1.13.12.7: firefly luciferase
This is an abbreviated version!
For detailed information about firefly luciferase, go to the full flat file.
Word Map on EC 1.13.12.7
-
1.13.12.7
-
bioluminescence
-
luminescence
-
chemiluminescence
-
emit
-
renilla
-
noninvasive
-
luciferases
-
cypridina
-
photon
-
lentiviral
-
adenovirus
-
click
-
luciferase-expressing
-
herpes
-
engraft
-
nude
-
co-transfected
-
cytomegalovirus
-
camera
-
electroporation
-
simplex
-
hsp70
-
emitter
-
replication-deficient
-
excited-state
-
promoter-driven
-
charge-coupled
-
nonviral
-
nanoluc
-
non-invasively
-
gaussia
-
luminol
-
intramyocardial
-
coelenterazine
-
bicistronic
-
yellow-green
-
molecular biology
-
light-emitting
-
cap-independent
-
aequorin
-
biotechnology
-
red-shifted
-
dnaj
-
luminometer
-
grpe
-
polyethylenimine
-
bioimaging
-
luciferase-based
-
medicine
-
photoproteins
-
glow
-
analysis
-
multicolor
-
brighter
- 1.13.12.7
-
bioluminescence
-
luminescence
-
chemiluminescence
-
emit
- renilla
-
noninvasive
- luciferases
- cypridina
-
photon
-
lentiviral
- adenovirus
-
click
-
luciferase-expressing
-
herpes
-
engraft
-
nude
-
co-transfected
- cytomegalovirus
-
camera
-
electroporation
- simplex
- hsp70
-
emitter
-
replication-deficient
-
excited-state
-
promoter-driven
-
charge-coupled
-
nonviral
- nanoluc
-
non-invasively
- gaussia
- luminol
-
intramyocardial
- coelenterazine
-
bicistronic
-
yellow-green
- molecular biology
-
light-emitting
-
cap-independent
- aequorin
- biotechnology
-
red-shifted
- dnaj
-
luminometer
- grpe
- polyethylenimine
-
bioimaging
-
luciferase-based
- medicine
-
photoproteins
-
glow
- analysis
-
multicolor
-
brighter
Reaction
Synonyms
AL1, AL2, beetle luciferase, CBG99luc, CBRluc, FFL, firefly luciferase, firefly luciferin luciferase, fluc, LpLuc1, LpLuc2, Luc, Luc1, Luc1-type luciferase, Luc2, Luc2-type luciferase, luciferase, luciferase (firefly luciferin), luciferase FM, luciferin, Luciola italica luciferase, lucPpe, lucPpy, orange light-producing luciferase, oxygen 4-oxidoreductase, PC3-Luc, Photinus luciferin 4-monooxygenase (ATP-hydrolyzing), Photinus pyralis luciferase, PML, PpLase, Ppy, Ppy GR-TS, Ppy RE-TS, PpyWT, PsntWT
ECTree
1.13.12.7 firefly luciferaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 1.13.12.7 - firefly luciferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
15 - 40
at 35°C native luciferase completely inactive, mutant H245N still 80% residual activity, mutant S284T and H431Y about 20% residual activity
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]
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)
25 - 45
30
32
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
37
40
42
45
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
55
73.1
Tm value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein
additional information
25 - 45
activity starts to decrease above 25°C and is almost completely lost at 45°C
25 - 45
activity starts to decrease above 25°C and is almost completely lost at 45°C
30
-
after 20 min more less than 1% remaining activity in the presence of [1,1,3,3-tetramethylguanidine][propionate]
30
-
after 20 min more than 10% remaining activity in the presence of [1,1,3,3-tetramethylguanidine][lactate]
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)
32
mutant E354R, E354K, E354R/ins356Arg with greater thermostability than wild-type luciferase
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
thermostability of recombinant wild-type and mutant enzymes, overview
35
-
about 70% loss of activity within 10 min, no residual activity after 60 min, in presence of osmolytes higher residual activity after 60 min: 90% with 1.5 M sucrose, 50% with 1.5 M sorbitol, 35% with 1.5 M proline
35
-
T1/2 results show that half-lives (t1/2) of wild-type, mutant A296C/A326C, mutant A296C/A326C/I232R and mutant I232R are 5, 40, 10 and 20 min at 35°C respectively
35
t1/2: 6.1 min (wild-type enzyme), 3.7 min (mutant enzyme H461D), 6.4 min (mutant enzyme H489K), 6.5 min (mutant enzyme H489D) and 5.7 min (mutant enzyme H489M)
37
-
half-life: 3.06 min for wild-type enzyme,8.5 min for mutant enzyme E345K/T214A, 15.5 min for E345K/I232A/T214A, 7.36 min for E345K/A215L, 72.4 min for E345K/I232A/T214A/F295L/S420T, 82.1 min for E345K/A215L/I232A/T214A/F295L, 75.1 min for E345K/A215L/I232A/T214A
37
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 47 min
37
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 240 min
37
4 h, 90% resiudal activity, 24 h, 70% residual activity, respectively, for engineered commercial enzyme. Wild-type enzyme loses 80% of initial activity within 39 min
40
-
at 40°C for 45 min the activity of the enzyme decreased to less than 1% of control
40
immobilized enzyme forms are stable for 1 min at 40°C and then lose their activities
40
-
thermal stability experiments of mutant A296C/A326C, mutant A296C/A326C/I232R and mutant I232R shows that their original activity remains approximately 54%, 28%, and 4% after incubation at 40°C for 5 min, respectively (compared to wild-type 0%)
42
50% decrease in activity after 6.9 min for wild-type luciferase, for mutant S118C after 13.4 min
42
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 50 s
42
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 61 s
45
-
mutant enzymes F14R, L35Q, V182K, I232K and F465R are stable up to 45°C
45
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 25 s
45
the mutant enzyme T214A/A215L/I232A/F295L/E345K displays high thermostability, retaining about 60% activity after 120 min at 45°C
45
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 40 s
additional information
-
a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases is more stable than the wild type enzyme, retaining 75% of the activity after 10 min at 50°C
additional information
-
higher stability in frozen state than in refrigerated
additional information
thermal stability and activity at 35°C of the enzyme in presence of magnetic magnetite nanoparticles supported ionic liquids is increased compared to the free enzyme, overview
additional information
-
thermal stability and activity at 35°C of the enzyme in presence of magnetic magnetite nanoparticles supported ionic liquids is increased compared to the free enzyme, overview
