1.13.12.7: firefly luciferase

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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

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 Oxidoreductases

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

1.13.12.7 firefly luciferase

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Results	in table
30	Activating Compound
817	AA Sequence
24	Application
1	CAS Registry Number
80	Cloned(Commentary)
11	Cofactor
4	Crystallization (Commentary)
11	General Information
22	General Stability
212	IC50 Value
348	Inhibitors
7	kcat/KM [mM/s]
37	Ki Value [mM]
338	KM Value [mM]
8	Localization
43	Metals/Ions
31	Molecular Weight [Da]
31	Natural Substrates/ Products (Substrates)
186	Organism
2	Pathway
33	PDB ID
76	pH Optimum
17	pH Range
2	pH Stability
6	pI Value
185	Protein Variants
56	Purification (Commentary)
1	Reaction
11	Reaction Type
181	Reference
2	Renatured (Commentary)
23	Source Tissue
25	Specific Activity [micromol/min/mg]
7	Storage Stability
222	Substrates and Products (Substrate)
16	Subunits
164	Synonyms
1	Systematic Name
52	Temperature Optimum [°C]
5	Temperature Range [°C]
56	Temperature Stability [°C]
52	Turnover Number [1/s]

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in the presence of the DnaKJE chaperone system thermally inactivated monomeric bacterial luciferase refolds. Monomeric bacterial luciferase thermally inactivated in the presence of ATPindependent trigger factor is not able to refold

Luciola mingrelica

Q26304

744279

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

Photinus pyralis

Q27758

688898