Literature summary for 2.3.1.230 extracted from

Storz, M.P.; Brengel, C.; Weidel, E.; Hoffmann, M.; Hollemeyer, K.; Steinbach, A.; Mueller, R.; Empting, M.; Hartmann, R.W.
Biochemical and biophysical analysis of a chiral PqsD inhibitor revealing tight-binding behavior and enantiomers with contrary thermodynamic signatures (2013), ACS Chem. Biol., 8, 2794-2801.

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Protein Variants

Protein Variants	Comment	Organism
C112S	about 8% of wild-type activtiy	Pseudomonas aeruginosa
H257F	inactive	Pseudomonas aeruginosa
S317A	activity similar to wild-type	Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism	Structure
(S)-(2-nitrophenyl)(phenyl)methanol	most active compound of the series, capable of reducing the HHQ and PQS levels as well as the biofilm volume in Pseudomonas aeruginosa PA14 without affecting cell viability. The (S)-enantiomer has a pronounced entropic binding profile. Docking results show a short hydrogen bond between NO2 and NH of Ser317. The hydroxyl group is involved in different interactions, either facing toward Asn287 or His256/Cys112	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	A0A0H2Z7U1	cf. EC 2.3.1.180	-

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0032	-	pH not specified in the publication, temperature not specified in the publication	Pseudomonas aeruginosa	(S)-(2-nitrophenyl)(phenyl)methanol

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Release 2023.1 (January 2023)