Journal:JMB:2
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- | <applet load="Workbench_test2.pdb" size="500" color="white" frame="true" align="right" caption="rePON1 with 2HQ" scene="Journal:JMB:2/Opening/ | + | <applet load="Workbench_test2.pdb" size="500" color="white" frame="true" align="right" caption="rePON1 with 2HQ" scene="Journal:JMB:2/Opening/4" /> |
=== Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1 === | === Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1 === |
Revision as of 21:40, 19 March 2012
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Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1
Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD [1]
Molecular Tour
Previously PON1 was . The authors sought a physiologically active pH and. Note . Especially, observe the . The authors also solved PON1 at 6.5 pH in . Here, the authors for the first time observe ordered. The residues colored red ., suggesting that lactone adopt a similar position. 2HQ makes contact with()
- ↑ Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS. Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1. J Mol Biol. 2012 Mar 1. PMID:22387469 doi:10.1016/j.jmb.2012.02.042
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