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Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase and Organism(s) Helicobacter pylori and UniProt Accession Q9ZMW8

for references in articles please use BRENDA:EC4.4.1.21
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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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Helicobacter pylori
UNIPROT: Q9ZMW8
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Word Map
The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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-ribosylhomocysteinelyase
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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
S-ribosylhomocysteine
L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
show the reaction diagram
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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
additional information
?
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growth phase regulation of flaA expression in Helicobacter pylori is luxS-dependent
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-
?
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
additional information
?
-
-
growth phase regulation of flaA expression in Helicobacter pylori is luxS-dependent
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutation affects motility/flagella formation/metabolism
physiological function
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loh, J.T.; Forsyth, M.H.; Cover, T.L.
Growth phase regulation of flaA expression in Helicobacter pylori is luxS dependent
Infect. Immun.
72
5506-5510
2004
Helicobacter pylori
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, Serratia plymuthica, Staphylococcus aureus, 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
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)
Manually annotated by BRENDA team
Doherty, N.C.; Shen, F.; Halliday, N.M.; Barrett, D.A.; Hardie, K.R.; Winzer, K.; Atherton, J.C.
In Helicobacter pylori, LuxS is a key enzyme in cysteine provision through a reverse transsulfuration pathway
J. Bacteriol.
192
1184-1192
2010
Helicobacter pylori
Manually annotated by BRENDA team