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Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase and Organism(s) Escherichia coli for references in articles please use BRENDA:EC4.4.1.21
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EC Tree
IUBMB Comments 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 .
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
AI-2 synthase, autoinducer-2 synthase, BsLuxS, EcLuxS,
lsrR ,
Lux S ,
LuxS , LuxS protein, S-ribosyl homocysteinase, S-ribosylhomocysteinase,
more
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S-ribosylhomocysteine lyase
S-ribosylhomocysteinelyase
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LuxS
-
-
S-ribosylhomocysteinase
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-
S-ribosylhomocysteinase
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S-ribosylhomocysteinase
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S-ribosylhomocysteine lyase
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S-ribosylhomocysteine lyase
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additional information
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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
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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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37288-63-4
not distinguished from EC 3.2.1.148, formerly 3.3.1.3
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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 + (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
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
-
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
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
-
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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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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
-
-
?
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S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
-
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
-
-
?
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Zn2+
-
Zn2+ substitution produces an enzyme with 10-fold lower activity
Co2+
-
-
Co2+
-
Co2+ substitution produces a highly stable enzyme
Fe2+
-
-
Fe2+
-
acts as a Lewis acid
Fe2+
-
LuxS is a metalloenzyme containing a tetrahedrally coordinated Fe2+ ion in its active site
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(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
-
-
D-erythronohydroxamic acid
-
-
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
-
S-[3-fluoro-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
-
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0.027
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
0.016 - 0.037
S-ribosylhomocysteine
0.016
S-ribosylhomocysteine
-
C41A mutant; wild type enzyme
0.016
S-ribosylhomocysteine
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Co2+ substitued enzyme
0.037
S-ribosylhomocysteine
-
wild type enzyme
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0.4
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
0.4
S-ribosylhomocysteine
-
wild type enzyme
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0.0127
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Co2+ substituted enzyme
0.0032
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Co2+ substituted enzyme
0.72
D-erythronohydroxamic acid
-
Co2+ substituted enzyme
0.047
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
wild type enzyme
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-
-
brenda
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SwissProt
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SwissProt
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EHEC, O157:H7
SwissProt
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malfunction
mutation affects motility/flagella formation/metabolism
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
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A0A1Y2YCU9_ECOLX
171
0
19460
TrEMBL
A0A4T4NWB2_ECOLX
171
0
19402
TrEMBL
A0A376D3C4_ECOLX
108
0
12352
TrEMBL
A0A3K0UC65_ECOLX
171
0
19430
TrEMBL
A0A5E9ZYL6_ECOLX
171
0
19433
TrEMBL
A0A0K6DC98_ECOLX
171
0
19401
TrEMBL
A0A0K4SB60_ECOLX
171
0
19357
TrEMBL
A0A377FJ40_ECOLX
171
0
19442
TrEMBL
J7QGW0_ECOLX
171
0
19430
TrEMBL
C3SY42_ECOLX
171
0
19444
TrEMBL
A0A4U9U5C7_ECOLX
156
0
17514
TrEMBL
A0A4V6LXZ6_ECOLX
171
0
19454
TrEMBL
A0A3Z3EQV8_ECOLX
171
0
19415
TrEMBL
A0A5B9ARD5_ECOLX
171
0
19386
TrEMBL
A0A066RNM3_ECOLX
171
0
19417
TrEMBL
F2XHH9_ECOLX
171
0
19416
TrEMBL
A0A3Q0P292_ECOLX
171
0
19442
TrEMBL
A0A449CDZ1_ECOLX
171
0
19471
TrEMBL
A0A2K3TQ94_ECOLX
171
0
19427
TrEMBL
A0A370YTU1_ECOLX
151
0
16868
TrEMBL
E2QQE1_ECOLX
171
0
19443
TrEMBL
A0A3K3INN3_ECOLX
171
0
19489
TrEMBL
A0A418H3G4_ECOLX
71
0
8046
TrEMBL
A0A3L0VXR5_ECOLX
169
0
18791
TrEMBL
A0A376I224_ECOLX
171
0
19364
TrEMBL
A0A418GS41_ECOLX
133
0
14997
TrEMBL
A0A210GFX1_ECOLX
171
0
19385
TrEMBL
A0A5E8HN61_ECOLX
171
0
19391
TrEMBL
A0A376D4K4_ECOLX
72
1
8043
TrEMBL
A0A0L1C2M1_ECOLX
171
0
19431
TrEMBL
A0A370YMZ1_ECOLX
171
0
19283
TrEMBL
Q6A197_ECOLX
142
0
16055
TrEMBL
A0A2T1LGJ0_ECOLX
171
0
19339
TrEMBL
A0A3W4SPP7_ECOLX
171
0
19446
TrEMBL
A0A4Y9C710_ECOLX
171
0
19189
TrEMBL
A0A0K4BFT8_ECOLX
171
0
19402
TrEMBL
A0A5P0LWU7_ECOLX
171
0
19389
TrEMBL
A0A376HPL1_ECOLX
171
0
19388
TrEMBL
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C41A
-
by site directed mutagenesis
C83D
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by site directed mutagenesis
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Q-Sepharose Fast-Flow column chromatography and ultrafiltration
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as lsrR knockout by chromosomal gene replacement
LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms
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mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms
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analysis
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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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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
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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
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, Escherichia coli (P45578), 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
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
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
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
Bacillus anthracis (Q81KF3), Bacillus cereus (Q816N5), Bacillus clausii (Q5WDW1), 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), Lactobacillus 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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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
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