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Information on EC 1.14.14.3 - bacterial luciferase and Organism(s) Aliivibrio fischeri and UniProt Accession P19908
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1.14.14.3 bacterial luciferaseIUBMB Comments
The reaction sequence starts with the incorporation of a molecule of oxygen into reduced FMN bound to the enzyme, forming luciferase peroxyflavin. The peroxyflavin interacts with an aliphatic long-chain aldehyde, producing a highly fluorescent species believed to be luciferase hydroxyflavin. The enzyme is highly specific for reduced FMN and for long-chain aliphatic aldehydes with eight carbons or more. The highest efficiency is achieved with tetradecanal. cf. EC 1.13.12.18, dinoflagellate luciferase.
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The taxonomic range for the selected organisms is: Aliivibrio fischeri
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
luciferase, bacterial luciferase, luxab, luxcdabe, vibrio harveyi luciferase, vibrio fischeri luciferase, aldehyde monooxygenase, gluc luciferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde monooxygenase
-
-
-
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alkanal monooxygenase (FMN)
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-
-
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bacterial luciferase
luciferase
Vibrio fischeri luciferase
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-
-
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bacterial luciferase
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-
-
-
luciferase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
The reaction sequence starts with the incorporation of a molecule of oxygen into reduced FMN bound to the enzyme, forming luciferase peroxyflavin. The peroxyflavin interacts with an aliphatic long-chain aldehyde, producing a highly fluorescent species believed to be luciferase hydroxyflavin. The enzyme is highly specific for reduced FMN and for long-chain aliphatic aldehydes with eight carbons or more. The highest efficiency is achieved with tetradecanal. cf. EC 1.13.12.18, dinoflagellate luciferase.
CAS REGISTRY NUMBER
COMMENTARY
9014-00-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-dodec-2-enal + FMNH2 + O2
(E)-dodec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-tetradec-2-enal + FMNH2 + O2
(E)-tetradec-2-enoate + FMN + H2O + hn
-
-
-
-
?
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
n-decanal + FMNH2 + O2
n-decanoate + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
-
-
light emission at 490 nm
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
-
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, NADPH-specific FMN reductase and luciferase form a complex in vivo, reduction of reductase-bound FMN cofactor by NADPH is reversible, allowing the cellular contents of NADP+ and NADPH as a factor for the regulation of the production of FMNH2 by FRPVh for luciferase bioluminescence, overview
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-
?
additional information
?
-
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aldehydes of chain-length 8 or more required
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-
?
additional information
?
-
-
electrochemical luminescence system using bacterial luciferase, in which one of the substrates, FMNH2, is regenerated by the electrochemical reduction of FMN at a Pt-mesh electrode
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-
?
additional information
?
-
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enzyme accepts unsaturated aldehydes as substrates but light emission drops drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence are much slower, when using unsaturated substrates. As a result the duration of the light emission is doubled
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
-
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, NADPH-specific FMN reductase and luciferase form a complex in vivo, reduction of reductase-bound FMN cofactor by NADPH is reversible, allowing the cellular contents of NADP+ and NADPH as a factor for the regulation of the production of FMNH2 by FRPVh for luciferase bioluminescence, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMNH2
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dodecanamide
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inhibits bacterial luciferase luminescence reaction. By injecting the dodecaneamide into the bacterial luciferase system, the luminescence intensity decreases to about half of the initial intensity
methanol
-
bacterial luciferase luminescence intensity decreases to the steady state depending on the methanol concentration
additional information
-
1-hexanol does not inhibit the enzyme luminescence
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methanol
-
bacterial luciferase luminescence intensity slightly increases during the initial stage of the methanol injection
additional information
-
the enzyme shows enhanced affinity for chaperone DnaK
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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348580, 348585, 348587, 348596, 676010, 689388, 702496, 726677, 726678, 726679, 726764, 728228, 728284, 744492, 745731
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genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
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P19907 i.e. subunit LuxA, P19908 i.e. subunit LuxB
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the recombinant enzyme shows unaffected thermal stability after expression in an Escherichia coli clpA-mutant strain lacking chaperone Hsp100, carbonyl cyanide 3-chlorophenylhydrazone highly decreases the thermal stability of the enzyme in vivo to in vitro level, lack of chaperone ClpB decreases the thermal stability of the recombinant enzyme in vivo
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
longchain alkylresorcinol homologues exhibit a protective effect at micromolar concentrations only, while their millimolar concentrations increase the sensitivity of the model proteins to thermal treatment
-
phosphate stabilizes against inactivation by proteases, heat, urea
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sulfate stabilizes against inactivation by proteases, heat, urea
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in different Escherichia coli strains, which are wild-type, or deficient in gene clpA, clpB, and clpX encoding Hsp chaperones, respectively
-
genes luxA and luxB, expression under the control of a consensus-type promoter, lacUV5, in Escherichia coli, activity declines abruptly upon entry into the stationary growth phase, while the levels of luciferase proteins remian constant, the phenomenon, termed ADLA, i.e. abrupt decline of luciferase activity, is caused by a decrease in the availability of flavin mononucleotide
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
heterodimeric bacterial luciferase thermally inactivated in the presence of ATPindependent trigger factor is able to refold. In the presence of the DnaKJE chaperone system thermally inactivated heterodimeric bacterial luciferase also refolds
quick refolding within several min at room temperature or 25°C of thermoinactivated enzyme requires ATP and the DnaK-DnaJ-GrpE-system encoding the Hsp70 chaperone but is independent of chaperone ClpA, 80% activity after reactivation, refolding depends on the Escherichia coli strain used for recombinant expression of the luciferase, overview
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the functional activity of heat-inactivated enzyme is restored by micromolar concentrations of shortchain alkylresorcinols, while longchain homologues inhibit refolding over a wide concentration range. The preincubation of bacterial cells with longchain alkylresorcinols leads to the dose-dependent stimulation of heat shock protein synthesis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
biotechnology
-
the enzyme and cyanine fluorescent protein are useful dual reporters for the quantitative analysis of the effects of n-dodecyltrimethylammonium bromide on whole cells and intracellular proteins of Pseudomonas putida
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Angell, P.; Langley, D.; Chamberlain, A.H.L.
Localization of luciferase in luminous marine bacteria by gold immunocytochemical labelling
FEMS Microbiol. Lett.
65
177-182
1989
Aliivibrio fischeri, Vibrio harveyi
-
Baldwin, T.O.; Holzman, T.F.; Holzman, R.B.; Riddle, V.A.
Purification of bacterial luciferase by affinity methods
Methods Enzymol.
133
98-108
1986
Aliivibrio fischeri, Photobacterium phosphoreum, Vibrio harveyi
Viswanathan, T.S.; Campling, M.R.; Cushley, R.J.
Interactions of long-chain aldehydes with luciferase. A carbon-13 nuclear magnetic resonance study
Biochemistry
18
2504-2508
1979
Aliivibrio fischeri
Hastings, J.W.; Baldwin, T.O.; Nicoli, M.Z.
Bacterial luciferase: Assay, purification, and properties
Methods Enzymol.
57
135-152
1978
Aliivibrio fischeri, Photobacterium phosphoreum, Vibrio harveyi
-
Hastings, J.W.
Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde
CRC Crit. Rev. Biochem.
5
163-184
1978
Aliivibrio fischeri, Photobacterium leiognathi, Vibrio harveyi
Becvar, J.E.; Tu, S.C.; Hastings, J.W.
Activity and stability of the luciferase-flavin intermediate
Biochemistry
17
1807-1812
1978
Aliivibrio fischeri, Vibrio harveyi
Friedland, J.; Hastings, J.W.
The reversibility of the denaturation of bacterial luciferase
Biochemistry
6
2893-2900
1967
Aliivibrio fischeri
Zavilgelsky, G.B.; Kotova, V.Y.; Mazhul, M.M.; Manukhov, I.V.
Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB) chaperones in refolding and increased thermal stability of bacterial luciferases in Escherichia coli cells
Biochemistry (Moscow)
67
986-992
2002
Aliivibrio fischeri, Photorhabdus luminescens
Koga, K.; Harada, T.; Shimizu, H.; Tanaka, K.
Bacterial luciferase activity and the intracellular redox pool in Escherichia coli
Mol. Genet. Genomics
274
180-188
2005
Aliivibrio fischeri
Tu, S.C.
Activity coupling and complex formation between bacterial luciferase and flavin reductases
Photochem. Photobiol. Sci.
7
183-188
2008
Aliivibrio fischeri, Vibrio harveyi
Yamasaki, S.; Nakashima, S.; Yamada, S.; Takehara, K.
Steady-state bioluminescence of bacterial luciferase using electrochemical regeneration of flavin substrate and its application to inhibitory analysis
Bioelectrochemistry
75
67-70
2009
Aliivibrio fischeri
Waidmann, M.; Bleichrodt, F.; Laslo, T.; Riedel, C.
Bacterial luciferase reporters: the swiss army knife of molecular biology
Bioeng. Bugs
2
8-16
2011
Aliivibrio fischeri, Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio harveyi, Photorhabdus laumondii subsp. laumondii, Photorhabdus laumondii subsp. laumondii TT01, Photobacterium phosphoreum ATCC 11040, Photobacterium leiognathi ATCC 25521, Vibrio harveyi ATCC BAA1116
Yamasaki, S.; Yamada, S.; Takehara, K.
Inhibition of electrochemically controlled bioluminescence of bacterial luciferase by n-alkyl alcohols
Anal. Sci.
27
357
2011
Aliivibrio fischeri
Kawanami, Y.; Yamasaki, S.; Yamada, S.; Takehara, K.
Immobilization of bacterial luciferase into poly(N-isopropylacrylamide) film for electrochemical control of a bioluminescence reaction
Anal. Sci.
28
1013-1015
2012
Aliivibrio fischeri
Yamasaki, S.; Yamada, S.; Takehara, K.
Bioluminescence inhibition of bacterial luciferase by aliphatic alcohol, amine and carboxylic acid: inhibition potency and mechanism
Anal. Sci.
29
41-46
2013
Aliivibrio fischeri
Zhang, C.; Su, F.Y.; Zhang, J.F.; Yan, S.T.; Xing, X.H.
Luciferase and fluorescent protein as dual reporters analyzing the effect of n-dodecyltrimethylammonium bromide on the physiology of Pseudomonas putida
Appl. Microbiol. Biotechnol.
93
393-400
2012
Aliivibrio fischeri
Tehrani, G.A.; Mirzaahmadi, S.; Bandehpour, M.; Kazemi, B.
Coexpression of luxA and luxB genes of Vibrio fischeri in NIH3T3 mammalian cells and evaluation of its bioluminescence activities
Luminescence
29
13-19
2014
Aliivibrio fischeri
Melkina, O.; Goryanin, I.; Manukhov, I.; Zavilgelskii, G.
Trigger factor-dependent refolding of bacterial luciferases in Escherichia coli: Kinetics, efficiency, and effect of bichaperone system
Mol. Biol.
47
435-439
2013
Aliivibrio fischeri, Photobacterium leiognathi, Photorhabdus luminescens, Vibrio harveyi
-
Melkina, O.E.; Goryanin, I.I.; Manukhov, I.V.; Baranova, A.V.; Kolb, V.A.; Svetlov, M.S.; Zavilgelsky, G.B.
Trigger factor assists the refolding of heterodimeric but not monomeric luciferases
Biochemistry (Moscow)
79
62-68
2014
Photobacterium leiognathi, Photobacterium leiognathi (P07740 and P07739), Vibrio harveyi (P07740 and P07739), Aliivibrio fischeri (P19907 and P19908), Aliivibrio fischeri MJ-1 (P19907 and P19908)
Brodl, E.; Ivkovic, J.; Tabib, C.R.; Breinbauer, R.; Macheroux, P.
Synthesis of alpha,beta-unsaturated aldehydes as potential substrates for bacterial luciferases
Bioorg. Med. Chem.
25
1487-1495
2017
Aliivibrio fischeri, Photobacterium leiognathi, Vibrio harveyi, Vibrio harveyi ATCC 14126, Aliivibrio fischeri ATCC 7744
Deryabin, D.; Gryazeva, I.; Davydova, O.; El-Registan, G.
Effect of alkylresorcinols on thermal denaturation and refolding of bacterial luciferase and synthesis of heat shock proteins revealed in the luminescent molecular and cellular test systems
Mikrobiologiia
83
640-652
2014
Aliivibrio fischeri, Photobacterium leiognathi
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