2.7.1.189: autoinducer-2 kinase
This is an abbreviated version!
For detailed information about autoinducer-2 kinase, go to the full flat file.
Word Map on EC 2.7.1.189
-
2.7.1.189
-
quorum
-
cell-cell
-
interspecies
-
repressor
-
chemotaxis
-
amp
-
prevailing
-
typhimurium
-
envision
-
quorum-sensing
-
fight
-
drug development
- 2.7.1.189
-
quorum
-
cell-cell
-
interspecies
- repressor
-
chemotaxis
- amp
-
prevailing
- typhimurium
-
envision
-
quorum-sensing
-
fight
- drug development
Reaction
Synonyms
AI-2 kinase, AI-2 processing kinase, Lsr kinase, lsrK, LsrK kinase
ECTree
Advanced search results
Inhibitors
Inhibitors on EC 2.7.1.189 - autoinducer-2 kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
2,3,4,5-tetrachloro-6-(2,3,4,5-tetrachloroanilino)benzoic acid
-
2-(1,3-benzothiazol-2-yl)-5-(5-methylfuran-2-yl)-3-oxopentanenitrile
-
2-(3-chloro-2-methylanilino)benzoic acid
-
2-(3-chloroanilino)benzoic acid
-
2-(4-chloroanilino)benzoic acid
-
2-anilino-4-chlorobenzoic acid
-
2-[2-chloro-5-(trifluoromethyl)anilino]-5-methoxybenzoic acid
-
7-dehydroxypryogallin-4-carboxylic acid
-
HPr
a phosphocarrier protein central to the sugar phosphotransferase system of Escherichia coli. HPr copurifies with LsrK. LsrK activity is inhibited when bound to HPr. HPr inhibited LsrK activity in a mixed manner of competitive and uncompetitive, not via competitive or uncompetitive inhibition alone. Phosphorylation of HPr reduces its inhibitory effect on LsrK
-
HPr H15A
the HPr H15A mutant displays almost no inhibition of the enzyme
-
HPr H15E
the HPr H15E mutant displays several times lower inhibition compared to the wild-type
-
rosolic acid
rosolic acid positively stabilizes His-LsrK in thermal shift at high concentrations, suggesting a low affnity binding interaction between the two, high target specificity
[(3-chloro-2-methylphenyl)amino]benzoic acid
-
structure-based virtual screening of LsrK kinase inhibitors to target quorum sensing, overview. LsrK 3D modeling and virtual screening of a locally available database. Identified LsrK inhibitors can be further optimized as antivirulence agents
-
additional information
poor inhibition by aurin tricarboxylic acid
-