EC Number   |
General Information |
Reference |
|---|
   2.3.1.184 | evolution |
ExpI is related to members of the LuxI family |
720492 |
| 2.3.1.184 | evolution |
the evolutionary history of acylhomoserine lactone synthase and acylhomoserine lactone receptor homologs in sequenced genomes and metagenomes of nitrifying bacteria is analzed |
755851 |
| 2.3.1.184 | malfunction |
a smaI mutation abolishes the synthesis of the antibiotic carbapenem, the pigment prodigiosin, and several hydrolytic enzymes, while a smaR smaI double mutant restores their production |
-, 720492 |
| 2.3.1.184 | malfunction |
an expR-virR-expI triple mutant is a phenocopy of the virR-expI double mutant, suggesting that ExpR does not play any role in regulating these genes. Exoenzyme production in a virR-expI mutant is still induced at high cell density, rather than constitutive |
720492 |
| 2.3.1.184 | malfunction |
disruption of esaI caused a sharp decrease in exopolysaccharide accumulation, and production was restored by adding N-3-oxohexanoyl-L-homoserine lactone. EsaR mutants overproduce the same exopolysaccharide, indicating that null mutations in esaR and esaI have opposite phenotypes |
720492 |
| 2.3.1.184 | malfunction |
mutation of expI abolishes production of two N-acyl-L-homoserine lactones, but does not affect the production of a third one, suggesting the existence of at least one more AHL synthase gene. Mutations of expI and expR have little effect on pectate lyase synthesis, which remains quorum-regulated |
720492 |
| 2.3.1.184 | metabolism |
acylhomoserine lactone quorum sensing is a method of bacterial communication and gene regulation. Acylhomoserine lactone synthase gene is required for, but does not guarantee, cell density-dependent acylhomoserine lactone production |
755851 |
| 2.3.1.184 | metabolism |
the enzyme is involved in biosynthesis of N-acyl homoserine lactone |
-, 757055 |
| 2.3.1.184 | more |
LuxR is an N-3-oxohexanoyl-L-homoserine lactone sensor and an N-3-oxohexanoyl-L-homoserine lactone-dependent transcriptional activator of the luciferase operon. As a population of Vibrio fischeri cells grows in density, the concentration of external N-3-oxohexanoyl-L-homoserine lactone increases. When the concentration of this signal reaches the nanomolar range, its passive efflux from the cells becomes balanced by an influx, so that it can interact with LuxR. LuxR-OHHL complexes bind the promoter of the luxICDABEG operon and activate its transcription. LuxR structure, overview. Three amino acids clustered in the C-terminal domain of LuxR are required for positive control of transcription. Molecular mechanism of action of LuxR as transcription factor, overview |
720492 |
| 2.3.1.184 | more |
molecular mechanism of action of EsaR as transcription factor, overview |
720492 |
