EC Number   |
General Information |
Reference |
|---|
    4.4.1.21 | 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 |
-, 730192 |
| 4.4.1.21 | malfunction |
mutation affects biofilm formation |
702928 |
| 4.4.1.21 | malfunction |
mutation affects motility/flagella formation/metabolism |
702928 |
| 4.4.1.21 | malfunction |
mutation affects toxin production |
702928 |
| 4.4.1.21 | 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 |
-, 729919 |
| 4.4.1.21 | more |
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 |
730256 |
| 4.4.1.21 | more |
modeling of enzyme protein structure and luxS-mediated global regulation using the genome-wide microarray analyses, overview |
-, 730192 |
| 4.4.1.21 | physiological function |
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 |
-, 747704 |
| 4.4.1.21 | 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) |
715165 |
| 4.4.1.21 | 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 |
715358 |
