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IUBMB CommentsContains 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 .
Synonyms
luxs protein, s-ribosylhomocysteinase, ai-2 synthase, s-ribosylhomocysteine lyase, autoinducer-2 synthase, s-ribosylhomocysteinelyase, s-ribosyl homocysteinase,
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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].
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S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
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S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
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S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
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the reactive by-product of the LuxS-catalysed reaction 4,5-dihydroxy-2,3-pentanedione undergoes spontaneous cyclization reactions to form autoinducer 2
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S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
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the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
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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
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LuxS is required for normal biofilm development
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S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
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the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
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additional information
?
-
additional information
?
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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
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?
additional information
?
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LuxS is required for normal biofilm development
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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
Escherichia coli, Neisseria meningitidis, no activity in Pseudomonas aeruginosa, Porphyromonas gingivalis, Staphylococcus aureus
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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
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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, Serratia plymuthica, Staphylococcus aureus, Vibrio harveyi
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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
Alkalihalobacillus clausii (Q5WDW1), Bacillus anthracis (Q81KF3), Bacillus cereus (Q816N5), Bacillus subtilis (O34667), Bifidobacterium longum (Q8G568), Campylobacter jejuni (Q9PN97), Clostridium perfringens (Q0SWJ6), Deinococcus geothermalis (Q1IW42), Deinococcus radiodurans (Q9RRU8), Escherichia coli (Q8X902), Haemophilus influenzae (P44007), Helicobacter pylori (Q9ZMW8), Lactobacillus acidophilus (Q5FK48), Lactobacillus johnsonii (Q74HV0), Limosilactobacillus reuteri (Q5QHW1), Psychromonas ingrahamii (A1SZZ2), Shigella flexneri (Q83JZ4), Staphylococcus aureus (Q6GEU1), Staphylococcus epidermidis (Q8CNI0), Streptococcus mutans (Q8DVK8), Streptococcus pyogenes (P0C0C7), Thermus thermophilus (Q72IE6), Vibrio cholerae (Q9KUG4)
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