1.14.14.3: bacterial luciferase
This is an abbreviated version!
For detailed information about bacterial luciferase, go to the full flat file.
Word Map on EC 1.14.14.3
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1.14.14.3
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metastasis
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transwell
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bioluminescence
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chromatin
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lncrnas
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sponge
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tumorigenesis
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endothelial
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3\'utr
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transactivation
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firefly
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3'-untranslated
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necrosis
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agonist
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tnf
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prostate
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estrogen
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sp1
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luminescence
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nude
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nf-kappab
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5'-flanking
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epithelial-mesenchymal
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co-transfection
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cyclin
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glioma
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nsclc
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emsas
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ovarian
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carcinogenesis
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mapks
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pull-down
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hypoxia-inducible
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osteoblast
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erk
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non-small
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bcl-2
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adenovirus
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osteosarcoma
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chemoresistance
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stat3
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pten
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c-jun
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tunel
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e-cadherin
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cardiomyocytes
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transcription-quantitative
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runx2
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osteogenic
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homeobox
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biotechnology
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agriculture
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diagnostics
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medicine
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molecular biology
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analysis
- 1.14.14.3
- metastasis
-
transwell
-
bioluminescence
- chromatin
- lncrnas
- sponge
- tumorigenesis
- endothelial
-
3\'utr
-
transactivation
- firefly
-
3'-untranslated
- necrosis
- agonist
- tnf
- prostate
- estrogen
- sp1
-
luminescence
-
nude
- nf-kappab
-
5'-flanking
-
epithelial-mesenchymal
-
co-transfection
- cyclin
- glioma
-
nsclc
-
emsas
- ovarian
- carcinogenesis
- mapks
-
pull-down
-
hypoxia-inducible
- osteoblast
- erk
-
non-small
- bcl-2
- adenovirus
- osteosarcoma
-
chemoresistance
- stat3
- pten
- c-jun
-
tunel
- e-cadherin
- cardiomyocytes
-
transcription-quantitative
- runx2
-
osteogenic
-
homeobox
- biotechnology
- agriculture
- diagnostics
- medicine
- molecular biology
- analysis
Reaction
Synonyms
4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase, aldehyde monooxygenase, alkanal monooxygenase (FMN), bacterial luciferase, COB, Gluc luciferase, HFOOH, luciferase, Lux, LuxA, LuxAB, LuxB, LuxCDABE, LuxF, Vibrio fischeri luciferase, Vibrio harveyi luciferase
ECTree
1.14.14.3 bacterial luciferaseAdvanced search results
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results (Cofactor
Cofactor on EC 1.14.14.3 - bacterial luciferase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
4a-hydroxy-4a,5-dihydroriboflavin-5'-phosphate
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model bioluminescence emitter molecule, binding and fluorescence quantum yield studies, complexed with the enzyme in a 1:1 molcular ratio
additional information
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the 4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase transforms from a low quantum yield IIx to a high quantum yield IIy fluorescent species on exposure to excitation light
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FMN
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presence of two discrete and well-separated intensity decay lifetimes (ca. 1 and 5 ns) and intensity decay heterogeneity, of the neat sample suggests that the endogenous FMN senses a heterogeneous fluorescence quenching microenvironment at the active site of the luciferase. Free FMN in solution (isotropic environment), exhibits a single decay lifetime (5 ns), i.e., no intensity decay heterogeneity. Intensity decay heterogeneity of endogenous FMN is largely preserved in the presence of quinone. Averaged rotational rate of FMN increases with the increasing hydrophobicity of the quinone
FMNH2
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348552, 348579, 657751, 657923, 657927, 657939, 657994, 658495, 671610, 671978, 671985, 698992, 711341
FMNH2
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specific for, low activity with other flavins or flavin analogs
FMNH2
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enzyme is complexed with flavin mononucleotide, enzyme possesses a binding platform for the isoalloxazine ring of flavin, a chromophore whose 7,8-dimethyl benzene plane interacts with the isopropyl chain of alphaVal173, structure-fuction analysis
FMNH2
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reduced FMN, i.e. FMNH2, generated by several species of flavin reductases, is utilized along with a long-chain aliphatic aldehyde and molecular oxygen by luciferase as substrates for the bioluminescence reaction, direct transfer of reduced flavin cofactor and reduced flavin product of reductase to luciferase, overview
FMNH2
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reduced FMN, i.e. FMNH2, generated by several species of flavin reductases, is utilized along with a long-chain aliphatic aldehyde and molecular oxygen by luciferase as substrates for the bioluminescence reaction, direct transfer of reduced flavin cofactor and reduced flavin product of reductase to luciferase, overview
FMNH2
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binds to a mobile loop of 29 amino acids in the luciferase protein, structure and conformation, overview
