Information on EC 1.14.14.3 - alkanal monooxygenase (FMN)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.14.14.3
-
RECOMMENDED NAME
GeneOntology No.
alkanal monooxygenase (FMN)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu
show the reaction diagram
reaction mechanism, Cys106 is essential for stabilization of the reaction intermediate, for consumption of aldehyde substrate, and for activity
-
an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu
show the reaction diagram
reaction mechanism and scheme, cofactor binding
-
an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu
show the reaction diagram
residue Val173 of the alpha-subunit is essential for flavin binding and located in the active site, formation of a C4a-hydroperoxyflavin intermediate
-
an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu
show the reaction diagram
reaction mechanism via 4a-hydroperoxyflavin intermediates II-IV and H2O2 release, overview, catalytically important active site residues of the alpha-subunit are alphaF46, alphaF49, alphaF114, and alphaF117, alphaF46 and alphaF117 also appear to be involved in the binding of reduced flavin substrate
-
an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu
show the reaction diagram
reaction mechanism via 4a-hydroperoxyflavin intermediates II-IV and H2O2 release, alphaE238, alphaA75, and alphaA74 are catalytically important active site residues of the alpha-subunit, structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
The reaction sequence involves incorporation of a molecule of oxygen into reduced FMN, and subsequent reaction with the aldehyde to form an activated FMN.H2O complex, which breaks down with emission of light. The enzyme is highly specific for reduced FMN, and for long-chain aliphatic aldehydes with eight carbons or more.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase
-
-
AhR binding-dependent luciferase
-
-
aldehyde monooxygenase
-
-
-
-
bacterial luciferase
-
-
-
-
bacterial luciferase
-
-
bacterial luciferase
Aliivibrio fischeri ES114
-
-
-
bacterial luciferase
-
-
bacterial luciferase
Photobacterium leiognathi ATCC 25521
-
-
-
bacterial luciferase
-
-
bacterial luciferase
Photobacterium phosphoreum ATCC 11040
-
-
-
bacterial luciferase
-
-
bacterial luciferase
P19839, P19840
-
bacterial luciferase
Photorhabdus luminescens subsp. laumondii TT01
-
-
-
bacterial luciferase
P07740
-
bacterial luciferase
Vibrio harveyi ATCC BAA1116
-
-
-
dioxin-responsive chemical-activated luciferase
-
-
firefly luciferase
-
-
luciferase
-
-
-
-
luciferase
-
-
Vibrio fischeri luciferase
-
-
-
-
Vibrio harveyi luciferase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9014-00-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
formerly Photobacterium fischeri
-
-
Manually annotated by BRENDA team
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
marine bacterium
-
-
Manually annotated by BRENDA team
Aliivibrio fischeri ES114
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
not classified
-
-
Manually annotated by BRENDA team
a gram-positive intracellular pathogen, gene lux
-
-
Manually annotated by BRENDA team
a gram-positive intracellular pathogen, strain EGD, gene lux
-
-
Manually annotated by BRENDA team
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
Photobacterium leiognathi ATCC 25521
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
Photobacterium phosphoreum ATCC 11040
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
gene luxA; genes luxA and luxB
UniProt
Manually annotated by BRENDA team
gene luxB; genes luxA and luxB
UniProt
Manually annotated by BRENDA team
i.e. Photorhabdus luminescens
-
-
Manually annotated by BRENDA team
terrestrial bacterium
-
-
Manually annotated by BRENDA team
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
Photorhabdus luminescens subsp. laumondii TT01
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
formerly Beneckea harveyi
-
-
Manually annotated by BRENDA team
gene luxA-B
-
-
Manually annotated by BRENDA team
gene luxAB
-
-
Manually annotated by BRENDA team
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
luminescent wild-type strains BB7 and BB392 and dark mutant strains, 2 luciferases encoded by genes luxA and luxB
-
-
Manually annotated by BRENDA team
Vibrio harveyi ATCC BAA1116
genes lux A and luxB, of the luxCDABE operon, encoding the alpha and beta subunits of the luciferase
-
-
Manually annotated by BRENDA team
symbiotic bacterium from Kryptophanaron alfredi, flashlight fish
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
bacterial luciferase requires an exogenous source of reduced flavin mononucleotide for bioluminescence activity. There is no stable complex formation between luciferase and oxidoreductases Fre/NfsA from Escherichia coli or Frp from Vibrio harveyi, which are believed to provide reduced flavin for luciferase activity. No difference in the levels of luciferase expression in either the DELTAfre or DELTANsfA strains
physiological function
-
luciferase is the enzyme responsible for light emission in bioluminescent bacteria, it catalyzes the reaction of reduced flavin mononucleotide FMNH2, O2, and an aliphatic aldehyde to yield FMN, the corresponding carboxylic acid, and blue-green light
physiological function
-
the luxCDABE encoded protein products synergistically generate bioluminescent light signals exclusive of supplementary substrate additions or exogenous manipulations
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aldehyde + FMNH2 + O2
?
show the reaction diagram
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
a long chain aliphatic aldehyde as substrate
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
Photobacterium phosphoreum ATCC 11040, Photorhabdus luminescens subsp. laumondii TT01, Photobacterium leiognathi ATCC 25521, Aliivibrio fischeri ES114, Vibrio harveyi ATCC BAA1116
-
-
-
-
?
beetle luciferin + FMNH2 + O2
?
show the reaction diagram
-
-
-
-
ir
coelenterazine + FMNH2 + O2
CO2 + coelenteramide + FMN + light + H2O
show the reaction diagram
-
an imidazolopyrazine derivative
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
?
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
P07740
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
show the reaction diagram
-
formation of a 4a-hydroperoxy-FMN intermediate II
-
-
ir
decanal + FMNH2 + O2
decanoate + FMN + H2O + hv
show the reaction diagram
-
-
-
-
ir
decanal + riboflavin + O2
?
show the reaction diagram
-
riboflavin is a very poor substrate for bacterial luciferase
-
-
?
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
?
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
show the reaction diagram
P07740
-
-
-
?
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
dodecyl aldehyde + FMNH + O2
?
show the reaction diagram
-
-
-
-
?
fatty aldehyde + FMNH2 + O2
fatty acid + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
hexachlorethane + e-
tetrachlorethylene + Cl-
show the reaction diagram
-
-
-
-
?
luciferin + FMNH2 + O2
?
show the reaction diagram
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
myristic aldehyde + FMNH + O2
myristic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
?
n-caprinaldehyde + FMNH2 + O2
n-caprinoate + FMN + H2O + hv
show the reaction diagram
-
-
-
-
ir
n-decanal + FMNH2 + O2
n-decanoate + FMN + H2O + hn
show the reaction diagram
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
nonanal + FMNH2 + O2
nonanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
?
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
show the reaction diagram
P07740
-
-
-
?
octanal + FMNH2 + O2
octanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
pentachlorethane + e-
trichlorethylene + Cl-
show the reaction diagram
-
-
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
long-chain aldehydes
long-chain fatty acids, bioluminescence reaction
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
formation of a 4a-hydroperoxy-FMN intermediate II
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
formation of a C4a-hydroperoxyflavin intermediate
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
show the reaction diagram
-
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
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
undecanal + FMNH2 + O2
undecanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
additional information
?
-
-
aldehydes of chain-length 8 or more required
-
-
-
additional information
?
-
-
complex formation in a 1:1 molar ratio between monomeric, but not dimeric, NADPH:FMN oxidoreductase FRP and luciferase for direct transfer of cofactor FMNH2
-
-
-
additional information
?
-
-
luminescence pathway, overview
-
-
-
additional information
?
-
-
the decay rate of the enzyme is determined by residue Glu175 of the central region of the LuxA subunit, distinction between slow and fast decay luciferases is primarily due to differences in aldehyde affinity and in the decomposition of the luciferase-flavin-oxygen intermediate
-
-
-
additional information
?
-
-
the enzyme plays a role in protection of cells against oxidative stress
-
-
-
additional information
?
-
-
substrate specificities of mutant enzymes and wild-type enzyme, overview
-
-
-
additional information
?
-
-
substrate specificity and quantum yield of mutant E175G as a function of aldehyde chain length
-
-
-
additional information
?
-
-
the Gluc luciferase retains its luminescence output in the stationary phase of growth and exhibits enhanced stability during exposure to low pH, hydrogen peroxide, and high temperature
-
-
-
additional information
?
-
-
Vibrio harveyi NADPH-specific flavin reductase FRP transfers reduced riboflavin-5'-phosphate to luciferase by both free diffusion and direct transfer, resulting inbioluminescence production, FRP:luciferase coupled bioluminescence reaction, overview, increases in oxygen concentration lead to gradual decreases of the peak bioluminescence intensity, Km for FMN, and Km for NADPH of NADPH-specific flavin reductase in the coupled reaction with luciferase
-
-
-
additional information
?
-
-
active site hydrophobicity is critical to the bioluminescence activity of Vibrio harveyi luciferase
-
-
-
additional information
?
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
FMNH2 binds to a mobile loop of 29 amino acids in the luciferase protein, loop modeling of ligand-free and -bound enzyme, conformation and dynamics, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
show the reaction diagram
Photorhabdus luminescens subsp. laumondii, Photobacterium phosphoreum ATCC 11040, Photorhabdus luminescens subsp. laumondii TT01, Photobacterium leiognathi ATCC 25521, Aliivibrio fischeri ES114, Vibrio harveyi ATCC BAA1116
-
-
-
-
?
beetle luciferin + FMNH2 + O2
?
show the reaction diagram
-
-
-
-
ir
coelenterazine + FMNH2 + O2
CO2 + coelenteramide + FMN + light + H2O
show the reaction diagram
-
an imidazolopyrazine derivative
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
show the reaction diagram
-
-
-
-
ir
fatty aldehyde + FMNH2 + O2
fatty acid + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
n-caprinaldehyde + FMNH2 + O2
n-caprinoate + FMN + H2O + hv
show the reaction diagram
-
-
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
show the reaction diagram
-
long-chain aldehydes
long-chain fatty acids, bioluminescence reaction
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
show the reaction diagram
-
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
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
show the reaction diagram
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + CO2 + light
show the reaction diagram
-
-
-
-
ir
additional information
?
-
-
complex formation in a 1:1 molar ratio between monomeric, but not dimeric, NADPH:FMN oxidoreductase FRP and luciferase for direct transfer of cofactor FMNH2
-
-
-
additional information
?
-
-
luminescence pathway, overview
-
-
-
additional information
?
-
-
the decay rate of the enzyme is determined by residue Glu175 of the central region of the LuxA subunit, distinction between slow and fast decay luciferases is primarily due to differences in aldehyde affinity and in the decomposition of the luciferase-flavin-oxygen intermediate
-
-
-
additional information
?
-
-
the enzyme plays a role in protection of cells against oxidative stress
-
-
-
additional information
?
-
-
the Gluc luciferase retains its luminescence output in the stationary phase of growth and exhibits enhanced stability during exposure to low pH, hydrogen peroxide, and high temperature
-
-
-
additional information
?
-
-
Vibrio harveyi NADPH-specific flavin reductase FRP transfers reduced riboflavin-5'-phosphate to luciferase by both free diffusion and direct transfer, resulting inbioluminescence production, FRP:luciferase coupled bioluminescence reaction, overview, increases in oxygen concentration lead to gradual decreases of the peak bioluminescence intensity, Km for FMN, and Km for NADPH of NADPH-specific flavin reductase in the coupled reaction with luciferase
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-deaza-FMNH2
-
can replace FMNH2
2',3'-Diacetyl-FMNH2
-
as substitute for FMNH2
2-Thio-FMNH2
-
as substitute for FMNH2
3'-Carboxymethyl-FMNH2
-
as substitute for FMNH2
-
4a-hydroxy-4a,5-dihydroriboflavin-5'-phosphate
-
model bioluminescence emitter molecule, binding and fluorescence quantum yield studies, complexed with the enzyme in a 1:1 molcular ratio
FMN
-
potassium iodide quenches the fluorescence of FMN
FMN
-
the luminescence reaction is initiated by the reduction of FMN
FMN
-
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
-
specific for, low activity with other flavins or flavin analogs
FMNH2
-
8-substituted FMN-analogs
FMNH2
-
physiological cofactor
FMNH2
-
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
-
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
-
binds to a mobile loop of 29 amino acids in the luciferase protein, structure and conformation, overview
additional information
-
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,3-Dichloro-(6-phenylphenoxy)ethylamine
-
-
2,3-Dichloro-(6-phenylphenoxy)ethylamine
-
-
2,4-Dinitrofluorobenzene
-
i.e. Sanger's reagent
2-Bromodecanal
-
protection by dithiothreitol or mercaptoethanol
2-Diethylaminoethyl-2,2-diphenylvalerate
-
-
2-Diethylaminoethyl-2,2-diphenylvalerate
-
-
2-methyl-1,4-benzoquinone
-
-
2-methyl-5-isopropyl-1,4-benzoquinone
-
-
5-decyl-4a-hydroxy-4a,5-dihydroriboflavin-5'-phosphate
-
binding and fluorescence quantum yield studies of the substance as a model, complexed with the enzyme in a 1:1 molcular ratio leading to 80% and 90% inhibition of wild-type and mutant C106A at 0.01 mM, respectively, binds to the active site
8-Anilino-1-naphthalenesulfonate
-
-
8-Anilino-1-naphthalenesulfonate
-
-
8-Anilino-1-naphthalenesulfonate
-
-
8-Anilino-1-naphthalenesulfonate
-
inhibitor binding site separate from FMN-binding site by 30 A
Aliphatic alcohols
-
-
Aliphatic alkanes
-
-
-
benzylalcohol
-
-
butanoic acid
-
IC50: 13.6 mM
Chloroform
-
-
Decanoic acid
-
IC50: 0.0132 mM
diethylether
-
-
diethylether
-
-
dodecanamide
-
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
dodecanoic acid
-
IC50: 0.0012 mM
hexadecanoic acid
-
IC50: 0.00067 mM
Hexanoic acid
-
IC50: 3.4 mM
iodoacetamide
-
-
Isoflurane
-
-
methanol
-
bacterial luciferase luminescence intensity decreases to the steady state depending on the methanol concentration
Methoxyflurane
-
-
N,N-Diethyl-2,4-dichloro-(6-phenylphenoxy)ethylamine
-
-
n-decanal
-
reversible substrate inhibition, depending on phosphate concentration
N-ethylmaleimide
-
protection by substrates
octadecanoic
-
IC50: 0.00063 mM
-
Octanoic acid
-
IC50: 2.9 mM
Paraldehyde
-
-
potassium iodide
-
quenches the fluorescence of FMN effectively at 0.2 M, and enhances the decay of wild-type and HFOOH enzymes, the wild-type enzyme forms an inactive complex with KI
Proteases
-
trypsin, chymotrypsin
-
reduced riboflavin
-
-
tetradecanoic acid
-
IC50: 0.00068 mM
Urea
-
denaturation curve, thermodynamics, wild-type and mutants, overview
Methoxyflurane
-
-
additional information
-
luxA mutant and luxB mutant strains are more sensitive to oxidants like H2O2, cumene hydroperoxide, tert-butyl hydroperoxide, or ferrous sulfate, than the wild-type strain, growth behaviour overview
-
additional information
-
increases in oxygen concentration lead to gradual decreases of the peak bioluminescence intensity, Km for FMN, and Km for NADPH of NADPH-specific flavin reductase in the coupled reaction with luciferase
-
additional information
-
hydrophobicity of the quinone plays a role in the non-specific inhibition mechanism of xenobiotic molecules in the bacterial bioluminescence system via altering the rotational mobility of the endogenous flavin in the luciferase. Added quinone reduces the averaged binding affinity of the endogenous FMN to the active site of luciferase by increasing the fraction of the weak FMN binding sites of luciferase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-fluoroethylamine
-
alphaH44A mutant, works as catalytic base
ammonia
-
alphaH44A mutant, works as catalytic base
cyanomethylamine
-
alphaH44A mutant, works as catalytic base
ethanolamine
-
alphaH44A mutant, works as catalytic base
ethylamine
-
alphaH44A mutant, works as catalytic base
halogenated aromatic hydrocarbons
-
stable aryl hydrocarbon receptor ligands from crude extracts of environmental samples, that activate the enzyme, detailed overview
-
imidazole
-
alphaH44A mutant, works as catalytic base
methanol
-
bacterial luciferase luminescence intensity slightly increases during the initial stage of the methanol injection
omega-carboxypentylflavin
-
as substitute for FMNH2
polyaromatic hydrocarbons
-
labile aryl hydrocarbon receptor ligands from crude extracts of environmental samples, that activate the enzyme, detailed overview
-
Propylamine
-
alphaH44A mutant, works as catalytic base
Sodium acetate
-
activates mutant E328A
Methylamine
-
alphaH44A mutant, works as catalytic base
additional information
-
the enzyme shows enhanced affinity for chaperone DnaK
-
additional information
-
the enzyme shows enhanced affinity for chaperone ClpA
-
additional information
-
the enzyme is a dioxin-responsive chemical-activated luciferase
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
0.01
aldehydes
-
-
0.0003
-
decanal
-
wild type, 50 mM phosphate
0.0004
-
decanal
-
recombinant mutant alphaF261S, pH 7.0, 25C; recombinant mutant alphaG275I, pH 7.0, 25C
0.001
-
decanal
-
recombinant wild-type enzyme, pH 7.0, 25C
0.00101
-
decanal
-
pH 7.0, 23C, recombinant mutant F49Y
0.0013
-
decanal
-
pH 7.0, 23C, recombinant mutant F46A
0.0016
-
decanal
-
recombinant mutant alphaF261Y, pH 7.0, 25C
0.0016
-
decanal
-
pH 7.0, 23C, recombinant wild-type enzyme
0.0016
-
decanal
-
pH 7.0, 23C, recombinant wild-type enzyme and mutant A74G
0.0017
-
decanal
-
recombinant mutant alphaF261A, pH 7.0, 25C
0.0018
-
decanal
-
recombinant mutant alphaG275P, pH 7.0, 25C
0.0021
-
decanal
-
alphaR107S, 50 mM phosphate
0.0022
-
decanal
-
alphaR107E, 50 mM phosphate
0.0022
-
decanal
-
recombinant mutant alphaG275A, pH 7.0, 25C
0.0023
-
decanal
-
pH 7.0, 23C, recombinant mutant E328Q
0.0024
-
decanal
-
pH 7.0, 23C, recombinant mutant F117S; pH 7.0, 23C, recombinant mutant F46Y
0.0026
-
decanal
-
pH 7.0, 23C, recombinant mutant F46S
0.0027
-
decanal
-
recombinant mutant alphaG275F, pH 7.0, 25C
0.0027
-
decanal
-
pH 7.0, 23C, recombinant mutant F114Y
0.003
-
decanal
-
pH 7.0, 23C, recombinant mutants F49D, F117A, and F49A
0.0031
-
decanal
-
alphaR107A, 50 mM phosphate
0.0031
-
decanal
-
pH 7.0, 23C, recombinant mutant F117D
0.0032
-
decanal
-
pH 7.0, 23C, recombinant mutant F46D
0.0033
-
decanal
-
pH 7.0, 23C, recombinant mutant F49S
0.0033
-
decanal
-
pH 7.0, 23C, recombinant mutant E328A
0.0037
-
decanal
-
recombinant mutant alphaG284P, pH 7.0, 25C
0.0045
-
decanal
-
pH 7.0, 23C, recombinant mutant E328F
0.0046
-
decanal
-
recombinant mutant alphaF261D, pH 7.0, 25C
0.005
-
decanal
-
pH 7.0, 23C, recombinant mutant E328D
0.0051
-
decanal
-
pH 7.0, 23C, recombinant mutant F117Y
0.0073
-
decanal
-
pH 7.0, 23C, recombinant mutant F114D
0.008
-
decanal
-
wild-type
0.0083
-
decanal
-
pH 7.0, 23C, recombinant mutant F114S
0.0093
-
decanal
-
pH 7.0, 23C, recombinant mutant F114A
0.0095
-
decanal
-
pH 7.0, 23C, recombinant mutant E328H
0.0097
-
decanal
-
pH 7.0, 23C, recombinant mutant E328L
0.01
-
decanal
-
mutant K286A
0.0105
-
decanal
-
mutant K283A
0.0173
-
decanal
-
pH 7.0, 23C, recombinant mutant A74F
0.0009
-
FMN
-
in the presence of different flavin concentrations, 0.001 mM Fre oxidoreductase, 10 mM decanal, and 0.01 mM NADPH and 0.005 mM luciferase
0.00015
-
FMNH
-
alpha subunit
0.0004
0.0008
FMNH
-
-
0.0004
0.0008
FMNH
-
-
0.00058
-
FMNH
-
beta subunit
0.0008
-
FMNH
-
wild type, 10 mM phosphate
0.0018
-
FMNH
-
wild type, 300 mM phosphate
0.0038
-
FMNH
-
alphaR107S, 10 mM phosphate
0.0049
-
FMNH
-
alphaR107S, 300 mM phosphate
0.0081
-
FMNH
-
alphaR107A, 10 mM phosphate
0.0095
-
FMNH
-
alphaR107A, 300 mM phosphate
0.0114
-
FMNH
-
alphaR107E, 300 mM phosphate
0.0234
-
FMNH
-
alphaR107E, 10 mM phosphate
0.0002
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F114S
0.0002
-
FMNH2
-
pH 7.0, 23C, recombinant mutants E328Q and E328H
0.0003
-
FMNH2
-
recombinant wild-type enzyme, pH 7.0, 25C
0.0003
-
FMNH2
-
pH 7.0, 23C, recombinant mutants F46Y, F114A, F117Y, and F114Y
0.0003
-
FMNH2
-
pH 7.0, 23C, recombinant mutants E328L and E328A
0.0004
-
FMNH2
-
pH 7.0, 23C, recombinant mutant E328D
0.0006
-
FMNH2
-
recombinant mutant alphaG284P, pH 7.0, 25C
0.0006
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F49Y; pH 7.0, 23C, recombinant wild-type enzyme
0.0006
-
FMNH2
-
pH 7.0, 23C, recombinant wild-type enzyme
0.0007
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F49S
0.001
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F114D
0.0013
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F117S; pH 7.0, 23C, recombinant mutant F49D
0.0015
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F117A
0.0015
-
FMNH2
-
pH 7.0, 23C, recombinant mutant A74G
0.0022
-
FMNH2
-
recombinant mutant alphaG275P, pH 7.0, 25C
0.0027
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F49A
0.0039
-
FMNH2
-
pH 7.0, 23C, recombinant mutant E328F
0.0043
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F46S
0.0075
-
FMNH2
-
recombinant mutant alphaF261D, pH 7.0, 25C
0.0087
-
FMNH2
-
pH 7.0, 23C, recombinant mutant A74F
0.0123
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F46A
0.0148
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F46D
0.0192
-
FMNH2
-
recombinant mutant alphaF261Y, pH 7.0, 25C
0.0281
-
FMNH2
-
recombinant mutant alphaF261A, pH 7.0, 25C
0.0358
-
FMNH2
-
recombinant mutant alphaG275A, pH 7.0, 25C
0.0369
-
FMNH2
-
recombinant mutant alphaF261S, pH 7.0, 25C
0.0411
-
FMNH2
-
recombinant mutant alphaG275F, pH 7.0, 25C
0.052
-
FMNH2
-
pH 7.0, 23C, recombinant mutant F117D
0.0012
0.009
n-decanal
-
depending on buffer system
0.0001
-
O2
-
-
0.0013
-
riboflavin
-
in the presence of different flavin concentrations, 0.001 mM Fre oxidoreductase, 10 mM decanal, and 0.01 mM NADPH and 0.005 mM luciferase
0.0584
-
FMNH2
-
recombinant mutant alphaG275I, pH 7.0, 25C
additional information
-
additional information
-
stopped flow spectroscopy
-
additional information
-
additional information
-
detailed reaction and folding kinetics, thermodynamics
-
additional information
-
additional information
-
kinetics, substrate and cofactor binding
-
additional information
-
additional information
-
enzyme activities in complex formation, kinetics, dissociation constants
-
additional information
-
additional information
-
affinity and dissociation constants for FMNH2 of wild-type and mutants enzymes, kinetics
-
additional information
-
additional information
-
kinetics of the FRP:luciferase coupled bioluminescence reaction
-
additional information
-
additional information
-
stopped-flow kinetics of wild-type and mutant enzymes
-
additional information
-
additional information
-
stopped-flow and Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
-
additional information
-
time-course changes of mixture effects on AhR binding-dependent luciferase activity in a crude extract from a compost sample
-
additional information
-
additional information
-
kinetics of FMN reductase-luciferase complex formation, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5e-05
-
FMNH
-
myristic aldehyde as second substrate
2.5e-05
-
FMNH
-
dodecanoic aldehyde as second substrate
3.17e-05
-
FMNH
-
decanoic aldehyde as second substrate
0.1
-
FMNH2
-
purified enzyme
additional information
-
additional information
-
tetradecanal + FMNH + O2 (possibly) turnover rate determined by measuring the half-time for decay of luminescence between 70% and 35% of the maximum intensity, values depending on chain-length of aldehyde
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
slow turnover rate
-
additional information
-
additional information
-
single turnover, luminescence
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13.6
-
butanoic acid
-
IC50: 13.6 mM
0.0132
-
Decanoic acid
-
IC50: 0.0132 mM
0.0012
-
dodecanoic acid
-
IC50: 0.0012 mM
0.00067
-
hexadecanoic acid
-
IC50: 0.00067 mM
3.4
-
Hexanoic acid
-
IC50: 3.4 mM
0.00063
-
octadecanoic
-
IC50: 0.00063 mM
-
2.9
-
Octanoic acid
-
IC50: 2.9 mM
0.00068
-
tetradecanoic acid
-
IC50: 0.00068 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.105
-
-
substrate tetradecanal, uncoupled enzyme
additional information
-
-
substrate specificity
additional information
-
-
luminescence activity and decay of wild-type and mutants with different aldehyde substrates
additional information
-
-
quantum yield of wild-type and mutant enzymes, overview
additional information
-
-
light and dark quantum yield of wild-type and mutant enzymes, overview
additional information
-
-
measuring luminescence of recombinant luciferase in transfected Leishmania amazonensis amostigotes
additional information
-
-
development of a quantitative and highly sensitive luciferase-based assay for antiviral toxins, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
-
optimum for reaction velocity
6.5
-
-
optimum for binding of FMNH2
7
-
-
assay at
8.1
-
-
optimum for quantum yield
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
additional information
-
-
temperature dependence of thermodynamic parameters
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
gene expression kit of dioxin-responsive chemical-activated luciferase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75430
-
-
wild-type enzyme, analytical ultracentrifugation
76360
-
-
mutant beta-H82A, analytical ultracentrifugation
76740
-
-
mutant beta-H81A, analytical ultracentrifugation
76750
-
-
mutant beta-H81A/E89D, analytical ultracentrifugation
76860
-
-
mutant alpha-A81H, analytical ultracentrifugation
77000
78000
-
gel filtration
77000
78000
-
-
77000
78000
-
nucleotide sequence data
84000
-
-
renatured enzyme, osmometry
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
heterodimer
dimer
-
alphabeta heterodimer containing a single active site at a cleft in the alpha subunit
dimer
-
alphabeta heterodimer, structure-function relationship, overview
heterodimer
-
alphabeta, 1 * 41389 + 1 * 37112, nucleotide sequence
heterodimer
-
alphabeta, 1 * 40108 + 1 * 36349 nucleotide sequence
heterodimer
-
alpha-subunit, encoded by the luxA gene, and beta-subunit, encoded by the luxB gene
heterodimer
Photobacterium phosphoreum ATCC 11040
-
alpha-subunit, encoded by the luxA gene, and beta-subunit, encoded by the luxB gene
-
monomer
-
1 * 78000, produced by gene fusion of luxA and luxB genes
additional information
-
functional roles of conserved residues in the protease-labile, unstructured loop of the alpha-subunit, formed by residues 257-291, the loop undergoed conformational changes during catalysis, overview
additional information
-
analysis of subunit interface structure and role in the conformational stability of the heterodimeric enzyme, the beta-sunbunit can self-associate to form a stable but inactive homodimer, unfolding in a four-state mechanism
additional information
-
structure-function relationship, roles of Cys106, Ala75, Ala74, and the isoalloxazine ring of FMN
additional information
-
luciferase is composed of two homologous subunits designated alpha and beta, both of which assume the TIM barrel fold. Although the beta-subunit is required for activity, the catalytic site resides exclusively on the alpha-subunit. The most substantial compositional difference between subunits corresponds to a highly conserved stretch of residues between positions 260 and 290 unique to the alpha chains of luminous bacteria. In the luciferase/FMN complex, the asymmetric unit contains two beta/alpha-heterodimers
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bacterial luciferase/FMN complex, by the hanging drop method, at 2.3 A resolution. Crystals of recombinant luciferase are grown at room temperature prior to soaking with millimolar concentrations of FMN. Belongs to space group P212121. The isoalloxazine ring is coordinated by an unusual cis-Ala-Ala peptide bond. The reactive sulfhydryl group of Cys106 projects toward position C-4a, the site of flavin oxygenation. Mobile loop that is crystallographically disordered, appears to be a boundary between solvent and the active center. Within this portion of the protein, there is a single contact between Phe272 of the R subunit and Tyr151 of the beta subunit
P07740
structure is determined in absence of substrate at low-salt concentrations
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
the enzyme exhibits enhanced stability during exposure to low pH, hydrogen peroxide, and high temperature
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
stable below
37
-
-
comparison of stability of wild-type enzyme and gene-fusion monomeric enzyme
37
-
P07740
wild-type enzyme has a 90% reduction in activity after 92 min. Comparable loss for the Y151W mutant after only 11 min
40
-
-
wild-type enzyme and mutanbt A75G: loss of 60% activity within 50 min, mutants C106V and C106V/A75G show increased thermolability loosing 99% and 90% activity, respectively
43.5
-
-
inactivation, temperature-labile enzyme
43.5
-
-
inactivation in vitro, temperature-stable enzyme
45
-
-
half-life over 3 h
45
-
-
half-life 5 min
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
additional information
-
-
the recombinant enzyme shows reduced thermal stability in absence of chaperone Hsp100 after expression in an Escherichia coli clpA-mutant strain, lack of chaperone ClpB decreases the thermal stability of the recombinant enzyme in vivo
additional information
-
-
the enzyme exhibits enhanced stability during exposure to low pH, hydrogen peroxide, and high temperature
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
citrate stabilizes against inactivation by proteases, heat, urea
-
diphosphate stabilizes against inactivation by proteases, heat, urea
-
inactivation by lyophilization
-
labile to proteases
-
no inactivation by repeated freezing/thawing
-
phosphate stabilizes against inactivation by proteases, heat, urea
-
sulfate stabilizes against inactivation by proteases, heat, urea
-
phosphate stabilizes against inactivation by proteases, heat, urea
-
sulfate stabilizes against inactivation by proteases, heat, urea
-
citrate stabilizes against inactivation by proteases, heat, urea
-
diphosphate stabilizes against inactivation by proteases, heat, urea
-
inactivation by lyophilization
-
labile to proteases
-
no inactivation by repeated freezing/thawing
-
phosphate stabilizes against inactivation by proteases, heat, urea
-
sulfate stabilizes against inactivation by proteases, heat, urea
-
the wild-type enzyme belongs to the group of luciferases with slow decay, mutant E175G is turned into a luciferase with fast decay, the decay rate of the enzyme is determined by residue Glu175
-
citrate stabilizes against inactivation by proteases, heat, urea
-
diphosphate stabilizes against inactivation by proteases, heat, urea
-
inactivation by lyophilization
-
labile to proteases
-
no inactivation by repeated freezing/thawing
-
phosphate stabilizes against inactivation by proteases, heat, urea
-
repeated freezing/thawing causes inactivation of immobilized enzyme
-
sulfate stabilizes against inactivation by proteases, heat, urea
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme exhibits enhanced stability during exposure to low pH, hydrogen peroxide, and high temperature
-
671414
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50 mM potassium phosphate buffer, pH 7.0, protein concentration 1 mg/ml , -20C, 0.1 M phosphate buffer, pH 7, 0.1 mM dithiothreitol, 1 mM EDTA
-
-20C, 50 mM potassium phosphate buffer, pH 7.0, protein concentration 1 mg/ml , -20C, 0.1 M phosphate buffer, pH 7, 0.1 mM dithiothreitol, 1 mM EDTA
-
-20C, phosphate buffer
-
-80C, 0.5 mM dithiothreitol
-
0-4C, immobilized enzyme, 0.1 mM dithiothreitol, 20% loss of activity in 3 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity methods
-
recombinant enzyme from Escherichia coli
-
recombinant enzyme from Escherichia coli
-
affinity methods
-
nickel affinity column
-
on a nickel affinity column, to more than 90% purity
P07740
on nickel affinity column, to more than 90% purity
-
preparation of enzyme with modified subunits
-
preparation of subunits
-
recombinant enzyme from Escherichia coli strain JM101 to over 95% purity
-
recombinant wild-type and mutant C106A enzymes from Escherichia coli strain JM101 to over 95% purity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM101 to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 to over 85% homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
luxCDABE operon, genetic organization, overview
-
gene Gluc, expression in Mycobacterium smegmatis using an hsp60 promoter, subcloning in Escherichia coli strain DH5alpha
-
expression analysis, cloning into expression vector pPL2lux useable as a reporter system based on the luciferase activity of the enzyme, overview
-
gene lux, improvement of a tagging system for luciferase by construction of a highly active, constitutive promoter resulting in a 100fold higher recombinant activity compared to native activity
-
overexpression 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
-
expression in transfected Leishmania amazonensis strain LV79 amastigotes, transfection by electroporation
-
luxCDABE operon, genetic organization, overview
-
expression of fused luxA and luxB genes and also luxF gene in Escherichia coli and Nicotiana plumbaginifolia
-
luxCDABE operon, genetic organization, overview
-
expression in different Escherichia coli strains, which are wild-type, or deficient in gene clpA, clpB, and clpX encoding Hsp chaperones, respectively
-
expression in Escherichia coli
-
expression of fused luxA and luxB genes in Escherichia coli
-
expression of wild-type and randomly generated mutants in Escherichia coli strain BL21
-
stable expression, using a bicistronic expression vector, of wild type luxA and luxB, WTA/WTB, codon-optimized luxA and wild type luxB, COA/WTB, and codon-optimized versions of both luxA and luxB genes, COA/COB, in HEK-293 cells, expression analysis, method evaluation and optimization, highest bioluminescence by expression of both codon-optimized genes, overview; stable expression, using a bicistronic expression vector, of wild type luxA and luxB, WTA/WTB, codon-optimized luxA and wild type luxB, COA/WTB, and codon-optimized versions of both luxA and luxB genes, COA/COB, in HEK-293 cells, expression analysis, method evaluation and optimization, highest bioluminescence by expression of both codon-optimized genes, overview
P19839, P19840
luxCDABE operon, genetic organization, overview
-
expression of fused luxA and luxB genes in Escherichia coli
-
amplified from the pJHD500 plasmid and ligated into a pET21b vector, expressed from pZCH2 in an Escherichia coli BL21 (lambdaDE3) cell line after growth to an OD600 of 0.5
P07740
coexpression of luciferase and cytochrome P-450; expression in Pseudomonas putida
-
expressed in Escherichia coli from pJHD500, ligated into a pET21b vector. Luciferase subcloned from pZCH2 into a pASKIBA-3c vector with the restriction sites XbaI and XhoI. The resulting luciferase containing a strep-II tag on the C terminus of the beta-subunit (pZCB4) expressed
-
expression in Escherichia coli strain JM101
-
expression of fused luxA and luxB genes in Saccharomyces cerevisiae, Bacillus subtilis, plant cells, plasmid expression vector and in Escherichia coli
-
expression of luxA gene in Escherichia coli
-
expression of seperated luxA and luxB gene in Escherichia coli JM109
-
expression of the enzyme in Mycobacterium tuberculosis under control of the inducible/repressible promotor of the alanine dehydrogenase from Mycobacterium tuberculosis strain H37Rv, usage of a mycobacterial-Escherichia coli shuttle vector
-
expression of wild-type and mutant C106A enzymes in Escherichia coli strain JM101
-
expression of wild-type and mutant enzymes in Escherichia coli
-
gene luxA, expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
gene luxAB, expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
gene luxAB, functional coexpression in Saccharomyces cerevisiae with NADPH-specific FMN reductase FRP from Vibrio harveyi, subcloning in Escherichia coli
-
ligated into pET21-b vector, expressed from pZCH2 in Escherichia coli BL21 (lambdaDE3) cell line
-
luxCDABE operon, genetic organization, overview
-
overexpression of mutant in XL1 blue MRF' cell line
-
overexpression of wild-type and mutant enzymes in Escherichia coli strain JM101
-
the bacterial luciferase lux gene cassette consists of five genes, luxCDABE. The lux operon is re-synthesized through a process of multibicistronic, codon-optimization to demonstrate self-directed bioluminescence emission in a mammalian HEK-293 cell line in vitro and in vivo, overview. To overcome the limitations by FMNH2 supply, co-expression of a constitutively expressed flavin reductase gene frp from Vibrio harveyi is performed leading to a 151fold increased increase in bioluminescence in cells expressing mammalian codon-optimized luxCDE and frp genes
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D232G
-
random mutagenesis, 63% of wild-type luminescence activity
E175G
-
random mutagenesis, the single point mutation leads to increased decay rate of the enzyme, 0.9% of wild-type luminescence activity
E175G/N199D
-
random mutagenesis, 0.1% of wild-type luminescence activity
K202R
-
random mutagenesis, 95% of wild-type luminescence activity
M190T
-
random mutagenesis, 29% of wild-type luminescence activity
T198S
-
random mutagenesis, 84% of wild-type luminescence activity
A74F
-
site-directed mutagenesis, the mutant shows reduced activity and increased Km compared to the wild-type enzyme
A74G
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
A75G
-
site-directed mutagenesis, activity similar to the wild-type enzyme
A75G/C106V/V173A
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A75G/C106V/V173C
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A75G/C106V/V173S
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A75G/C106V/V173T
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A81H
-
site-directed mutagenesis, residue of the alpha-subunit, mutant shows 13% of wild-type activity
alphaDELTA262-290beta
-
four times higher affinity for FMN than wild type
alphaF114A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF114D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF114S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF114Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF117A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF117D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF117S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF117Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF327A
-
site-directed mutagenesis, mutant activity is similar to the wild-type enzyme
alphaF46A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF46D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF46S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF46Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF49A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF49D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF49S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF49Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF6A
-
site-directed mutagenesis, mutant activity is similar to the wild-type enzyme
alphaH44A
-
decreased bioluminescence
alphaH44A
-
rapid decay of the 4a-hydroperoxy-4a,5-dihydroFMN intermediate enzyme, HFOOH, in the mutant
alphaR107A
-
lower affinity for FMNH
alphaR107E
-
lower affinity for FMNH
alphaR107S
-
lower affinity for FMNH
C106A
-
site-directed mutagenesis, catalytic properties are similar to the wild-type enzyme, mutant shows 60% of wild-type quantum yield
C106V
-
site-directed mutagenesis, highly reduced ability to stabilize the reaction intermediate due to interaction between Val106 and Ala75 side chains, and therefore highly reduced activity and increased thermal lability compared to the wild-type enzyme
C106V/A75G
-
site-directed mutagenesis, mutation of Ala75 restores about 90% of the activity abolished by mutation of Cys106, shift in the light emission spectrum to that of Photobacterium phosphoreum possessing Val and Gly at positions 106 and 75, respectively
D262A
-
90% reduced activity with octanal, 36% reduced activity with decanal, activity with dodecanal as the wild-type
D265A
-
activity with octanal as the wild-type, 81% reduced activity with decanal, complete loss of dodecanal activity
D271A
-
complete loss of octanal and decanal activity, 18% reduced activity with dodecanal
E328A
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme, the activity is rescued by addition of sodium acetate, but not by phosphate, at pH 6.0-8.0 with increasing activity at lower pH
E328D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
E328F
-
site-directed mutagenesis, the mutant shows reduced activity and increased Km compared to the wild-type enzyme
E328H
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
E328L
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
E328Q
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
F261A
-
site-directed mutagenesis, residue of the alpha-subunit, 0.19% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
F261D
-
site-directed mutagenesis, residue of the alpha-subunit, 0.004% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
F261S
-
site-directed mutagenesis, residue of the alpha-subunit, 0.13% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
F261Y
-
site-directed mutagenesis, residue of the alpha-subunit, 2-3% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
G275A
-
site-directed mutagenesis, residue of the alpha-subunit, 27% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G275F
-
site-directed mutagenesis, residue of the alpha-subunit, 6-7% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G275I
-
site-directed mutagenesis, residue of the alpha-subunit, 15% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G275P
-
site-directed mutagenesis, residue of the alpha-subunit, 0.04% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G284P
-
site-directed mutagenesis, residue of the alpha-subunit, 1-2% of the wild-type activity
H285A
-
26% reduced activity with octanal, 74% reduced activity with decanal, complete loss of dodecanal activity
H81A
-
site-directed mutagenesis, residue of the beta-subunit, mutant shows 59% of wild-type activity
H81A/E89D
-
site-directed mutagenesis, residues of the beta-subunit, mutant shows 13% of wild-type activity
H82A
-
site-directed mutagenesis, residue of the beta-subunit, mutant shows 22% of wild-type activity
K274A
-
89% reduced activity with octanal, 21% reduced activity with decanal, 81% reduced activity with dodecanal
K283A
-
complete loss of octanal and decanal activity, 96% reduced activity with dodecanal, does not significantly impede binding of decanal, results in destabilization of intermediate II, results in a loss in quantum yield comparable with that of the loop deletion mutant, binds reduced flavin more weakly
R291A
-
77% reduced activity with octanal, 58% reduced activity with decanal, 71% reduced activity with dodecanal
V173A
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173C
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173F
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173H
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173I
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173L
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173N
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173S
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173T
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
W277A
-
11% reduced activity with octanal, 50% reduced activity with decanal and dodecanal
Y151A
P07740
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151D
P07740
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151K
P07740
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151R
P07740
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151T
P07740
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151W
P07740
least active mutant, binds reduced flavin with wild-type affinity, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
additional information
-
improvement of a tagging system, allowing real-time monitoring in vivo and in vitro, for luciferase by construction of a highly active, constitutive promoter resulting in a 100fold higher recombinant activity compared to native activity
K286A
-
92% reduced activity with octanal, complete loss of decanal activity, 87% reduced activity with dodecanal, does not significantly impede binding of decanal, increase in exposure of reaction intermediates to a dynamic quencher, results in a loss in quantum yield comparable with that of the loop deletion mutant, binds reduced flavin more weakly
additional information
-
Saccharomyces cerevisiae recombinantly expressing the Vibrio harveyi luciferase produces bright and stable luminescence, transformed yeast strains can grow on 0.5% v/v Z-9-tetradecenal, but die on 0.005% v/v decanal
additional information
-
substrate specificities of mutant enzymes and wild-type enzyme, overview, changes in the kinetics and emission spectrum on mutation of the chromophore-binding platform
additional information
-
immobilization of the FMN reductase-luciferase complex
additional information
-
codon optimization of the luxCDE and frp genes, e.g. adaptation of the bacterial protein to mammalian temperature of 37C, detailed overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
quick refolding within several min at room temperature or 25C 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
-
slow refolding at room temperature or 35C of thermoinactivated recominant enzyme requires the DnaK-DnaJ-GrpE-system encoding the Hsp70 chaperone, 7-8% activity after refolding over 10 min, refolding depends on the Escherichia coli strain used for recombinant expression of the luciferase, overview
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
Aliivibrio fischeri ES114
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
Aliivibrio fischeri ES114
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
biotechnology
-
establishment and evaluation of the enzyme used in a luciferase-based reporter system, pPL2lux, harboring the listerial secA and hlyA promoters translationally fused to luxABCDE, overview
analysis
-
expression of bioluminescent luciferase can be used for rapid and high throughput screening of drugs, e.g. quinolines, acting on Leishmania amastigote-harbouring macrophages and for quantitative real-time monitoring of parasitism features in living mice, overview
analysis
-
development of a quantitative and highly sensitive luciferase-based assay for bacterial toxins, overview
analysis
-
the enzyme is useful for detection and quantification of diverse stable and labile aryl hydrocarbon receptor ligands in different environmental samples, overview
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
Photobacterium leiognathi ATCC 25521
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
Photobacterium leiognathi ATCC 25521
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
Photobacterium phosphoreum ATCC 11040
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
Photobacterium phosphoreum ATCC 11040
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
analysis
P19839, P19840
expression of the bacterial luciferase system in mammalian cells for generation of bioreporters for in vivo monitoring and diagnostics technology, method evaluation and optimization, overview; expression of the bacterial luciferase system in mammalian cells for generation of bioreporters for in vivo monitoring and diagnostics technology, method evaluation and optimization, overview
analysis
-
high-throughput, homogeneous, bioluminescent assay for Pseudomonas aeruginosa gyrase inhibitors and other DNA-damaging agents based on a Photorhabdus luminescens luciferase operon transcriptional fusion to a promoter that responds to DNA damage caused by reduced gyrase levels and fluoroquinoline inhibition
diagnostics
P19839, P19840
expression of the bacterial luciferase system in mammalian cells for generation of bioreporters for in vivo monitoring and diagnostics technology, method evaluation and optimization, overview; expression of the bacterial luciferase system in mammalian cells for generation of bioreporters for in vivo monitoring and diagnostics technology, method evaluation and optimization, overview
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
Photorhabdus luminescens subsp. laumondii TT01
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
Photorhabdus luminescens subsp. laumondii TT01
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
analysis
-
enzyme can be used to monitor changes in gene expression as a reporter system in slow-growing mycobacteria, i.e. Mycobacterium tuberculosis strain H37Ra, determination of recombinant enzyme decay rate
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
enzyme can be used to monitor changes in gene expression as a reporter system in slow-growing mycobacteria, i.e. Mycobacterium tuberculosis strain H37Ra, determination of recombinant enzyme decay rate
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
Vibrio harveyi ATCC BAA1116
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
Vibrio harveyi ATCC BAA1116
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-