Corrections to Discovery of Leukotriene A4 Hydrolase Inhibitors Using Metabolomics Biased Fragment...
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2330 J. Med. Chem. 2010, 53, 2330–2331 Corrections to Discovery of Leukotriene A4 Hydrolase Inhibi- tors Using Metabolomics Biased Fragment Crystallography [J. Med. Chem. 2009, 52, 4694. DOI: 10.1021/jm900259h]. Douglas R. Davies, Bjorn Mamat, Olafur T. Magnusson, Jeff Christensen, Magnus H. Haraldsson, Rama Mishra, Brian Pease, Erik Hansen, Jasbir Singh, David Zembower, Hidong Kim, Alex S. Kiselyov, Alex B. Burgin, Mark E. Gurney, and Lance J. Stewart* Page 4702. In Figure 2, the chemical structure of compound 19 (DG-051) was incorrectly drawn as the (R)-enantiomer. Compound 19 is the (S)-enantiomer and is properly shown in the three-dimensional crystal structure image at the right- hand side in the corrected figure below. On page 4704, right hand column, first paragraph, line 19 and second paragraph line 22, (R)-prolinol should be changed to (S )-prolinol. Supporting Information Page S16. In Table 2, the chemical structure of compound 19 (DG-051) was incorrectly drawn as the (R)-enantiomer. The correct (S)-enantiomer has been included in the revised version of Supplemental Table 2 below. DOI: 10.1021/jm100015w Published on Web 02/12/2010 Figure 2. Panels showing ligand binding to LTA4H for compounds described in the manuscript. Enzyme assay IC 50 values are in μM, human whole blood cell assay IC 50 values are in nM when reported, and ligand efficiency (LE) values are in kcal/(mol 3 heavy atom). Compound structures are displayed as yellow stick structures, and LTA4H is displayed in gray. Green mesh corresponds to the F o - F c (difference) electron density at the 3.0σ level of the crystal structure with the compound omitted from the model. Polar contacts with LTA4H and/or bound water molecules are shown as red dashed lines. PDB IDs for each structure are indicated.
Transcript of Corrections to Discovery of Leukotriene A4 Hydrolase Inhibitors Using Metabolomics Biased Fragment...
2330 J. Med. Chem. 2010, 53, 2330–2331
Corrections to Discovery of Leukotriene A4 Hydrolase Inhibi-
tors Using Metabolomics Biased Fragment Crystallography
[J. Med. Chem. 2009, 52, 4694. DOI: 10.1021/jm900259h].
Douglas R. Davies, Bjorn Mamat, Olafur T. Magnusson,
Jeff Christensen, Magnus H. Haraldsson, Rama Mishra,
Brian Pease, Erik Hansen, Jasbir Singh, David Zembower,
HidongKim,AlexS.Kiselyov,AlexB.Burgin,MarkE.Gurney,
and Lance J. Stewart*
Page 4702. InFigure 2, the chemical structure of compound
19 (DG-051) was incorrectly drawn as the (R)-enantiomer.
Compound 19 is the (S)-enantiomer and is properly shown in
the three-dimensional crystal structure image at the right-
hand side in the corrected figure below.
On page 4704, right hand column, first paragraph, line 19
and second paragraph line 22, (R)-prolinol should be changed
to (S )-prolinol.
Supporting Information Page S16. In Table 2, the chemical
structure of compound 19 (DG-051) was incorrectly drawn as
the (R)-enantiomer. The correct (S)-enantiomer has been
included in the revised version of Supplemental Table 2 below.
DOI: 10.1021/jm100015w
Published on Web 02/12/2010
Figure 2. Panels showing ligand binding to LTA4H for compounds described in the manuscript. Enzyme assay IC50 values are in μM, humanwhole blood cell assay IC50 values are in nM when reported, and ligand efficiency (LE) values are in kcal/(mol 3heavy atom). Compoundstructures are displayed as yellow stick structures, andLTA4H is displayed in gray.Greenmesh corresponds to theFo-Fc (difference) electrondensity at the 3.0σ level of the crystal structure with the compound omitted from the model. Polar contacts with LTA4H and/or bound watermolecules are shown as red dashed lines. PDB IDs for each structure are indicated.
Additions and Corrections Journal of Medicinal Chemistry, 2010, Vol. 53, No. 5 2331
Supplemental Table 2. Comparative IC50 data for peptidase, hydrolase, and HWB assays.
SupplementalTable 2.Comparative IC50 data for peptidase, hydrolase, andHWBassays.For all compound structures described in thiswork, inhibitionassays were carried out using at least two independent methods, either the hydrolase assay, peptidase assay and/or a hydrolase assay in human wholeblood. SeeMaterials andMethods section for details. All results are given as IC50 values in μM, with the number of replicates and the standard error ofthe mean indicated where applicable.
