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Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase and Organism(s) Streptococcus suis

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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Streptococcus suis
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The taxonomic range for the selected organisms is: Streptococcus suis
The enzyme appears in selected viruses and cellular organisms
Synonyms
AI-2 synthase, autoinducer-2 synthase, BsLuxS, EcLuxS, lsrR, Lux S, LuxS, LuxS protein, S-ribosyl homocysteinase, S-ribosylhomocysteinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AI-2 synthase
autoinducer-2 synthase
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
calculated molar ratio of Zn2+ ion to each LuxS monomer is about 1:1
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0164 - 0.0708
S-ribosylhomocysteine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.102
S-ribosylhomocysteine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.149 - 6.21
S-ribosylhomocysteine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
inactivation of luxS gene leads to a wide range of phenotypic changes including thinner capsular walls, increased tolerance to H2O2, reduced adherence capacity to epithelial cells. In particular, loss of LuxS impairs dramatically full virulence of serotype 2 in experimental model of piglets, and functional complementation restores virulence nearly to the level of parent strain
physiological function
the enzyme is required for synthesis of autoinducer 2, a signaling molecule for inter-species quorum sensing. Cell adherence analyses with human laryngeal epithelial cell line Hep-2 and human umbilical vein endothelial cells
additional information
modeling of enzyme protein structure and luxS-mediated global regulation using the genome-wide microarray analyses, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A4T2GKV5_STRSU
160
0
17972
TrEMBL
A0A426TJ97_STRSU
160
0
17931
TrEMBL
A0A0Z8NLD7_STRSU
160
0
18021
TrEMBL
B2CMA5_STRSU
160
0
17991
TrEMBL
A0A0N0DLR5_STRSU
160
0
17977
TrEMBL
A0A0Z8V0H5_STRSU
160
0
17990
TrEMBL
A0A3S6K1W8_STRSU
160
0
17973
TrEMBL
A0A4T2GT31_STRSU
160
0
18005
TrEMBL
A0A0Z8KZ02_STRSU
160
0
18003
TrEMBL
A0A123U4R3_STRSU
160
0
17981
TrEMBL
A0A3R8RAM6_STRSU
160
0
18090
TrEMBL
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.93 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C82A
inactive, mutation decreases autoinducer AI-2 production and biofilm formation
C82S
43fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
F80M
7fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
F80M/H87Y
42fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
H87Y
37fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
C82A
-
inactive, mutation decreases autoinducer AI-2 production and biofilm formation
C82S
-
43fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
F80M
-
7fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
F80M/H87Y
-
42fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
H87Y
-
37fold decrease in activity, mutation decreases autoinducer AI-2 production and biofilm formation
additional information
generation of a luxS null mutant of 05ZYH33 strain is obtained by homologous recombination
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha cells
-
expression in Escherichia coli
gene luxS, sequence comparisons, expression and transcriptome analysis of wild-type and enzyme knockout mutant strains
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, X.G.; Lu, C.P.
Detection of autoinducer-2 and analysis of the profile of luxS and pfs transcription in Streptococcus suis serotype 2
Curr. Microbiol.
58
146-152
2009
Streptococcus suis
Manually annotated by BRENDA team
Cao, M.; Feng, Y.; Wang, C.; Zheng, F.; Li, M.; Liao, H.; Mao, Y.; Pan, X.; Wang, J.; Hu, D.; Hu, F.; Tang, J.
Functional definition of LuxS, an autoinducer-2 (AI-2) synthase and its role in full virulence of Streptococcus suis serotype 2
J. Microbiol.
49
1000-1011
2011
Streptococcus suis 05ZYH33 (A4VTE8), Streptococcus suis (A4VTE8)
Manually annotated by BRENDA team
Wang, Y.; Yi, L.; Wang, S.; Fan, H.; Ding, C.; Mao, X.; Lu, C.
Crystal structure and identification of two key amino acids involved in AI-2 production and biofilm formation in Streptococcus suis LuxS
PLoS ONE
10
e0138826
2015
Streptococcus suis (B2CMA5), Streptococcus suis
Manually annotated by BRENDA team
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