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Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase and Organism(s) Limosilactobacillus reuteri and UniProt Accession Q5QHW1

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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Limosilactobacillus reuteri
UNIPROT: Q5QHW1
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Word Map
The taxonomic range for the selected organisms is: Limosilactobacillus reuteri
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
luxs protein, s-ribosylhomocysteinase, ai-2 synthase, s-ribosylhomocysteine lyase, autoinducer-2 synthase, s-ribosylhomocysteinelyase, s-ribosyl homocysteinase, more
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
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
transcriptomic and metabolomic changes of wild-type enzyme and an insertional knockout mutant strains, especially expression of lipoproteins of the YaeC family and cysteine synthase are affected, overview
physiological function
two potential roles for the enzyme, the first is in the production of autoinducer-2, mediating quorum sensing, and the second is as an enzyme in the activated methyl cycle, where it catalyzes the conversion of S-ribosylhomocysteine to homocysteine. The by-product of the reaction catalyzed by the enzyme is (S)-4,5-dihydroxy-2,3-pentanedione, which spontaneously forms the furanones known collectively as autoinducer-2, AI-2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LUXS_LIMRT
158
0
17727
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jelcic, I.; Huefner, E.; Schmidt, H.; Hertel, C.
Repression of the locus of the enterocyte effacement-encoded regulator of gene transcription of Escherichia coli O157:H7 by Lactobacillus reuteri culture supernatants is LuxS and strain dependent
Appl. Environ. Microbiol.
74
3310-3314
2008
Limosilactobacillus reuteri (Q2F7Q0)
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
Wilson, C.M.; Aggio, R.B.; OToole, P.W.; Villas-Boas, S.; Tannock, G.W.
Transcriptional and metabolomic consequences of LuxS inactivation reveal a metabolic rather than quorum-sensing role for LuxS in Lactobacillus reuteri 100-23
J. Bacteriol.
194
1743-1746
2012
Limosilactobacillus reuteri (B3XKW0), Limosilactobacillus reuteri, Limosilactobacillus reuteri 100-23 (B3XKW0)
Manually annotated by BRENDA team