Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro-Reference-Cited by-同舟云学术

Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro

Published:2015-11-26 Issue:11 Volume:90 Page:2711-2724
ISSN:0340-5761
Container-title:Archives of Toxicology
language:en
Short-container-title:Arch Toxicol

Author:

Goldsmith Moshe,Eckstein Simone,Ashani Yacov,Greisen Per,Leader Haim,Sussman Joel L.,Aggarwal Nidhi,Ovchinnikov Sergey,Tawfik Dan S.,Baker David,Thiermann Horst,Worek Franz

Funder

Defense Threat Reduction Agency

Publisher

Springer Science and Business Media LLC

Subject

Health, Toxicology and Mutagenesis,Toxicology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s00204-015-1626-2.pdf

Reference43 articles.

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3. Aurbek N, Thiermann H, Szinicz L, Eyer P, Worek F (2006) Analysis of inhibition, reactivation and aging kinetics of highly toxic organophosphorus compounds with human and pig acetylcholinesterase. Toxicology 224(1–2):91–99. doi: 10.1016/j.tox.2006.04.030

4. Ben-David M, Elias M, Filippi JJ et al (2012) Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1. J Mol Biol 418(3–4):181–196. doi: 10.1016/j.jmb.2012.02.042

5. Benning MM, Shim H, Raushel FM, Holden HM (2001) High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta. Biochemistry 40(9):2712–2722

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