Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
4.4.1.21
-
RECOMMENDED NAME
GeneOntology No.
S-ribosylhomocysteine lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
-
-
-
-
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
catalytic mechanism in which the metal ion catalyzes an intramolecular redox reaction, shifting the carbonyl group from the C-1 position to the C-3 position of the ribose. Subsequent beta-elimination at the C-4 and C-5 position releases homocysteine as a free thiol
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-S bond cleavage
-
-
C-S bond cleavage
-
-
C-S bond cleavage
-
-
C-S bond cleavage
Bacillus subtilis 168, Vibrio harveyi BB170
-
-
-
additional information
O34667
Bacillus subtilis can use methionine as sole sulfur source, the BsluxS knockout mutant grows poorly in the presence of methionine compared to the wild-type strain, methionine utilization requires first its conversion to homocysteine
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
Bacillus subtilis 168
-
Bacillus subtilis can use methionine as sole sulfur source, the BsluxS knockout mutant grows poorly in the presence of methionine compared to the wild-type strain, methionine utilization requires first its conversion to homocysteine
-
PATHWAY
KEGG Link
MetaCyc Link
autoinducer AI-2 biosynthesis I
-
autoinducer AI-2 biosynthesis II (Vibrio)
-
Cysteine and methionine metabolism
-
Metabolic pathways
-
S-adenosyl-L-methionine cycle I
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AI-2 synthase
B4XQ50
-
AI-2 synthase
Edwardsiella tarda TX1
B4XQ50
-
-
AI-2 synthase
-
-
autoinducer-2 synthase
A1Z1R8
-
autoinducer-2 synthase
-
-
BsLuxS
Bacillus subtilis 168
O34667
-
-
EcLuxS
P45578
-
lsrR
Q8X902
gene
LuxS
Actinobacillus pleuropneumoniae 4074
-
-
-
LuxS
Alishewanella fetalis CCUG 30811T
-
-
-
LuxS
Q81KF3
-
LuxS
Q816N5
-
LuxS
Q5WDW1
-
LuxS
Bacillus subtilis 168
O34667
-
-
LuxS
Campylobacter jejuni 81-176
Q3I354
-
-
LuxS
B4XQ50
-
LuxS
Edwardsiella tarda TX1
B4XQ50
-
-
LuxS
Erwinia amylovora NCPPB1665 (Ea1665)
-
-
-
LuxS
Q003Y1
-
LuxS
Q9ZMW8
-
LuxS
Serratia ficaria, Serratia fonticola, Serratia kiliensis, Serratia liquefaciens, Serratia malilotii
-
-
LuxS
A1Z1R8
-
LuxS
Serratia proteamaculans, Serratia putrefaciens
-
-
LuxS
Shewanella fidelis LMG 20552T
-
-
-
LuxS
Shewanella frigidimarina LMG 18921T
-
-
-
LuxS
Shewanella hafniensis DT-1
-
-
-
LuxS
Shewanella japonica LMG 19691T
-
-
-
LuxS
Shewanella marinintestina LMG 21403T
-
-
-
LuxS
Shewanella sairae LMG 21408T
-
-
-
LuxS
Shewanella schlegeliana LMG 21406T
-
-
-
LuxS
Q83JZ4
-
LuxS
Vibrio alginolyticus MVP01
-
-
-
LuxS
Q9KUG4
-
LuxS
Q9Z5X1
-
LuxS
Vibrio harveyi BB170
-
-
-
LuxS protein
-
-
S-ribosylhomocysteinase
-
-
S-ribosylhomocysteinase
O34667
-
S-ribosylhomocysteinase
Bacillus subtilis 168
O34667
-
-
S-ribosylhomocysteinase
Q3I354
-
S-ribosylhomocysteinase
Campylobacter jejuni 81-176
Q3I354
-
-
S-ribosylhomocysteinase
-
-
S-ribosylhomocysteinase
P45578
-
S-ribosylhomocysteinase
Q8X902
-
S-ribosylhomocysteinase
-
-
S-ribosylhomocysteinase
A6XJQ9
-
S-ribosylhomocysteinase
-
-
S-ribosylhomocysteinase
Q9Z5X1
-
S-ribosylhomocysteinase
Vibrio harveyi BB170
-
-
-
S-ribosylhomocysteine lyase
O34667
-
S-ribosylhomocysteine lyase
Bacillus subtilis 168
O34667
-
-
S-ribosylhomocysteine lyase
P45578
-
S-ribosylhomocysteine lyase
Q8X902
-
S-ribosylhomocysteine lyase
Q9Z5X1
-
S-ribosylhomocysteinelyase
Q81KF3
-
S-ribosylhomocysteinelyase
Q816N5
-
S-ribosylhomocysteinelyase
Q5WDW1
-
S-ribosylhomocysteinelyase
O34667
-
S-ribosylhomocysteinelyase
Q8G568
-
S-ribosylhomocysteinelyase
Q9PN97
-
S-ribosylhomocysteinelyase
Q0SWJ6
-
S-ribosylhomocysteinelyase
Q1IW42
-
S-ribosylhomocysteinelyase
Q9RRU8
-
S-ribosylhomocysteinelyase
Q8X902
-
S-ribosylhomocysteinelyase
P44007
-
S-ribosylhomocysteinelyase
Q9ZMW8
-
S-ribosylhomocysteinelyase
Q5FK48
-
S-ribosylhomocysteinelyase
Q74HV0
-
S-ribosylhomocysteinelyase
Q5QHW1
-
S-ribosylhomocysteinelyase
A1SZZ2
-
S-ribosylhomocysteinelyase
Q83JZ4
-
S-ribosylhomocysteinelyase
Q6GEU1
-
S-ribosylhomocysteinelyase
Q8CNI0
-
S-ribosylhomocysteinelyase
Q8DVK8
-
S-ribosylhomocysteinelyase
P0C0C7
-
S-ribosylhomocysteinelyase
Q72IE6
-
S-ribosylhomocysteinelyase
Q9KUG4
-
VhLuxS
Q9Z5X1
-
CAS REGISTRY NUMBER
COMMENTARY
37288-63-4
not distinguished from EC 3.2.1.148, formerly 3.3.1.3
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Actinobacillus pleuropneumoniae 4074
strain 4074
-
-
Manually annotated by BRENDA team
isolate SSU
Uniprot
Manually annotated by BRENDA team
strain CCUG 30811T
-
-
Manually annotated by BRENDA team
Alishewanella fetalis CCUG 30811T
strain CCUG 30811T
-
-
Manually annotated by BRENDA team
strain 168, BSIP1758 mutant lacking luxS
SwissProt
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168, BSIP1758 mutant lacking luxS
SwissProt
Manually annotated by BRENDA team
strain 81-176
UniProt
Manually annotated by BRENDA team
Campylobacter jejuni 81-176
strain 81-176
UniProt
Manually annotated by BRENDA team
strain TX1
UniProt
Manually annotated by BRENDA team
Edwardsiella tarda TX1
strain TX1
UniProt
Manually annotated by BRENDA team
strain NCPPB1665 (Ea1665)
-
-
Manually annotated by BRENDA team
Erwinia amylovora NCPPB1665 (Ea1665)
strain NCPPB1665 (Ea1665)
-
-
Manually annotated by BRENDA team
EHEC, O157:H7
SwissProt
Manually annotated by BRENDA team
strain O157:H7
-
-
Manually annotated by BRENDA team
strains ATCC 55730, LTH6560, and 100-23C
Q2F7Q0
UniProt
Manually annotated by BRENDA team
no activity in Agrobacterium tumefaciens
-
-
-
Manually annotated by BRENDA team
no activity in Alphaproteobacteria
-
-
-
Manually annotated by BRENDA team
no activity in Bacteroidetes
-
-
-
Manually annotated by BRENDA team
no activity in Desulfovibrio desulfuricans
-
-
-
Manually annotated by BRENDA team
no activity in Enterobacter aerogenes
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella pneumoniae
-
-
-
Manually annotated by BRENDA team
no activity in Marinomonas sp.
-
-
-
Manually annotated by BRENDA team
no activity in Marinomonas sp. MED121
-
-
-
Manually annotated by BRENDA team
no activity in Neptuniibacter caesariensis
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa
-
-
-
Manually annotated by BRENDA team
no activity in Rhodobacter capsulatus
-
-
-
Manually annotated by BRENDA team
no activity in Rhodobacter sphaeroides strain 2.4.1
-
-
-
Manually annotated by BRENDA team
no activity in Salmonella typhimurium
-
-
-
Manually annotated by BRENDA team
no activity in Sinorhizobium meliloti
-
-
-
Manually annotated by BRENDA team
no activity in Vibrio vulnificus
-
-
-
Manually annotated by BRENDA team
no activity in Zymomonas mobilis
-
-
-
Manually annotated by BRENDA team
Serratia kiliensis
-
-
-
Manually annotated by BRENDA team
Serratia malilotii
-
-
-
Manually annotated by BRENDA team
Serratia putrefaciens
-
-
-
Manually annotated by BRENDA team
strain DSM 9167T
-
-
Manually annotated by BRENDA team
strain LMG 20552T
-
-
Manually annotated by BRENDA team
Shewanella fidelis LMG 20552T
strain LMG 20552T
-
-
Manually annotated by BRENDA team
strain LMG 18921T
-
-
Manually annotated by BRENDA team
Shewanella frigidimarina LMG 18921T
strain LMG 18921T
-
-
Manually annotated by BRENDA team
strain DT-1
-
-
Manually annotated by BRENDA team
Shewanella hafniensis DT-1
strain DT-1
-
-
Manually annotated by BRENDA team
strain LMG 19691T
-
-
Manually annotated by BRENDA team
Shewanella japonica LMG 19691T
strain LMG 19691T
-
-
Manually annotated by BRENDA team
strain LMG 21403T
-
-
Manually annotated by BRENDA team
Shewanella marinintestina LMG 21403T
strain LMG 21403T
-
-
Manually annotated by BRENDA team
strain MR-1
-
-
Manually annotated by BRENDA team
strain MR-1, ATCC 700500T
-
-
Manually annotated by BRENDA team
strain LMG 21408T
-
-
Manually annotated by BRENDA team
Shewanella sairae LMG 21408T
strain LMG 21408T
-
-
Manually annotated by BRENDA team
strain LMG 21406T
-
-
Manually annotated by BRENDA team
Shewanella schlegeliana LMG 21406T
strain LMG 21406T
-
-
Manually annotated by BRENDA team
strain RN6390B
-
-
Manually annotated by BRENDA team
Staphylococcus aureus RN6390B
strain RN6390B
-
-
Manually annotated by BRENDA team
serotypes M1 and M19
-
-
Manually annotated by BRENDA team
serotype 2, strain HA9801
-
-
Manually annotated by BRENDA team
strain ATCC 33787 and isolate MVP01
UniProt
Manually annotated by BRENDA team
strain MVP01
-
-
Manually annotated by BRENDA team
Vibrio alginolyticus MVP01
strain MVP01
-
-
Manually annotated by BRENDA team
strain BB170
-
-
Manually annotated by BRENDA team
strains BB170 ATCC BAA1117 and BB152 ATCC BAA1119
-
-
Manually annotated by BRENDA team
Vibrio harveyi BB170
strain BB170
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q9PN97
mutation affects motility/flagella formation/metabolism
malfunction
Q0SWJ6
mutation affects toxin production
malfunction
Q8X902
mutation affects motility/flagella formation/metabolism
malfunction
P44007
mutation affects biofilm formation
malfunction
Q9ZMW8
mutation affects motility/flagella formation/metabolism
malfunction
Q83JZ4
mutation affects toxin production
malfunction
Q6GEU1
mutation affects motility/flagella formation/metabolism
malfunction
Q8CNI0
mutation affects biofilm formation
malfunction
Q8DVK8
mutation affects biofilm formation
malfunction
P0C0C7
mutation affects toxin production
malfunction
Q9KUG4
mutation affects toxin production
physiological function
-
produces precursor of type 2 autoinducer for bacterial cell-cell communication
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
P45578
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
-
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
O34667
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
-
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
Q9Z5X1
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
Q8X902
-
-
-
?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
Bacillus subtilis 168
O34667
-
-
-
?
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Vibrio harveyi, Vibrio harveyi BB170
-
-
the autoinducer Al-2, a five-carbon furanone results from the spontaneous cyclization of 4,5-dihydroxy-2,3-pentanedione
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
O34667
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-, B1PWE7
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Q2F7Q0
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
A1Z1R8
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Serratia malilotii, Serratia kiliensis, Serratia odorifera, Serratia putrefaciens
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Q3I354
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
A6XJQ9
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
B4XQ50, -
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Q1KMU6
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Q003Y1
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Q2PA28
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
mechanism
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
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
show the reaction diagram
-
key step in biosynthesis pathway of type II autoinducer AI-2
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
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
show the reaction diagram
Shewanella frigidimarina LMG 18921T, Shewanella sairae LMG 21408T, Shewanella fidelis LMG 20552T, Shewanella marinintestina LMG 21403T, Shewanella japonica LMG 19691T
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Edwardsiella tarda TX1
B4XQ50
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Alishewanella fetalis CCUG 30811T
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Erwinia amylovora NCPPB1665 (Ea1665)
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Actinobacillus pleuropneumoniae 4074
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Campylobacter jejuni 81-176
Q3I354
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Vibrio alginolyticus MVP01
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Shewanella schlegeliana LMG 21406T, Shewanella hafniensis DT-1
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
P45578
-
-
-
?
S-ribosylhomocysteine
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
-
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
show the reaction diagram
Q9Z5X1
-
-
-
?
S-ribosylhomocysteine
L-homocysteine + (S)-4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
assay at pH 7.0, 23C
-
-
?
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
L-homocysteine + ?
show the reaction diagram
-
-
-
-
?
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
-
-
-
additional information
?
-
-
growth phase regulation of flaA expression in Helicobacter pylori is luxS-dependent
-
-
-
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
?
-
-
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 affects both luminescence regulation and colonization competence - however its quantitative contribution is small when compared to that of the AinS signal
-
-
-
additional information
?
-
-
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
-
additional information
?
-
Q1KMU6
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
-
additional information
?
-
Q003Y1
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
-
additional information
?
-
Q2PA28
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 is functional in the autoinducer-2-mediated quorum sensing and may regulate different behaviors including biofilm formation and virulence
-
-
-
additional information
?
-
-
LuxS is involved in the activated methyl cycle and influences biofilm formation
-
-
-
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
-
additional information
?
-
-
LuxS plays an important role in the regulation of motility and flagella biogenesis
-
-
-
additional information
?
-
A6XJQ9
the LuxS quorum sensing system plays an important role in regulating the expression of virulence factors
-
-
-
additional information
?
-
Staphylococcus aureus RN6390B
-
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
?
-
Erwinia amylovora NCPPB1665 (Ea1665)
-
LuxS catalyzes the last step in the production of autoinducer-2
-
-
-
additional information
?
-
Actinobacillus pleuropneumoniae 4074
-
LuxS is functional in the autoinducer-2-mediated quorum sensing and may regulate different behaviors including biofilm formation and virulence
-
-
-
additional information
?
-
Vibrio alginolyticus MVP01
-
LuxS plays an important role in the regulation of motility and flagella biogenesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
-
the autoinducer Al-2, a five-carbon furanone results from the spontaneous cyclization of 4,5-dihydroxy-2,3-pentanedione
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
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
show the reaction diagram
-
key step in biosynthesis pathway of type II autoinducer AI-2
-
-
?
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
-
the enzyme is required for AI-2 synthesis, important metabolic function in recycling of S-adenosylhomocysteine
-
-
?
S-ribosylhomocysteine
homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
Vibrio harveyi BB170
-
-
the autoinducer Al-2, a five-carbon furanone results from the spontaneous cyclization of 4,5-dihydroxy-2,3-pentanedione
-
?
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
-
-
-
additional information
?
-
-
growth phase regulation of flaA expression in Helicobacter pylori is luxS-dependent
-
-
-
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
?
-
-
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 catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
-
additional information
?
-
Q1KMU6
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
-
additional information
?
-
Q003Y1
LuxS catalyzes production of the AI-2 autoinducer molecule for a second quorum sensing system
-
-
-
additional information
?
-
Q2PA28
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 is functional in the autoinducer-2-mediated quorum sensing and may regulate different behaviors including biofilm formation and virulence
-
-
-
additional information
?
-
-
LuxS is involved in the activated methyl cycle and influences biofilm formation
-
-
-
additional information
?
-
-
LuxS is required for normal biofilm development
-
-
-
additional information
?
-
-
LuxS plays an important role in the regulation of motility and flagella biogenesis
-
-
-
additional information
?
-
A6XJQ9
the LuxS quorum sensing system plays an important role in regulating the expression of virulence factors
-
-
-
additional information
?
-
Staphylococcus aureus RN6390B
-
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
?
-
Erwinia amylovora NCPPB1665 (Ea1665)
-
LuxS catalyzes the last step in the production of autoinducer-2
-
-
-
additional information
?
-
Actinobacillus pleuropneumoniae 4074
-
LuxS is functional in the autoinducer-2-mediated quorum sensing and may regulate different behaviors including biofilm formation and virulence
-
-
-
additional information
?
-
Vibrio alginolyticus MVP01
-
LuxS plays an important role in the regulation of motility and flagella biogenesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
; Co2+ substitution produces a highly stable enzyme
Co2+
Q9Z5X1
; Co2+ substitution produces a highly stable enzyme
Co2+
-
Co2+ substitution produces a highly stable enzyme
Fe(III)
-
Fe(III) upregulates expression of luxS and Fe(III) strongly enhances biofilm formation at concentrations above 50 microM
Fe2+
-
contains
Fe2+
-
; acts as a Lewis acid
Fe2+
Q9Z5X1
; acts as a Lewis acid
Fe2+
-
acts as a Lewis acid
Zinc
-
zinc-dependent metalloenzyme, each active site contains a zinc ion coordinated by the conserved residues His54, His58 and Cys126, and includes residues from both subunits
Zn2+
-
the metal center is composed of a Zn2+ atom coordinated by two histidines, a cysteine, and a solvent molecule
Zn2+
-
Zn2+ substitution produces an enzyme with 10fold lower activity
Zn2+
Q9Z5X1
Zn2+ substitution produces an enzyme with 10fold lower activity
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
additional information
-
to gain insight into the catalytic mechanism of the unusual reaction and the function of the metal cofactor, an efficient expression and purification system is developed to produce LuxS enriched in either Fe2+, Co2+ or Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
-
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
Q9Z5X1
-
(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
-
-
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
Q9Z5X1
-
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
-
(2S)-2-amino-6-(N-formyl-N-hydroxyamino)hexanoic acid
-
-
D-erythronohydroxamic acid
-
-
D-erythronohydroxamic acid
Q9Z5X1
-
D-erythronohydroxamic acid
-
-
D-ribosylornithine
-
-
S-(1-amino-1,4-anhydro-1,5-dideoxy-D-ribitol-5-yl)-L-homocysteine
-
inhibition of Co(II)-substituted enzyme
S-(3,5-dideoxy-3-fluoro-1-O-methyl-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(3,5-dideoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(3,5-dideoxy-D-erythro-pentofuranos-5-yl)homocysteine
-
-
S-(4-amino-4,5-dideoxy-alpha/beta-D-ribofuranos-5-yl)-L-homocysteine
-
inhibition of Co(II)-substituted enzyme. The hemiaminal may undergo ring opening to form an aldehyde which may undergo the aldose-ketose isomerization reaction to form a 2-ketone, which presumably binds to the LuxS active site with higher affinity than the original ribose analogue
S-(4-amino-4,5-dideoxy-D-ribono-1,4-lactam-5-yl)-L-homocysteine
-
inhibition of Co(II)-substituted enzyme
S-(5-deoxy-3-deoxy-3-bromo-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(5-deoxy-3-deoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-(5-deoxy-3-O-methyl-D-ribofuranos-5-yl)homocysteine
-
-
S-(5-deoxy-3-O-methyl-D-xylofuranos-5-yl)homocysteine
-
-
S-(5-deoxy-D-xylofuranos-5-yl)-L-homocysteine
-
-
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
-
S-[3-fluoro-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
-
additional information
-
5,6,7,8,9-pentadeoxy-6-fluoro-D-ribo-dec-5(Z)-enofuranuronate a S-ribosylhomocysteine analogue and 5,6-dideoxy-6-fluoro-D-ribo-hex-5-enofuranose a S-ribosylhomocysteine analogue have no inhibitory activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
D-glucose
B4XQ50, -
expression of LuxS is increased by 0.5% (w/v) D-glucose
additional information
-
luxS expression is not regulated by autoinducer-2, modulation of luxS expression levels allows adjusting bacterial fitness in response to changing host conditions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0036
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
0.027
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
0.041
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme S6A
0.098
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme E57A
0.15
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme R39M
0.52
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme H11Q
0.7
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme C83A
0.0014
-
S-ribosylhomocysteine
-
-
0.0019
-
S-ribosylhomocysteine
-
Fe2+ containing BsLuxS
0.0023
-
S-ribosylhomocysteine
-
Co2+ substituted BsLuxS
0.0023
-
S-ribosylhomocysteine
-
wild type enzyme
0.0025
-
S-ribosylhomocysteine
-
native enzyme
0.016
-
S-ribosylhomocysteine
-
C41A mutant; wild type enzyme
0.016
-
S-ribosylhomocysteine
-
Co2+ substitued enzyme
0.037
-
S-ribosylhomocysteine
-
wild type enzyme
0.039
-
S-ribosylhomocysteine
-
-
0.039
-
S-ribosylhomocysteine
Q9Z5X1
Co2+ substituted VhLuxS
0.041
-
S-ribosylhomocysteine
-
mutant enzyme S6A
0.058
-
S-ribosylhomocysteine
-
Zn2+ substituted BsLuxS
0.18
-
S-ribosylhomocysteine
-
mutant enzyme E57D
0.73
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme E57D
additional information
-
additional information
-
KM-values of enzyme forms enriched in either Fe2+, Co2+ or Zn2+
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme E57A
0.016
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme R39M
0.022
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme C83A
0.024
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme H11Q
0.026
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme E57D
0.038
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
0.14
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
mutant enzyme S6A
0.4
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
0.027
-
S-ribosylhomocysteine
-
mutant enzyme S6A
0.03
-
S-ribosylhomocysteine
-
-
0.03
-
S-ribosylhomocysteine
-
wild type enzyme
0.4
-
S-ribosylhomocysteine
-
-
0.4
-
S-ribosylhomocysteine
-
wild type enzyme
0.64
-
(2R)-2-amino-4-[[(2S,4S)-2,4,5-trihydroxy-3-oxopentyl]sulfanyl]butanoic acid
-
wild type enzyme
additional information
-
additional information
-
turnover numbers of enzyme forms enriched in either Fe2+, Co2+ or Zn2+
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00037
-
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Co2+ substituted enzyme
0.00043
-
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Fe2+ substituted enzyme
0.0106
-
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Zn2+ substituted enzyme
0.0127
-
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Co2+ substituted enzyme
0.0128
-
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
Q9Z5X1
Co2+ substituted enzyme
0.00072
-
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Co2+ substituted enzyme; Fe2+ substituted enzyme
0.0032
-
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Co2+ substituted enzyme
0.0097
-
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
Q9Z5X1
Co2+ substituted enzyme
0.0196
-
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
Zn2+ substituted enzyme
0.147
-
D-erythronohydroxamic acid
-
Fe2+ substituted enzyme
0.156
-
D-erythronohydroxamic acid
-
Co2+ substituted enzyme
0.55
-
D-erythronohydroxamic acid
Q9Z5X1
Co2+ substituted enzyme
0.72
-
D-erythronohydroxamic acid
-
Co2+ substituted enzyme
2.4
-
D-erythronohydroxamic acid
-
Zn2+ substituted enzyme
0.068
-
D-ribosylornithine
-
Co2+ substituted enzyme
0.061
-
methionine
-
Co2+ substituted enzyme
0.048
-
S-(1-amino-1,4-anhydro-1,5-dideoxy-D-ribitol-5-yl)-L-homocysteine
-
pH 7.0, 22C
0.042
-
S-(3,5-dideoxy-3-fluoro-1-O-methyl-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.0077
-
S-(3,5-dideoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.055
-
S-(3,5-dideoxy-D-erythro-pentofuranos-5-yl)homocysteine
-
pH 7.0, 23C
0.0035
-
S-(4-amino-4,5-dideoxy-alpha/beta-D-ribofuranos-5-yl)-L-homocysteine
-
pH 7.0, 22C
0.037
-
S-(4-amino-4,5-dideoxy-D-ribono-1,4-lactam-5-yl)-L-homocysteine
-
pH 7.0, 22C
0.0079
-
S-(5-deoxy-3-deoxy-3-bromo-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.0106
-
S-(5-deoxy-3-deoxy-3-fluoro-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.042
-
S-(5-deoxy-3-O-methyl-D-ribofuranos-5-yl)homocysteine
-
pH 7.0, 23C
0.066
-
S-(5-deoxy-3-O-methyl-D-xylofuranos-5-yl)homocysteine
-
pH 7.0, 23C
0.0042
-
S-(5-deoxy-D-xylofuranos-5-yl)-L-homocysteine
-
pH 7.0, 23C
0.0079
-
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
wild type enzyme
0.047
-
S-[3-bromo-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
wild type enzyme
0.0106
-
S-[3-fluoro-3,5-dideoxy-D-ribofuranos-5-yl]-L-homocysteine
-
wild type enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
luxS expression is detectable only at the base of fruiting bodies
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Helicobacter pylori (strain J99 / ATCC 700824)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homodimer
-
3 * 12500
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Co2+-substituted BsLuxS is cocrystallized with inhibitors (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid and (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid by the hanging drop vapor diffusion method
-
hanging drop vapor diffusion, inactive mutant C84A of Co2+-substituted LuxS is cocrystallized with the 2-ketone intermediate and the structure is determined to 1.8 A resolution
-
hanging-drop vapor diffusion method with ammonium sulfate as precipitant, structure at 1.6 A resolution
-
hanging-drop vapour diffusion method with ammonium sulfate as the precipitant. The crystals belong to the enantiomorphic space groups P6(1)22 or P6(5)22 with approximate unit-cell parameters A = b = 63.6, c = 151.5 A. The crystals diffract X-rays to at least 1.55 A resolution on a synchrotron-radiation source
-
structure of LuxS is determined at 1.2 A resolution, together with the binary complexes of LuxS with S-ribosylhomocysteine and homocysteine to 2.2 A and 2.3 A resolution, hanging-drop vapour diffusion method
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
B4XQ50, -
LuxS expression is decreased at 37C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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
Q9Z5X1
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the DELTAluxS mutant shows higher sensitivity to both hydrogen peroxide and cumene hydroperoxide than the wild type enzyme with consistently greater zones of inhibition
Q3I354
692435
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, when stored in the frozen form, the LuxS proteins are stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Q-Sepharose Fast-Flow column chromatography and ultrafiltration
-
Q-Sepharose Fast-Flow column chromatography and ultrafiltration
Q9Z5X1
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli DH5alpha cells
-
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
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
-
expressed in Escherichia coli DH5alpha cells
-
as lsrR knockout by chromosomal gene replacement
Q8X902
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
-
expressed in Escherichia coli DH5alpha cells
-
expressed in Escherichia coli DH5alpha cells
-
mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms; mutant LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms
Q9Z5X1
overexpression as glutathione-S-transferase fusion in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Fe(III) upregulates expression of luxS and Fe(III) strongly enhances biofilm formation at concentrations above 50 microM
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C84A
-
no catalytic activity
C84D
-
more than 220fold reduced activity
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
C41A
-
by site directed mutagenesis
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
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
Actinobacillus pleuropneumoniae 4074
-
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
-, B1PWE7
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
Y89F
-
by site directed mutagenesis
additional information
Q3I354
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
Campylobacter jejuni 81-176
-
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
Erwinia amylovora NCPPB1665 (Ea1665)
-
inactivation of the luxS gene impairs motility, extracellular polysaccharide production, and tolerance for hydrogen peroxide, and reduces virulence on pear leaves
-
C83D
-
by site directed mutagenesis
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
-
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
-
inactive luxS leads to decreased virulence in Vibrio alginolyticus
additional information
A6XJQ9
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
Vibrio alginolyticus MVP01
-
inactive luxS leads to decreased virulence in Vibrio alginolyticus
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
Q8X902
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