Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.4.1.21
-
RECOMMENDED NAME
GeneOntology No.
S-ribosylhomocysteine lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-S bond cleavage
additional information
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
autoinducer AI-2 biosynthesis I
-
-
autoinducer AI-2 biosynthesis II (Vibrio)
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
methionine metabolism
-
-
S-adenosyl-L-methionine cycle I
-
-
SYSTEMATIC NAME
IUBMB Comments
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]
Contains Fe2+. The 4,5-dihydroxypentan-2,3-dione formed spontaneously cyclizes and combines with borate to form an autoinducer (AI-2) in the bacterial quorum-sensing mechanism, which is used by many bacteria to control gene expression in response to cell density [2].
CAS REGISTRY NUMBER
COMMENTARY hide
37288-63-4
not distinguished from EC 3.2.1.148, formerly 3.3.1.3
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 4074
-
-
Manually annotated by BRENDA team
strain 4074
-
-
Manually annotated by BRENDA team
isolate SSU
Uniprot
Manually annotated by BRENDA team
strain CCUG 30811T
-
-
Manually annotated by BRENDA team
strain CCUG 30811T
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain 168, BSIP1758 mutant lacking luxS
SwissProt
Manually annotated by BRENDA team
gene luxS
-
-
Manually annotated by BRENDA team
gene luxS
-
-
Manually annotated by BRENDA team
gene luxS
UniProt
Manually annotated by BRENDA team
gene luxS
UniProt
Manually annotated by BRENDA team
strain 81-176
UniProt
Manually annotated by BRENDA team
strain TX1
UniProt
Manually annotated by BRENDA team
strain TX1
UniProt
Manually annotated by BRENDA team
strain NCPPB1665 (Ea1665)
-
-
Manually annotated by BRENDA team
Erwinia amylovora NCPPB1665 (Ea1665)
strain NCPPB1665 (Ea1665)
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene luxS
UniProt
Manually annotated by BRENDA team
strain GG
-
-
Manually annotated by BRENDA team
strain GG
-
-
Manually annotated by BRENDA team
no activity in Agrobacterium tumefaciens
-
-
-
Manually annotated by BRENDA team
no activity in Alphaproteobacteria
-
-
-
Manually annotated by BRENDA team
no activity in Bacteroidetes
-
-
-
Manually annotated by BRENDA team
no activity in Desulfovibrio desulfuricans
-
-
-
Manually annotated by BRENDA team
no activity in Enterobacter aerogenes
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella pneumoniae
-
-
-
Manually annotated by BRENDA team
no activity in Marinomonas sp.
-
-
-
Manually annotated by BRENDA team
no activity in Marinomonas sp. MED121
-
-
-
Manually annotated by BRENDA team
no activity in Neptuniibacter caesariensis
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa
-
-
-
Manually annotated by BRENDA team
no activity in Rhodobacter capsulatus
-
-
-
Manually annotated by BRENDA team
no activity in Rhodobacter sphaeroides strain 2.4.1
-
-
-
Manually annotated by BRENDA team
no activity in Salmonella typhimurium
-
-
-
Manually annotated by BRENDA team
no activity in Sinorhizobium meliloti
-
-
-
Manually annotated by BRENDA team
no activity in Vibrio vulnificus
-
-
-
Manually annotated by BRENDA team
no activity in Zymomonas mobilis
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Serratia kiliensis
-
-
-
Manually annotated by BRENDA team
Serratia malilotii
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Serratia putrefaciens
-
-
-
Manually annotated by BRENDA team
strain DSM 9167T
-
-
Manually annotated by BRENDA team
strain LMG 20552T
-
-
Manually annotated by BRENDA team
Shewanella fidelis LMG 20552T
strain LMG 20552T
-
-
Manually annotated by BRENDA team
strain LMG 18921T
-
-
Manually annotated by BRENDA team
strain LMG 18921T
-
-
Manually annotated by BRENDA team
strain DT-1
-
-
Manually annotated by BRENDA team
strain DT-1
-
-
Manually annotated by BRENDA team
strain LMG 19691T
-
-
Manually annotated by BRENDA team
strain LMG 19691T
-
-
Manually annotated by BRENDA team
strain LMG 21403T
-
-
Manually annotated by BRENDA team
strain LMG 21403T
-
-
Manually annotated by BRENDA team
strain LMG 21408T
-
-
Manually annotated by BRENDA team
Shewanella sairae LMG 21408T
strain LMG 21408T
-
-
Manually annotated by BRENDA team
strain LMG 21406T
-
-
Manually annotated by BRENDA team
strain LMG 21406T
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain RN6390B
-
-
Manually annotated by BRENDA team
serotype 2, gene luxS
UniProt
Manually annotated by BRENDA team
strain MVP01
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain BB170
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
L-homocysteine + ?
show the reaction diagram
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
assay at pH 7.0, 23C
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe(III)
-
Fe(III) upregulates expression of luxS and Fe(III) strongly enhances biofilm formation at concentrations above 50 microM
Zinc
-
zinc-dependent metalloenzyme, each active site contains a zinc ion coordinated by the conserved residues His54, His58 and Cys126, and includes residues from both subunits
additional information
-
to gain insight into the catalytic mechanism of the unusual reaction and the function of the metal cofactor, an efficient expression and purification system is developed to produce LuxS enriched in either Fe2+, Co2+ or Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
(2S)-2-amino-6-(N-formyl-N-hydroxyamino)hexanoic acid
-
-
D-erythronohydroxamic acid
D-ribosylornithine
-
-
methionine
-
-
S-(1-amino-1,4-anhydro-1,5-dideoxy-D-ribitol-5-yl)-L-homocysteine
-
inhibition of Co(II)-substituted enzyme
S-(3,5-dideoxy-3-fluoro-1-O-methyl-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(3,5-dideoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(3,5-dideoxy-D-erythro-pentofuranos-5-yl)homocysteine
-
-
S-(4-amino-4,5-dideoxy-alpha/beta-D-ribofuranos-5-yl)-L-homocysteine
-
inhibition of Co(II)-substituted enzyme. The hemiaminal may undergo ring opening to form an aldehyde which may undergo the aldose-ketose isomerization reaction to form a 2-ketone, which presumably binds to the LuxS active site with higher affinity than the original ribose analogue
S-(4-amino-4,5-dideoxy-D-ribono-1,4-lactam-5-yl)-L-homocysteine
-
inhibition of Co(II)-substituted enzyme
S-(5-deoxy-3-deoxy-3-bromo-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(5-deoxy-3-deoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(5-deoxy-3-O-methyl-D-ribofuranos-5-yl)homocysteine
-
-
S-(5-deoxy-3-O-methyl-D-xylofuranos-5-yl)homocysteine
-
-
S-(5-deoxy-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
S-[3-fluoro-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
additional information
-
5,6,7,8,9-pentadeoxy-6-fluoro-D-ribo-dec-5(Z)-enofuranuronate a S-ribosylhomocysteine analogue and 5,6-dideoxy-6-fluoro-D-ribo-hex-5-enofuranose a S-ribosylhomocysteine analogue have no inhibitory activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose
expression of LuxS is increased by 0.5% (w/v) D-glucose
additional information
-
luxS expression is not regulated by autoinducer-2, modulation of luxS expression levels allows adjusting bacterial fitness in response to changing host conditions
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036 - 0.73
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
0.0014 - 0.18
S-ribosylhomocysteine
additional information
additional information
-
KM-values of enzyme forms enriched in either Fe2+, Co2+ or Zn2+
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.64
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
0.027 - 0.4
S-ribosylhomocysteine
additional information
additional information
Bacillus subtilis
-
turnover numbers of enzyme forms enriched in either Fe2+, Co2+ or Zn2+
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00037 - 0.0128
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
0.00072 - 0.0196
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
0.147 - 2.4
D-erythronohydroxamic acid
0.068
D-ribosylornithine
-
Co2+ substituted enzyme
0.061
methionine
-
Co2+ substituted enzyme
0.048
S-(1-amino-1,4-anhydro-1,5-dideoxy-D-ribitol-5-yl)-L-homocysteine
-
pH 7.0, 22C
0.042
S-(3,5-dideoxy-3-fluoro-1-O-methyl-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.0077
S-(3,5-dideoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.055
S-(3,5-dideoxy-D-erythro-pentofuranos-5-yl)homocysteine
-
pH 7.0, 23C
0.0035
S-(4-amino-4,5-dideoxy-alpha/beta-D-ribofuranos-5-yl)-L-homocysteine
-
pH 7.0, 22C
0.037
S-(4-amino-4,5-dideoxy-D-ribono-1,4-lactam-5-yl)-L-homocysteine
-
pH 7.0, 22C
0.0079
S-(5-deoxy-3-deoxy-3-bromo-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.0106
S-(5-deoxy-3-deoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.042
S-(5-deoxy-3-O-methyl-D-ribofuranos-5-yl)homocysteine
-
pH 7.0, 23C
0.066
S-(5-deoxy-3-O-methyl-D-xylofuranos-5-yl)homocysteine
-
pH 7.0, 23C
0.0042
S-(5-deoxy-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.0079 - 0.047
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
0.0106
S-[3-fluoro-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
wild type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
3 * 12500
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Co2+-substituted BsLuxS is cocrystallized with inhibitors (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid and (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid by the hanging drop vapor diffusion method
-
hanging drop vapor diffusion, inactive mutant C84A of Co2+-substituted LuxS is cocrystallized with the 2-ketone intermediate and the structure is determined to 1.8 A resolution
-
hanging-drop vapor diffusion method with ammonium sulfate as precipitant, structure at 1.6 A resolution
-
hanging-drop vapour diffusion method with ammonium sulfate as the precipitant. The crystals belong to the enantiomorphic space groups P6(1)22 or P6(5)22 with approximate unit-cell parameters A = b = 63.6, c = 151.5 A. The crystals diffract X-rays to at least 1.55 A resolution on a synchrotron-radiation source
-
structure of LuxS is determined at 1.2 A resolution, together with the binary complexes of LuxS with S-ribosylhomocysteine and homocysteine to 2.2 A and 2.3 A resolution, hanging-drop vapour diffusion method
-
purified recombinant enzyme, hanging-drop vapour-diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl pH 8.0, 100 mM NaCl, 1 mM DTT, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl pH 8.0, 20% w/v PEG 3350, and equilibartion against 0.2 ml of reservoir solution, 18C, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
LuxS expression is decreased at 37C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
absorption and electron paramagnetic resonance spectroscopic studies reveals that the active form of LuxS contains a metal-bound water and a thiolate ion at Cys-83, an invariant Arg-39 in the active site is partially responsible for stabilizing the thiolate anion of Cys-83
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the DELTAluxS mutant shows higher sensitivity to both hydrogen peroxide and cumene hydroperoxide than the wild type enzyme with consistently greater zones of inhibition
692435
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, when stored in the frozen form, the LuxS proteins are stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose Fast-Flow column chromatography and ultrafiltration
recombinant soluble GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, desalting gel filtration, ultrafiltration, anion exchange chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as lsrR knockout by chromosomal gene replacement
expressed in Escherichia coli DH5alpha cells
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
gene luxS, DNA and amino acid sequence determination and analysis, sequence comparisons
gene luxS, DNA and amino acid sequence determination and analysis, sequence comparisons, the functional luxS orthologue can complement autoinducer AI-2 production in Escherichia coli strain BL21(DE3)
-
gene luxS, sequence comparisons, expression and transcriptome analysis of wild-type and enzyme knockout mutant strains
gene luxS, soluble expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
-
LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms
-
LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms; mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms
-
mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms
-
mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms; mutant LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms
overexpression as glutathione-S-transferase fusion in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Fe(III) upregulates expression of luxS and Fe(III) strongly enhances biofilm formation at concentrations above 50 microM
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C84S
-
more than 220fold reduced activity
C85A
-
catalytically inactive mutant
E57A
-
no detectable activity
E57D
-
220fold reduced activity
E57Q
-
no detectable activity
H11Q
-
by site directed mutagenesis
R39M
-
by site directed mutagenesis
S6A
-
by site directed mutagenesis
Y89F
-
by site directed mutagenesis
C41A
-
by site directed mutagenesis
C83D
-
by site directed mutagenesis
C83A
-
mutant shows lower activity than the wild type enzyme
E57A
-
mutant shows lower activity than the wild type enzyme
E57D
-
mutant shows lower activity than the wild type enzyme
H11Q
-
mutant shows lower activity than the wild type enzyme
R39M
-
mutant shows lower activity than the wild type enzyme
S6A
-
mutant shows lower activity than the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
rapid, selective, and sensitive liquid chromatography-tandem mass spectrometry assay for the simultaneous quantification of the metabolites and precursors of the activated methyl cycle. Analytes are extracted from Escherichia coli MG1655 and chemically derivatized as N(O,S)-iso-butyloxycarbonyl iso-butyl esters using iso-butyl chloroformate in an aqueous iso-butanol/pyridine environment. S-Adenosylmethionine, S-adenosylhomocysteine, S-ribosylhomocysteine, homocysteine, methionine, cystathionine, cysteine, and homoserine are quantified by liquid chromatography-positive ion tandem electrospray ionization mass spectrometry. Internal standards are isotopically labeled [13CD3]methionine and S-adenosylcysteine. Linearity of the assay is established up to a concentration of 700 microg/g cell dry weight for each analyte
medicine
autoinducer-2 promotes interspecies signaling, the autoinducer-3 activates enterohemorrhagic Escherichia coli virulence genes, knocking out luxS in the enterohemorrhagic human pathogen Escherichia coli reveals a defect in AI-3 production, but not in AI-2 production
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