4.4.1.21: S-ribosylhomocysteine lyase
This is an abbreviated version!
For detailed information about S-ribosylhomocysteine lyase, go to the full flat file.
Word Map on EC 4.4.1.21
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4.4.1.21
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quorum
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quorum-sensing
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interspecies
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harveyi
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thioether
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4,5-dihydroxy-2,3-pentanedione
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nucleosidase
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luxs-dependent
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furanone
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medicine
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analysis
- 4.4.1.21
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quorum
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quorum-sensing
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interspecies
- harveyi
- thioether
- 4,5-dihydroxy-2,3-pentanedione
- nucleosidase
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luxs-dependent
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furanone
- medicine
- analysis
Reaction
Synonyms
AI-2 synthase, autoinducer-2 synthase, BsLuxS, EC 3.13.1.2, EC 3.2.1.148, EC 3.3.1.3, EcLuxS, lsrR, Lux S, LuxS, LuxS protein, S-ribosyl homocysteinase, S-ribosylhomocysteinase, S-ribosylhomocysteine lyase, S-ribosylhomocysteinelyase, VhLuxS
ECTree
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General Information
General Information on EC 4.4.1.21 - S-ribosylhomocysteine lyase
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malfunction
physiological function
additional information
malfunction
mutation affects motility/flagella formation/metabolism
malfunction
mutation affects motility/flagella formation/metabolism
malfunction
mutation affects motility/flagella formation/metabolism
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
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
malfunction
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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
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malfunction
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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
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produces precursor of type 2 autoinducer for bacterial cell-cell communication
physiological function
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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
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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
physiological function
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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
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S-ribosyl homocysteinase is a key enzyme in the formation of the signaling molecule of QS-2, autoinducer II
physiological function
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S-ribosylhomocysteinase from Streptococcus mutans plays a crucial role in the quorum-sensing system
physiological function
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the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
physiological function
the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
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
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
physiological function
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Deletion of the luxS gene increases biofilm formation, but does not affect the bacterial growth rate. Deletion of the luxS gene also increases cell-surface hydrophobicity. The luxS mutant strain tends to aggregate into distinct clusters and relatively dense structures, whereas the wild-type strain appears confluent and more evenly distributed. All genes examined are up-regulated in the biofilms formed by the luxS mutant strain
physiological function
Enterococcus faecalis ATCC 33186
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Deletion of the luxS gene increases biofilm formation, but does not affect the bacterial growth rate. Deletion of the luxS gene also increases cell-surface hydrophobicity. The luxS mutant strain tends to aggregate into distinct clusters and relatively dense structures, whereas the wild-type strain appears confluent and more evenly distributed. All genes examined are up-regulated in the biofilms formed by the luxS mutant strain
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physiological function
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the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
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physiological function
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the enzyme is required for biosynthesis of autoinducer 2, AI-2, a hormone-like molecule involved in quorum sensing, which is a cell-cell signaling mechanism based on cell density
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physiological function
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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
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physiological function
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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
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elucidation of the mechanism of the first stage of the enzyme catalytic process by docking and molecular dynamics simulations, overview. An active site water stably locates within the active site, it can facilitate ring-opening of either alpha-S-ribosylhomocysteine or beta-furanose, leading to formation of a common active-site-bound 2-keto-S-ribosylhomocysteine intermediate, without the need to pass through a linear aldose S-ribosylhomocysteine configuration. Catalytic importance of several active site residues including Ser6, His11, Arg39, Cys84, and Glu57
additional information
modeling of enzyme protein structure and luxS-mediated global regulation using the genome-wide microarray analyses, overview
additional information
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modeling of enzyme protein structure and luxS-mediated global regulation using the genome-wide microarray analyses, overview
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