-1458

2009

Photinus pyralis, Photuris pensylvanica

19215089

Chandran, S.S.; Williams, S.A.; Denmeade, S.R.

Extended-release PEG-luciferin allows for long-term imaging of firefly luciferase activity in vivo

Luminescence

24

35-38

2009

Photinus pyralis

18780328

Ribeiro, C.; Esteves da Silva, J.C.

Kinetics of inhibition of firefly luciferase by oxyluciferin and dehydroluciferyl-adenylate

Photochem. Photobiol. Sci.

7

1085-1090

2008

Photinus pyralis

18754056

Caysa, H.; Jacob, R.; Muether, N.; Branchini, B.; Messerle, M.; Soeling, A.

A redshifted codon-optimized firefly luciferase is a sensitive reporter for bioluminescence imaging

Photochem. Photobiol. Sci.

8

52-56

2009

Photinus pyralis

19247529

Riahi-Madvar, A.; Hosseinkhani, S.

Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis

Protein Eng. Des. Sel.

22

655-663

2009

Photinus pyralis

19661129

Ebrahimi, M.; Hosseinkhani, S.; Heydari, A.; Khavari-Nejad, R.A.; Akbari, J.

Improvement of thermostability and activity of firefly luciferase through [TMG][Ac] ionic liquid mediator

Appl. Biochem. Biotechnol.

168

604-615

2012

Photinus pyralis

22810202

Fushimi, T.; Miura, N.; Shintani, H.; Tsunoda, H.; Kuroda, K.; Ueda, M.

Mutant firefly luciferases with improved specific activity and dATP discrimination constructed by yeast cell surface engineering

Appl. Microbiol. Biotechnol.

97

4003-4011

2013

Photinus pyralis

23149753

Woodroofe, C.C.; Meisenheimer, P.L.; Klaubert, D.H.; Kovic, Y.; Rosenberg, J.C.; Behney, C.E.; Southworth, T.L.; Branchini, B.R.

Novel heterocyclic analogues of firefly luciferin

Biochemistry

51

9807-9813

2012

Photinus pyralis

23164087

Amini-Bayat, Z.; Hosseinkhani, S.; Jafari, R.; Khajeh, K.

Relationship between stability and flexibility in the most flexible region of Photinus pyralis luciferase

Biochim. Biophys. Acta

1824

350-358

2012

Photinus pyralis

22155276

Liu, Y.; Fang, J.; Cai, H.; Xiao, F.; Ding, K.; Hu, Y.

Identification and synthesis of substituted pyrrolo[2,3-d]pyrimidines as novel firefly luciferase inhibitors

Bioorg. Med. Chem.

20

5473-5482

2012

Photinus pyralis

22898255

Karimzadeh, S.; Moradi, M.; Hosseinkhani, S.

Delicate balance of electrostatic interactions and disulfide bridges in thermostability of firefly luciferase

Int. J. Biol. Macromol.

51

837-844

2012

Photinus pyralis

22750581

727631

Riahi-Madvar, A.; Hosseinkhani, S.; Rezaee, F.

Implication of Arg213 and Arg337 on the kinetic and structural stability of firefly luciferase

Int. J. Biol. Macromol.

52

157-163

2013

Photinus pyralis

22986180

Ebrahimi, M.; Hosseinkhani, S.; Heydari, A.; Khavari-Nejad, R.; Akbari, J.

Controversial effect of two methylguanidine-based ionic liquids on firefly luciferase

Photochem. Photobiol. Sci.

11

828-834

2012

Photinus pyralis

22391965

728712

Priyanka, B.; Rastogi, N.; Raghavarao, K.; Thakur, M.

Downstream processing of luciferase from fireflies (Photinus pyralis) using aqueous two-phase extraction

Process Biochem.

47

1358-1363

2012

Photinus pyralis

-

744012

Branchini, B.R.; Southworth, T.L.; Fontaine, D.M.; Kohrt, D.; Talukder, M.; Michelini, E.; Cevenini, L.; Roda, A.; Grossel, M.J.

An enhanced chimeric firefly luciferase-inspired enzyme for ATP detection and bioluminescence reporter and imaging applications

Anal. Biochem.

484

148-153

2015

Photinus pyralis (P08659), Photinus pyralis, Luciola italica (Q1AG35), Luciola italica

26049097

744013

Morita, N.; Haga, S.; Ohmiya, Y.; Ozaki, M.

Long-term ex vivo and in vivo monitoring of tumor progression by using dual luciferases

Anal. Biochem.

497

24-26

2016

Photinus pyralis (P08659)

26717897

744062

Noori, A.R.; Hosseinkhani, S.; Ghiasi, P.; Akbari, J.; Heydari, A.

Magnetic nanoparticles supported ionic liquids improve firefly luciferase properties

Appl. Biochem. Biotechnol.

172

3116-3127

2014

Photinus pyralis (P08659), Photinus pyralis

24492953

Branchini, B.R.; Southworth, T.L.; Fontaine, D.M.; Davis, A.L.; Behney, C.E.; Murtiashaw, M.H.

A Photinus pyralis and Luciola italica chimeric firefly luciferase produces enhanced bioluminescence

Biochemistry

53

6287-6289

2014

Photinus pyralis (P08659), Photinus pyralis, Luciola italica (Q1AG35), Luciola italica

25264115

Yu, H.; Zhao, Y.; Guo, C.; Gan, Y.; Huang, H.

The role of proline substitutions within flexible regions on thermostability of luciferase

Biochim. Biophys. Acta

1854

65-72

2015

Photinus pyralis (P08659), Photinus pyralis

25448017

Branchini, B.R.; Southworth, T.L.; Fontaine, D.M.; Murtiashaw, M.H.; McGurk, A.; Talukder, M.H.; Qureshi, R.; Yetil, D.; Sundlov, J.A.; Gulick, A.M.

Cloning of the orange light-producing luciferase from Photinus scintillans - a new proposal on how bioluminescence color is determined

Photochem. Photobiol.

93

479-485

2017

Photinus scintillans (A0A1B3TNR9), Photinus scintillans, Photinus pyralis (P08659), Photinus pyralis

27861940

Si, M.; Xu, Q.; Jiang, L.; Huang, H.

SpyTag/SpyCatcher cyclization enhances the thermostability of firefly luciferase

PLoS ONE

11

e0162318

2016

Photinus pyralis (P08659), Photinus pyralis

27658030

746376

Mitani, Y.; Oshima, Y.; Mitsuda, N.; Tomioka, A.; Sukegawa, M.; Fujita, M.; Kaji, H.; Ohmiya, Y.

Efficient production of glycosylated Cypridina luciferase using plant cells

Protein Expr. Purif.

133

102-109

2017

Photinus pyralis (P08659)

28288897

Li, Y.; Jin, C.; Xu, H.; Wu, W.; Wang, Y.; Wu, J.; Liu, T.; Wan, G.; Yue, X.; Bu, X.

Identification of 2-benzylidene-tetralone derivatives as highly potent and reversible firefly luciferase inhibitors

ACS Med. Chem. Lett.

13

304-311

2022

Photinus pyralis (P08659)

35178187

Pozzo, T.; Akter, F.; Nomura, Y.; Louie, A.Y.; Yokobayashi, Y.

Firefly luciferase mutant with enhanced activity and thermostability

ACS Omega

3

2628-2633

2018

Photinus pyralis (P08659), Photinus pyralis

30023842

Rahban, M.; Salehi, N.; Saboury, A.A.; Hosseinkhani, S.; Karimi-Jafari, M.H.; Firouzi, R.; Rezaei-Ghaleh, N.; Moosavi-Movahedi, A.A.

Histidine substitution in the most flexible fragments of firefly luciferase modifies its thermal stability

Arch. Biochem. Biophys.

629

8-18

2017

Photinus pyralis (P08659)

28711358