BMC Biochemistry

unofficial impact factor 1.84

Open Access Highly Access Research article

Identification of inhibitors of Plasmodium falciparum phosphoethanolamine methyltransferase using an enzyme-coupled transmethylation assay

April M Bobenchik1,2, Jae-Yeon Choi3, Arunima Mishra2, Iulian N Rujan4, Bing Hao4, Dennis R Voelker3, Jeffrey C Hoch4 and Choukri B Mamoun1*

Author Affiliations

1 Department of Internal Medicine, Section of Infectious Diseases, Yale School of Medicine, 333 Cedar St., New Haven, 06052, USA

2 Department of Genetics and Developmental Biology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, 06030, USA

3 The Program in Cell Biology, Department of Medicine, National Jewish Medical and Research Center, 1400 Jackson St, Denver, 80206, USA

4 Department of Molecular, Microbial, and Structural Biology University of Connecticut Health Center, 263 Farmington Ave., Farmington, 06030, USA

For all author emails, please log on.

BMC Biochemistry 2010, 11:4 doi:10.1186/1471-2091-11-4

Published: 19 January 2010

Additional files

Additional file 1:

Fig. S1. Overlay of the full 1H-15N HSQC spectra of PfPMT in the absence (red) or presence of 0.06 (orange), 0.12 (yellow), 0.25 (green), 0.5 (blue) and 1 mM (purple) of AQ.

Format: PPT Size: 785KB Download file

This file can be viewed with: Microsoft PowerPoint Viewer

Open Data

Additional file 2:

Fig. S2. Sequence alignment of HNMT and PfPMT. Residues that are identical, conserved, and semi-conserved are indicated by asterisk, colon, and period, respectively. The AQ-interacting residues are colored as in Fig. 8B. Phe19 and Tyr198 of HNMT and their corresponding residues in PfPMT are shown in italics and bold.

Format: PPT Size: 126KB Download file

This file can be viewed with: Microsoft PowerPoint Viewer

Open Data