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(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
L-homocysteine + ?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxy-2,3-pentanedione
assay at pH 7.0, 23°C
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
additional information
?
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
L-homocysteine + ?
-
-
-
-
?
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
L-homocysteine + ?
-
-
-
-
?
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
L-homocysteine + ?
-
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
-
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
-
furanose-containing S-ribosylhomocysteine
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the autoinducer Al-2, a five-carbon furanone results from the spontaneous cyclization of 4,5-dihydroxy-2,3-pentanedione
-
?
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the autoinducer Al-2, a five-carbon furanone results from the spontaneous cyclization of 4,5-dihydroxy-2,3-pentanedione
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
mechanism
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
key step in biosynthesis pathway of type II autoinducer AI-2
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
enzyme is involved in synthesis of the autoinducer AI-2 that is an universal signal, which may be used by a variety of bacteria for communication among and between species and may be responsible for regulation of virulence genes in Escherichia coli O157:H7
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
ETF12584, ETF12641
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
ETF12584, ETF12641
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
4,5-dihydroxy-2,3-pentanedione is the precursor of the quorum-sensing molecule autoinducer 2
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
Serratia kiliensis
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
Serratia malilotii
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
Serratia putrefaciens
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
-
the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
-
ir
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
mechanism
-
-
?
additional information
?
-
-
LuxS is functional in the autoinducer-2-mediated quorum sensing and may regulate different behaviors including biofilm formation and virulence
-
-
?
additional information
?
-
-
LuxS is functional in the autoinducer-2-mediated quorum sensing and may regulate different behaviors including biofilm formation and virulence
-
-
?
additional information
?
-
-
LuxS affects both luminescence regulation and colonization competence - however its quantitative contribution is small when compared to that of the AinS signal
-
-
?
additional information
?
-
-
autoinducer 2 synthesis enzyme assay using Vibrio harveyi sensor strains, wild-type BB120 is a sensor mutant derived from BB120 and responds only to presence of AI-2, but not the other autoinducers from Vibrio harveyi
-
-
?
additional information
?
-
-
autoinducer 2 synthesis enzyme assay using Vibrio harveyi sensor strains, wild-type BB120 is a sensor mutant derived from BB120 and responds only to presence of AI-2, but not the other autoinducers from Vibrio harveyi
-
-
?
additional information
?
-
-
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
?
additional information
?
-
-
LuxS catalyzes the last step in the production of autoinducer-2
-
-
?
additional information
?
-
-
LuxS catalyzes the last step in the production of autoinducer-2
-
-
?
additional information
?
-
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
?
additional information
?
-
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
?
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
?
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
?
additional information
?
-
-
growth phase regulation of flaA expression in Helicobacter pylori is luxS-dependent
-
-
?
additional information
?
-
ETF12584
both isoforms LuxS1 and LuxS2 can effectively convert S-ribosylhomocysteine to autoinducer AI-2 and homocysteine, and they may have redundant functions
-
-
?
additional information
?
-
ETF12641
both isoforms LuxS1 and LuxS2 can effectively convert S-ribosylhomocysteine to autoinducer AI-2 and homocysteine, and they may have redundant functions
-
-
?
additional information
?
-
-
both isoforms LuxS1 and LuxS2 can effectively convert S-ribosylhomocysteine to autoinducer AI-2 and homocysteine, and they may have redundant functions
-
-
?
additional information
?
-
ETF12584
both isoforms LuxS1 and LuxS2 can effectively convert S-ribosylhomocysteine to autoinducer AI-2 and homocysteine, and they may have redundant functions
-
-
?
additional information
?
-
ETF12641
both isoforms LuxS1 and LuxS2 can effectively convert S-ribosylhomocysteine to autoinducer AI-2 and homocysteine, and they may have redundant functions
-
-
?
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
?
additional information
?
-
-
LuxS is involved in the activated methyl cycle and influences biofilm formation
-
-
?
additional information
?
-
-
LuxS is involved in the activated methyl cycle and influences biofilm formation
-
-
?
additional information
?
-
-
the LuxS/AI-2 (autoinducer 2) system does not appear to contribute to the overall fitness of Staphylococcus aureus RN6390B during intracellular growth in epithelial cells
-
-
?
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
?
additional information
?
-
-
the LuxS/AI-2 (autoinducer 2) system does not appear to contribute to the overall fitness of Staphylococcus aureus RN6390B during intracellular growth in epithelial cells
-
-
?
additional information
?
-
-
LuxS is related on the one hand to down-regulation of competence, and on the other hand to attenuation of autolysis in cultures entering stationary phase. The impact of LuxS on competence, but not on autolysis, involves cel-cell communication
-
-
?
additional information
?
-
-
LuxS plays an important role in the regulation of motility and flagella biogenesis
-
-
?
additional information
?
-
the LuxS quorum sensing system plays an important role in regulating the expression of virulence factors
-
-
?
additional information
?
-
-
LuxS plays an important role in the regulation of motility and flagella biogenesis
-
-
?
additional information
?
-
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
?
additional information
?
-
-
the enzyme is involved in one of the the quorum sensing systems that function in parallel to control the density-dependent expression of the luciferase structural operon luxCDABE. Each system is composed of a sensor, sensor I or sensor 2, and its cognate autoinducer, AI-1 or AI-2. LuxS has a role in the enzymatic synthesis of AI-2
-
-
?
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malfunction
mutation affects biofilm formation
malfunction
mutation affects biofilm formation
malfunction
mutation affects biofilm formation
malfunction
mutation affects motility/flagella formation/metabolism
malfunction
mutation affects motility/flagella formation/metabolism
malfunction
mutation affects motility/flagella formation/metabolism
malfunction
mutation affects motility/flagella formation/metabolism
malfunction
mutation affects toxin production
malfunction
mutation affects toxin production
malfunction
mutation affects toxin production
malfunction
mutation affects toxin production
malfunction
inactivation of luxS gene leads to a wide range of phenotypic changes including thinner capsular walls, increased tolerance to H2O2, reduced adherence capacity to epithelial cells. In particular, loss of LuxS impairs dramatically full virulence of serotype 2 in experimental model of piglets, and functional complementation restores virulence nearly to the level of parent strain
malfunction
transcriptomic and metabolomic changes of wild-type enzyme and an insertional knockout mutant strains, especially expression of lipoproteins of the YaeC family and cysteine synthase are affected, overview
malfunction
-
transcriptomic and metabolomic changes of wild-type enzyme and an insertional knockout mutant strains, especially expression of lipoproteins of the YaeC family and cysteine synthase are affected, overview
-
malfunction
-
inactivation of luxS gene leads to a wide range of phenotypic changes including thinner capsular walls, increased tolerance to H2O2, reduced adherence capacity to epithelial cells. In particular, loss of LuxS impairs dramatically full virulence of serotype 2 in experimental model of piglets, and functional complementation restores virulence nearly to the level of parent strain
-
physiological function
produces precursor of type 2 autoinducer for bacterial cell-cell communication
physiological function
-
Fe(III) upregulates expression of luxS and Fe(III) strongly enhances biofilm formation at concentrations above 50 microM. A luxS-deficient mutant fails to form a biofilm, even with Fe(III) supplementation, whereas a derivative over-expressing luxS exhibits enhanced biofilm formation capacity, and can form a biofilm without added Fe(III). The luxS-deficient mutant exhibits reduced expression of the major Fe(III) transporter PiuA, and cellular cencentration of Fe(III) is significantly lower than in wild-type. The luxS overexpressing mutant has a significantly higher cellular concentration of Fe(III) than the wild-type. Release of extracellular DNA, which is an important component of the biofilm matrix, is also directly related to luxS expression. Genetic competence, as well as expression of competence genes comD, comX, comW, cglA and dltA, and the murein hydrolase cbpD associated with fratricide-dependent DN release, are all directly related to luxS expression levels, and further up-regulated by Fe(III)
physiological function
-
isogenic strains carrying mutations in luxS or its neighboring genes cysK, and metB can not grow without added cysteine, suggesting roles in cysteine synthesis. Growth of the DELTAluxSHp mutant is restored by homocysteine or cystathionine. S-ribosylhomocysteine accumulates in the DELTAluxS mutant, suggesting that in Helicobacter pylori, S-ribosylhomocysteine is converted by LuxS to homocysteine as in the classic activated methyl cycle, and thence by CysK to cystathionine and by MetB to cysteine
physiological function
-
mutation of luxS leads to profound differences in activated methyl cycle metabolite concentrations. Unable to metabolize these substrates, the concentration of S-ribosylhomocysteine continues to accrue throughout their growth. By the stationary phase, the concentration of ribosylhomocysteine in the DELTAluxS mutant is approximately 460fold higher when compared with that in the wild-type strain. Homocysteine is significantly lower in the mutant when compared with the wild-type
physiological function
-
S-ribosyl homocysteinase is a key enzyme in the formation of the signaling molecule of QS-2, autoinducer II
physiological function
-
S-ribosylhomocysteinase from Streptococcus mutans plays a crucial role in the quorum-sensing system
physiological function
-
the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
physiological function
the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
physiological function
the enzyme is required for synthesis of autoinducer 2, a signaling molecule for inter-species quorum sensing. Cell adherence analyses with human laryngeal epithelial cell line Hep-2 and human umbilical vein endothelial cells
physiological function
two potential roles for the enzyme, the first is in the production of autoinducer-2, mediating quorum sensing, and the second is as an enzyme in the activated methyl cycle, where it catalyzes the conversion of S-ribosylhomocysteine to homocysteine. The by-product of the reaction catalyzed by the enzyme is (S)-4,5-dihydroxy-2,3-pentanedione, which spontaneously forms the furanones known collectively as autoinducer-2, AI-2
physiological function
-
Deletion of the luxS gene increases biofilm formation, but does not affect the bacterial growth rate. Deletion of the luxS gene also increases cell-surface hydrophobicity. The luxS mutant strain tends to aggregate into distinct clusters and relatively dense structures, whereas the wild-type strain appears confluent and more evenly distributed. All genes examined are up-regulated in the biofilms formed by the luxS mutant strain
physiological function
-
Deletion of the luxS gene increases biofilm formation, but does not affect the bacterial growth rate. Deletion of the luxS gene also increases cell-surface hydrophobicity. The luxS mutant strain tends to aggregate into distinct clusters and relatively dense structures, whereas the wild-type strain appears confluent and more evenly distributed. All genes examined are up-regulated in the biofilms formed by the luxS mutant strain
-
physiological function
-
the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
-
physiological function
-
the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
-
physiological function
-
two potential roles for the enzyme, the first is in the production of autoinducer-2, mediating quorum sensing, and the second is as an enzyme in the activated methyl cycle, where it catalyzes the conversion of S-ribosylhomocysteine to homocysteine. The by-product of the reaction catalyzed by the enzyme is (S)-4,5-dihydroxy-2,3-pentanedione, which spontaneously forms the furanones known collectively as autoinducer-2, AI-2
-
physiological function
-
the enzyme is required for synthesis of autoinducer 2, a signaling molecule for inter-species quorum sensing. Cell adherence analyses with human laryngeal epithelial cell line Hep-2 and human umbilical vein endothelial cells
-
additional information
-
elucidation of the mechanism of the first stage of the enzyme catalytic process by docking and molecular dynamics simulations, overview. An active site water stably locates within the active site, it can facilitate ring-opening of either alpha-S-ribosylhomocysteine or beta-furanose, leading to formation of a common active-site-bound 2-keto-S-ribosylhomocysteine intermediate, without the need to pass through a linear aldose S-ribosylhomocysteine configuration. Catalytic importance of several active site residues including Ser6, His11, Arg39, Cys84, and Glu57
additional information
modeling of enzyme protein structure and luxS-mediated global regulation using the genome-wide microarray analyses, overview
additional information
-
modeling of enzyme protein structure and luxS-mediated global regulation using the genome-wide microarray analyses, overview
-
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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
C82A
inactive, mutation decreases autoinducer AI-2 production and biofilm formation
C82S
43fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
F80M
7fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
F80M/H87Y
42fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
H87Y
37fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
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
C84A
-
no catalytic activity
C84A
-
site-directed mutagenesis, catalytically inactive mutant, the mutant contains a Co2+ ion, in the wild-type the substrate's cyclic ribosyl moiety is positioned adjacent to the Zn2+ ion, while in the mutant the noncyclic ribosyl is ligated to the Co2+ via its C2-O carbonyl oxygen
C84D
-
more than 220fold reduced activity
C84D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
-
a luxS deletion mutant shows obvious growth deficiency when cultured in the serum-free medium and biofilm formation is significantly enhanced, in a mouse infection model, the 50% lethal dose of the mutant strain is increased up to 96fold, and the ability to colonize in different mouse tissues is significantly decreased
additional information
-
a luxS deletion mutant shows obvious growth deficiency when cultured in the serum-free medium and biofilm formation is significantly enhanced, in a mouse infection model, the 50% lethal dose of the mutant strain is increased up to 96fold, and the ability to colonize in different mouse tissues is significantly decreased
-
additional information
the luxS isogenic mutant, prepared by marker exchange mutagenesis, shows an alteration in the dynamics and architecture of the biofilm formation, a decrease in the motility of the bacterium, and an enhanced virulence in the septicemic mouse model
additional information
-
the luxS isogenic mutant, prepared by marker exchange mutagenesis, shows an alteration in the dynamics and architecture of the biofilm formation, a decrease in the motility of the bacterium, and an enhanced virulence in the septicemic mouse model
additional information
the DELTA luxS mutant abolishes AI-2 production and is more sensitive to hydrogen peroxide and cumene hydroperoxide than the wild type enzyme
additional information
-
the DELTA luxS mutant abolishes AI-2 production and is more sensitive to hydrogen peroxide and cumene hydroperoxide than the wild type enzyme
-
additional information
-
inactivation of the luxS gene impairs motility, extracellular polysaccharide production, and tolerance for hydrogen peroxide, and reduces virulence on pear leaves
additional information
-
inactivation of the luxS gene impairs motility, extracellular polysaccharide production, and tolerance for hydrogen peroxide, and reduces virulence on pear leaves
-
additional information
-
the luxS knockout mutant CMPG5412 shows drastically reduced persistence in mice which is related to less survival in simulated gastric juice, indicating that LuxS metabolism is crucial for the gastric stress resistance, the suppressor mutations in the luxS knockout mutant CMPG5413 compensates for the metabolic defects of the luxS mutation and restores the resistance to gastric juice but causes a defect in adherence, biofilm formation, and exopolysaccharide production
additional information
-
the luxS knockout mutant CMPG5412 shows drastically reduced persistence in mice which is related to less survival in simulated gastric juice, indicating that LuxS metabolism is crucial for the gastric stress resistance, the suppressor mutations in the luxS knockout mutant CMPG5413 compensates for the metabolic defects of the luxS mutation and restores the resistance to gastric juice but causes a defect in adherence, biofilm formation, and exopolysaccharide production
-
additional information
generation of a knockout mutant by insertional mutation of the luxS gene, transcriptomic and metabolomic changes of wild-type and mutant strains, overview
additional information
-
generation of a knockout mutant by insertional mutation of the luxS gene, transcriptomic and metabolomic changes of wild-type and mutant strains, overview
additional information
-
generation of a knockout mutant by insertional mutation of the luxS gene, transcriptomic and metabolomic changes of wild-type and mutant strains, overview
-
additional information
-
deletion of luxS alters biofilm formations in static and flow-through conditions, a luxS mutation does not cause a large difference in global gene expression
additional information
-
deletion of luxS alters biofilm formations in static and flow-through conditions, a luxS mutation does not cause a large difference in global gene expression
-
additional information
-
disruption of luxS affects hyaluronidase and intermedilysin gene expressions and leads to 5fold decrease in haemolytic activity of the mutant
additional information
-
a luxS null mutant, constructed by allelic exchange via the replacement of an erythromycin resistance determinant to the gene, is able to accelerate biofilm formation on a polystyrene surface during the mid-exponential growth phase
additional information
generation of a luxS null mutant of 05ZYH33 strain is obtained by homologous recombination
additional information
-
generation of a luxS null mutant of 05ZYH33 strain is obtained by homologous recombination
-
additional information
-
inactive luxS leads to decreased virulence in Vibrio alginolyticus
additional information
the luxS mutants MYJS and MYJM exhibit a lower growth rate and defective flagellar biosynthesis, show a significant decrease in protease production and an increase in both extracellular polysaccharide production and biofilm development
additional information
-
inactive luxS leads to decreased virulence in Vibrio alginolyticus
-
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Das, S.K.; Sedelnikova, S.E.; Baker, P.J.; Ruzheinikov, S.N.; Foster, S.; Hartley, A.; Horsburgh, M.J.; Rice, D.W.
Cloning, purification, crystallization and preliminary crystallographic analysis of Bacillus subtilis LuxS
Acta Crystallogr. Sect. D
57
1324-1325
2001
Bacillus subtilis
brenda
Miller, M.B.; Bassler, B.L.B.
Quorum sensing in bacteria
Annu. Rev. Microbiol.
55
165-199
2001
Vibrio harveyi
brenda
Zhu, J.; Dizin, E.; Hu, X.; Wavreille, A.S.; Park, J.; Pei, D.
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein
Biochemistry
42
4717-4726
2003
Bacillus subtilis
brenda
Anand, S.K.; Griffiths, M.W.
Quorum sensing and expression of virulence in Escherichia coli O157:H7
Int. J. Food Microbiol.
85
1-9
2003
Escherichia coli
brenda
Ruzheinikov, S.N.; Das, S.K.; Sedelnikova, S.E.; Hartley, A.; Foster, S.J.; Horsburgh, M.J.; Cox, A.G.; McCleod, C.W.; Mekhalfia, A.; Blackburn, G.M.; Rice, D.W.; Baker, P.J.
The 1.2 A structure of a novel quorum-sensing protein, Bacillus subtilis LuxS
J. Mol. Biol.
313
111-122
2001
Bacillus subtilis (O34667)
brenda
Winzer, K.; Hardie, K.R.; Burgess, N.; Doherty, N.; Kirke, D.; Holden, M.T.; Linforth, R.; Cornell, K.A.; Taylor, A.J.; Hill, P.J.; Williams, P.
LuxS: its role in central metabolism and the in vitro synthesis of 4-hydroxy-5-methyl-3(2H)-furanone
Microbiology
148
909-922
2002
Porphyromonas gingivalis, Escherichia coli, Staphylococcus aureus, Neisseria meningitidis, no activity in Pseudomonas aeruginosa
brenda
Schauder, S.; Shokat, K.; Surette, M.G.; Bassler, B.L.
The LuxS family of bacterial autoinducers: biosynthesis of a novel quorum-sensing signal molecule
Mol. Microbiol.
41
463-476
2001
Vibrio harveyi, Vibrio harveyi BB170
brenda
Hilgers, M.T.; Ludwig, M.L.
Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site
Proc. Natl. Acad. Sci. USA
98
11169-11174
2001
Bacillus subtilis (O34667)
brenda
Zhu, J.; Patel, R.; Pei, D.
Catalytic mechanism of S-ribosylhomocysteinase (LuxS): stereochemical course and kinetic isotope effect of proton transfer reactions
Biochemistry
43
10166-10172
2004
Bacillus subtilis, Vibrio harveyi
brenda
Rajan, R.; Zhu, J.; Hu, X.; Pei, D.; Bell, C.E.
Crystal structure of S-ribosylhomocysteinase (LuxS) in complex with a catalytic 2-ketone intermediate
Biochemistry
44
3745-3753
2005
Vibrio harveyi, Bacillus subtilis (O34667), Bacillus subtilis
brenda
Loh, J.T.; Forsyth, M.H.; Cover, T.L.
Growth phase regulation of flaA expression in Helicobacter pylori is luxS dependent
Infect. Immun.
72
5506-5510
2004
Helicobacter pylori
brenda
Lupp, C.; Ruby, E.G.
Vibrio fischeri LuxS and AinS: comparative study of two signal synthases
J. Bacteriol.
186
3873-3881
2004
Aliivibrio fischeri
brenda
Doherty, N.; Holden, M.T.; Qazi, S.N.; Williams, P.; Winzer, K.
Functional analysis of luxS in Staphylococcus aureus reveals a role in metabolism but not quorum sensing
J. Bacteriol.
188
2885-2897
2006
Staphylococcus aureus, Staphylococcus aureus RN6390B
brenda
Romao, S.; Memmi, G.; Oggioni, M.R.; Trombe, M.C.
LuxS impacts on LytA-dependent autolysis and on competence in Streptococcus pneumoniae
Microbiology
152
333-341
2006
Streptococcus pneumoniae
brenda
Hullo, M.F.; Auger, S.; Soutourina, O.; Barzu, O.; Yvon, M.; Danchin, A.; Martin-Verstraete, I.
Conversion of methionine to cysteine in Bacillus subtilis and its regulation
J. Bacteriol.
189
187-197
2007
Bacillus subtilis (O34667), Bacillus subtilis 168 (O34667)
brenda
Zhu, J.; Knottenbelt, S.; Kirk, M.L.; Pei, D.
Catalytic mechanism of S-ribosylhomocysteinase: ionization state of active-site residues
Biochemistry
45
12195-12203
2006
Bacillus subtilis (O34667), Escherichia coli (P45578), Escherichia coli, Vibrio harveyi (Q9Z5X1)
brenda
Walters, M.; Sircili, M.P.; Sperandio, V.
AI-3 synthesis is not dependent on luxS in Escherichia coli
J. Bacteriol.
188
5668-5681
2006
Escherichia coli (Q8X902)
brenda
Shen, G.; Rajan, R.; Zhu, J.; Bell, C.E.; Pei, D.
Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase
J. Med. Chem.
49
3003-3011
2006
Escherichia coli (P45578)
brenda
Wnuk, S.F.; Lalama, J.; Robert, J.; Garmendia, C.A.
Novel S-ribosylhomocysteine analogues as potential inhibitors of LuxS enzyme
Nucleosides Nucleotides Nucleic Acids
26
1051-1055
2007
Bacillus subtilis (O34667)
brenda
Jelcic, I.; Huefner, E.; Schmidt, H.; Hertel, C.
Repression of the locus of the enterocyte effacement-encoded regulator of gene transcription of Escherichia coli O157:H7 by Lactobacillus reuteri culture supernatants is LuxS and strain dependent
Appl. Environ. Microbiol.
74
3310-3314
2008
Limosilactobacillus reuteri (Q2F7Q0)
brenda
Lebeer, S.; Claes, I.J.; Verhoeven, T.L.; Shen, C.; Lambrichts, I.; Ceuppens, J.L.; Vanderleyden, J.; De Keersmaecker, S.C.
Impact of luxS and suppressor mutations on the gastrointestinal transit of Lactobacillus rhamnosus GG
Appl. Environ. Microbiol.
74
4711-4718
2008
Lacticaseibacillus rhamnosus, Lacticaseibacillus rhamnosus GG
brenda
Learman, D.R.; Yi, H.; Brown, S.D.; Martin, S.L.; Geesey, G.G.; Stevens, A.M.; Hochella, M.F.
Shewanella oneidensis MR-1 LuxS involvement in biofilm development and sulfur metabolism
Appl. Environ. Microbiol.
75
1301-1307
2009
Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550
brenda
Tian, Y.; Wang, Q.; Liu, Q.; Ma, Y.; Cao, X.; Guan, L.; Zhang, Y.
Involvement of LuxS in the regulation of motility and flagella biogenesis in Vibrio alginolyticus
Biosci. Biotechnol. Biochem.
72
1063-1071
2008
Vibrio alginolyticus, Vibrio alginolyticus MVP01
brenda
Bodor, A.; Elxnat, B.; Thiel, V.; Schulz, S.; Wagner-Doebler, I.
Potential for luxS related signalling in marine bacteria and production of autoinducer-2 in the genus Shewanella
BMC Microbiol.
8
13
2008
Shewanella oneidensis, Vibrio harveyi, Shewanella algae, Shewanella frigidimarina, no activity in Alphaproteobacteria, no activity in Bacteroidetes, Alishewanella fetalis, Shewanella fidelis, Shewanella japonica, Shewanella marinintestina, Shewanella sairae, Shewanella schlegeliana, Shewanella hafniensis, Shewanella frigidimarina LMG 18921T, Shewanella sairae LMG 21408T, Shewanella fidelis LMG 20552T, Shewanella marinintestina LMG 21403T, Shewanella japonica LMG 19691T, Alishewanella fetalis CCUG 30811T, Shewanella schlegeliana LMG 21406T, Shewanella hafniensis DT-1, Shewanella oneidensis MR-1 / ATCC 700550
brenda
Rezzonico, F.; Duffy, B.
Lack of genomic evidence of AI-2 receptors suggests a non-quorum sensing role for luxS in most bacteria
BMC Microbiol.
8
154
2008
Bifidobacterium adolescentis, no activity in Sinorhizobium meliloti, no activity in Rhodobacter sphaeroides strain 2.4.1, no activity in Marinomonas sp., no activity in Neptuniibacter caesariensis, no activity in Desulfovibrio desulfuricans, no activity in Rhodobacter capsulatus, Erwinia billingiae (Q003Y1), Vibrio anguillarum (Q1KMU6), Erwinia tasmaniensis (Q2PA28), no activity in Marinomonas sp. MED121
brenda
Siller, M.; Janapatla, R.P.; Pirzada, Z.A.; Hassler, C.; Zinkl, D.; Charpentier, E.
Functional analysis of the group A streptococcal luxS/AI-2 system in metabolism, adaptation to stress and interaction with host cells
BMC Microbiol.
8
188
2008
Streptococcus pyogenes
brenda
Tavender, T.J.; Halliday, N.M.; Hardie, K.R.; Winzer, K.
LuxS-independent formation of AI-2 from ribulose-5-phosphate
BMC Microbiol.
8
98
2008
Vibrio harveyi
brenda
Zhu, H.; Sun, S.J.; Dang, H.Y.
PCR detection of Serratia spp. using primers targeting pfs and luxS genes involved in AI-2-dependent quorum sensing
Curr. Microbiol.
57
326-330
2008
no activity in Agrobacterium tumefaciens, no activity in Enterobacter aerogenes, no activity in Escherichia coli, no activity in Klebsiella pneumoniae, no activity in Salmonella typhimurium, no activity in Vibrio vulnificus, no activity in Zymomonas mobilis, Serratia ficaria, Serratia fonticola, Serratia kiliensis, Serratia liquefaciens, Serratia malilotii, Serratia marcescens (A1Z1R8), Serratia odorifera, Serratia plymuthica, Serratia proteamaculans, Serratia putrefaciens
brenda
Gao, Y.; Song, J.; Hu, B.; Zhang, L.; Liu, Q.; Liu, F.
The luxS gene is involved in AI-2 production, pathogenicity, and some phenotypes in Erwinia amylovora
Curr. Microbiol.
58
1-10
2009
Erwinia amylovora, Erwinia amylovora NCPPB1665 (Ea1665)
brenda
Han, X.G.; Lu, C.P.
Detection of autoinducer-2 and analysis of the profile of luxS and pfs transcription in Streptococcus suis serotype 2
Curr. Microbiol.
58
146-152
2009
Streptococcus suis
brenda
He, Y.; Frye, J.G.; Strobaugh, T.P.; Chen, C.Y.
Analysis of AI-2/LuxS-dependent transcription in Campylobacter jejuni strain 81-176
Foodborne Pathog. Dis.
5
399-415
2008
Campylobacter jejuni (Q3I354), Campylobacter jejuni 81-176 (Q3I354)
brenda
Gopishetty, B.; Zhu, J.; Rajan, R.; Sobczak, A.J.; Wnuk, S.F.; Bell, C.E.; Pei, D.
Probing the catalytic mechanism of S-ribosylhomocysteinase (LuxS) with catalytic intermediates and substrate analogues
J. Am. Chem. Soc.
131
1243-1250
2009
Bacillus subtilis, Escherichia coli, Vibrio harveyi
brenda
Heurlier, K.; Vendeville, A.; Halliday, N.; Green, A.; Winzer, K.; Tang, C.M.; Hardie, K.R.
Growth deficiencies of Neisseria meningitidis pfs and luxS mutants are not due to inactivation of quorum sensing
J. Bacteriol.
191
1293-1302
2009
Neisseria meningitidis
brenda
Ye, J.; Ma, Y.; Liu, Q.; Zhao, D.L.; Wang, Q.Y.; Zhang, Y.X.
Regulation of Vibrio alginolyticus virulence by the LuxS quorum-sensing system
J. Fish Dis.
31
161-169
2008
Vibrio alginolyticus (A6XJQ9)
brenda
Huang, Z.; Meric, G.; Liu, Z.; Ma, R.; Tang, Z.; Lejeune, P.
luxS-Based quorum-sensing signaling affects biofilm formation in Streptococcus mutans
J. Mol. Microbiol. Biotechnol.
17
12-19
2008
Streptococcus mutans
brenda
Li, L.; Zhou, R.; Li, T.; Kang, M.; Wan, Y.; Xu, Z.; Chen, H.
Enhanced biofilm formation and reduced virulence of Actinobacillus pleuropneumoniae luxS mutant
Microb. Pathog.
45
192-200
2008
Actinobacillus pleuropneumoniae, Actinobacillus pleuropneumoniae 4074
brenda
Kozlova, E.V.; Popov, V.L.; Sha, J.; Foltz, S.M.; Erova, T.E.; Agar, S.L.; Horneman, A.J.; Chopra, A.K.
Mutation in the S-ribosylhomocysteinase (luxS) gene involved in quorum sensing affects biofilm formation and virulence in a clinical isolate of Aeromonas hydrophila
Microb. Pathog.
45
343-354
2008
Aeromonas hydrophila (B1PWE7), Aeromonas hydrophila
brenda
Zhang, M.; Sun, K.; Sun, L.
Regulation of autoinducer 2 production and luxS expression in a pathogenic Edwardsiella tarda strain
Microbiology
154
2060-2069
2008
Edwardsiella tarda (B4XQ50), Edwardsiella tarda, Edwardsiella tarda TX1 (B4XQ50)
brenda
Hardie, K.R.; Heurlier, K.
Establishing bacterial communities by word of mouth: LuxS and autoinducer 2 in biofilm development
Nat. Rev. Microbiol.
6
635-643
2008
Bacillus subtilis, Campylobacter jejuni, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Staphylococcus aureus, Serratia plymuthica, Vibrio harveyi
brenda
Pecharki, D.; Petersen, F.C.; Scheie, A.A.
LuxS and expression of virulence factors in Streptococcus intermedius
Oral Microbiol. Immunol.
23
79-83
2008
Streptococcus intermedius
brenda
Wnuk, S.F.; Robert, J.; Sobczak, A.J.; Meyers, B.P.; Malladi, V.L.; Zhu, J.; Gopishetty, B.; Pei, D.
Inhibition of S-ribosylhomocysteinase (LuxS) by substrate analogues modified at the ribosyl C-3 position
Bioorg. Med. Chem.
17
6699-6706
2009
Bacillus subtilis (O34667)
brenda
Bhattacharyya, M.; Vishveshwara, S.
Functional correlation of bacterial LuxS with their quaternary associations: interface analysis of the structure networks
BMC Struct. Biol.
9
8
2009
Psychromonas ingrahamii (A1SZZ2), Bacillus subtilis (O34667), Streptococcus pyogenes (P0C0C7), Haemophilus influenzae (P44007), Clostridium perfringens (Q0SWJ6), Deinococcus geothermalis (Q1IW42), Lactobacillus acidophilus (Q5FK48), Limosilactobacillus reuteri (Q5QHW1), Alkalihalobacillus clausii (Q5WDW1), Staphylococcus aureus (Q6GEU1), Thermus thermophilus (Q72IE6), Lactobacillus johnsonii (Q74HV0), Bacillus cereus (Q816N5), Bacillus anthracis (Q81KF3), Shigella flexneri (Q83JZ4), Staphylococcus epidermidis (Q8CNI0), Streptococcus mutans (Q8DVK8), Bifidobacterium longum (Q8G568), Escherichia coli (Q8X902), Vibrio cholerae (Q9KUG4), Campylobacter jejuni (Q9PN97), Deinococcus radiodurans (Q9RRU8), Helicobacter pylori (Q9ZMW8)
brenda
Pereira, C.S.; McAuley, J.R.; Taga, M.E.; Xavier, K.B.; Miller, S.T.
Sinorhizobium meliloti, a bacterium lacking the autoinducer-2 (AI-2) synthase, responds to AI-2 supplied by other bacteria
Mol. Microbiol.
70
1223-1235
2008
no activity in Sinorhizobium meliloti
brenda
Halliday, N.M.; Hardie, K.R.; Williams, P.; Winzer, K.; Barrett, D.A.
Quantitative liquid chromatography-tandem mass spectrometry profiling of activated methyl cycle metabolites involved in LuxS-dependent quorum sensing in Escherichia coli
Anal. Biochem.
403
20-29
2010
Escherichia coli
brenda
Malladi, V.L.; Sobczak, A.J.; Meyer, T.M.; Pei, D.; Wnuk, S.F.
Inhibition of LuxS by S-ribosylhomocysteine analogues containing a [4-aza]ribose ring
Bioorg. Med. Chem.
19
5507-5519
2011
Bacillus subtilis
brenda
Trappetti, C.; Potter, A.J.; Paton, A.W.; Oggioni, M.R.; Paton, J.C.
LuxS mediates iron-dependent biofilm formation, competence and fratricide in Streptococcus pneumoniae
Infect. Immun.
79
4550-4558
2011
Streptococcus pneumoniae
brenda
Doherty, N.C.; Shen, F.; Halliday, N.M.; Barrett, D.A.; Hardie, K.R.; Winzer, K.; Atherton, J.C.
In Helicobacter pylori, LuxS is a key enzyme in cysteine provision through a reverse transsulfuration pathway
J. Bacteriol.
192
1184-1192
2010
Helicobacter pylori
brenda
Li, H.; Zhao, H.; Zhu, L.; Hong, L.; Zhang, H.; Lin, F.; Xu, C.; Li, S.; Zhang, Z.
Crystallization and preliminary X-ray analysis of S-ribosylhomocysteinase from Streptococcus mutans
Acta Crystallogr. Sect. F
68
199-202
2012
Streptococcus mutans
brenda
Wilson, C.M.; Aggio, R.B.; OToole, P.W.; Villas-Boas, S.; Tannock, G.W.
Transcriptional and metabolomic consequences of LuxS inactivation reveal a metabolic rather than quorum-sensing role for LuxS in Lactobacillus reuteri 100-23
J. Bacteriol.
194
1743-1746
2012
Limosilactobacillus reuteri (B3XKW0), Limosilactobacillus reuteri, Limosilactobacillus reuteri 100-23 (B3XKW0)
brenda
Peixoto, R.J.; Miranda, K.R.; Ferreira, E.O.; de Paula, G.R.; Rocha, E.R.; Lobo, L.A.; Domingues, R.M.
Production of AI-2 is mediated by the S-ribosylhomocystein lyase gene luxS in Bacteroides fragilis and Bacteroides vulgatus
J. Basic Microbiol.
54
644-649
2014
Bacteroides fragilis, Phocaeicola vulgatus (A6KYS6), Phocaeicola vulgatus, Bacteroides fragilis B3b, Phocaeicola vulgatus ATCC 8482 (A6KYS6), Phocaeicola vulgatus ATCC 8482
brenda
Cao, M.; Feng, Y.; Wang, C.; Zheng, F.; Li, M.; Liao, H.; Mao, Y.; Pan, X.; Wang, J.; Hu, D.; Hu, F.; Tang, J.
Functional definition of LuxS, an autoinducer-2 (AI-2) synthase and its role in full virulence of Streptococcus suis serotype 2
J. Microbiol.
49
1000-1011
2011
Streptococcus suis (A4VTE8), Streptococcus suis 05ZYH33 (A4VTE8)
brenda
Huang, W.; Gherib, R.; Gauld, J.W.
An active site water broadens substrate specificity in S-ribosylhomocysteinase (LuxS): a docking, MD, and QM/MM study
J. Phys. Chem. B
116
8916-8929
2012
Bacillus subtilis
brenda
He, Z.; Liang, J.; Zhou, W.; Xie, Q.; Tang, Z.; Ma, R.; Huang, Z.
Effect of the quorum-sensing luxS gene on biofilm formation by Enterococcus faecalis
Eur. J. Oral Sci.
124
234-240
2016
Enterococcus faecalis, Enterococcus faecalis ATCC 33186
brenda
Wang, Y.; Yi, L.; Wang, S.; Fan, H.; Ding, C.; Mao, X.; Lu, C.
Crystal structure and identification of two key amino acids involved in AI-2 production and biofilm formation in Streptococcus suis LuxS
PLoS ONE
10
e0138826
2015
Streptococcus suis (B2CMA5), Streptococcus suis
brenda
Song, X.D.; Liu, C.J.; Huang, S.H.; Li, X.R.; Yang, E.; Luo, Y.Y.
Cloning, expression and characterization of two S-ribosylhomocysteine lyases from Lactobacillus plantarum YM-4-3 Implication of conserved and divergent roles in quorum sensing
Protein Expr. Purif.
145
32-38
2018
Lactiplantibacillus plantarum (ETF12584), Lactiplantibacillus plantarum (ETF12641), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum YM-4-3 (ETF12584), Lactiplantibacillus plantarum YM-4-3 (ETF12641)
brenda