The structure of an enzyme–product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism-Reference-Cited by-同舟云学术

The structure of an enzyme–product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism

Published:2005-08 Issue:1 Volume:1752 Page:56-64
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Jackson Colin,Kim Hye-Kyung,Carr Paul D.,Liu Jian-Wei,Ollis David L.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference28 articles.

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4. Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution;Yang;Protein Eng.,2003

5. High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta;Benning;Biochemistry,2001

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