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Research Article

In silico studies of urease inhibitors to explore ligand-enzyme interactions

, , , &
Pages 151-156 | Received 11 Oct 2007, Accepted 07 Jan 2008, Published online: 20 Oct 2008

Figures & data

Scheme 1.  General scheme for the synthesis of compounds 17 and their in vitro Jack bean urease inhibitory activities.

Scheme 1.  General scheme for the synthesis of compounds 1–7 and their in vitro Jack bean urease inhibitory activities.

Figure 1.  Compound 1 into the active site of urease. The molecule in gray is the ligand with the active site residues. Metals are represented in green.

Figure 1.  Compound 1 into the active site of urease. The molecule in gray is the ligand with the active site residues. Metals are represented in green.

Figure 2.  Compound 4 into the active site of urease. The lignad is represented as a ball and stick model.

Figure 2.  Compound 4 into the active site of urease. The lignad is represented as a ball and stick model.

Figure 3.  Superimposition of the docking pose of 6a (tan), 6b (gray), 7a (green) 7b (white) showing the difference in the orientation of ring B in the catalytic core of urease. Additionally the active site of urease clearly demonstrating the role of Asp224 and Cys322. The ligands are represented as a ball and stick model.

Figure 3.  Superimposition of the docking pose of 6a (tan), 6b (gray), 7a (green) 7b (white) showing the difference in the orientation of ring B in the catalytic core of urease. Additionally the active site of urease clearly demonstrating the role of Asp224 and Cys322. The ligands are represented as a ball and stick model.

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