Any feedback?
Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase and Organism(s) Escherichia coli and UniProt Accession P45578
for references in articles please use BRENDA:EC4.4.1.21Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.4.1.21 S-ribosylhomocysteine lyaseIUBMB 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 .
Specify your search results
Word Map
- 4.4.1.21
-
quorum
-
quorum-sensing
-
interspecies
- harveyi
- thioether
- 4,5-dihydroxy-2,3-pentanedione
- nucleosidase
-
luxs-dependent
-
furanone
- medicine
- analysis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
luxs protein, s-ribosylhomocysteinase, ai-2 synthase, s-ribosylhomocysteine lyase, autoinducer-2 synthase, s-ribosylhomocysteinelyase, s-ribosyl homocysteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LuxS
S-ribosylhomocysteinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
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
37288-63-4
not distinguished from EC 3.2.1.148, formerly 3.3.1.3
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
(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
-
-
-
?
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Zn2+
Zn2+ substitution produces an enzyme with 10-fold lower activity
Fe2+
-
LuxS is a metalloenzyme containing a tetrahedrally coordinated Fe2+ ion in its active site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
0.047
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
wild type enzyme
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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)
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)
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)
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
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
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)
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
EXTERNAL LINKS (specific for EC-Number 4.4.1.21)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
