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Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase and Organism(s) Escherichia coli

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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 .
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This record set is specific for:
Escherichia coli
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
luxs protein, ai-2 synthase, s-ribosylhomocysteinase, s-ribosylhomocysteine lyase, autoinducer-2 synthase, s-ribosylhomocysteinelyase, s-ribosyl homocysteinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-ribosylhomocysteinase
S-ribosylhomocysteine lyase
S-ribosylhomocysteinelyase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-S bond cleavage
additional information
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
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
-
-
-
0
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
-
-
0
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
additional information
?
-
-
LuxS is required for normal biofilm development
-
0
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
Zn2+ substitution produces an enzyme with 10-fold lower activity
INHIBITOR
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
-
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
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0K6DC98_ECOLX
171
0
19401
TrEMBL
-
A0A2T1LGJ0_ECOLX
171
0
19339
TrEMBL
-
A0A3K0UC65_ECOLX
171
0
19430
TrEMBL
-
A0A6D0EKM6_ECOLX
96
0
10773
TrEMBL
-
A0A0L1C2M1_ECOLX
171
0
19431
TrEMBL
-
A0A0K4BFT8_ECOLX
171
0
19402
TrEMBL
-
A0A376HPL1_ECOLX
171
0
19388
TrEMBL
-
Q6A197_ECOLX
142
0
16055
TrEMBL
-
A0A3Q0P292_ECOLX
171
0
19442
TrEMBL
-
A0A376D4K4_ECOLX
72
1
8043
TrEMBL
-
A0A376D3C4_ECOLX
108
0
12352
TrEMBL
-
C3SY42_ECOLX
171
0
19444
TrEMBL
-
E2QQE1_ECOLX
171
0
19443
TrEMBL
-
A0A377FJ40_ECOLX
171
0
19442
TrEMBL
-
A0A3K3INN3_ECOLX
171
0
19489
TrEMBL
-
A0A066RNM3_ECOLX
171
0
19417
TrEMBL
-
F2XHH9_ECOLX
171
0
19416
TrEMBL
-
A0A6H3KV67_ECOLX
171
0
19413
TrEMBL
-
A0A5B9ARD5_ECOLX
171
0
19386
TrEMBL
-
A0A1Y2YCU9_ECOLX
171
0
19460
TrEMBL
-
A0A3L5AJV1_ECOLX
171
0
19330
TrEMBL
-
A0A418GS41_ECOLX
133
0
14997
TrEMBL
-
A0A5E8HN61_ECOLX
171
0
19391
TrEMBL
-
A0A210GFX1_ECOLX
171
0
19385
TrEMBL
-
J7QGW0_ECOLX
171
0
19430
TrEMBL
-
A0A5R1M8M8_ECOLX
171
0
19404
TrEMBL
-
A0A3L0VXR5_ECOLX
169
0
18791
TrEMBL
-
A0A376I224_ECOLX
171
0
19364
TrEMBL
-
A0A418H3G4_ECOLX
71
0
8046
TrEMBL
-
A0A4T4NWB2_ECOLX
171
0
19402
TrEMBL
-
A0A5E9ZYL6_ECOLX
171
0
19433
TrEMBL
-
A0A0K4SB60_ECOLX
171
0
19357
TrEMBL
-
A0A6D0EP37_ECOLX
42
0
4998
TrEMBL
-
A0A2K3TQ94_ECOLX
171
0
19427
TrEMBL
-
A0A6G4BYZ6_ECOLX
171
0
19443
TrEMBL
-
A0A5N9VZU7_ECOLX
106
0
11812
TrEMBL
-
A0A6D0DKL5_ECOLX
171
0
19415
TrEMBL
-
A0A6G6KVY5_ECOLX
171
0
19406
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12500
3 * 12500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
3 * 12500
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C41A
by site directed mutagenesis
C83D
by site directed mutagenesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose Fast-Flow column chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
as lsrR knockout by chromosomal gene replacement
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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), Lactobacillus 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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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