Biochemical Characterization and Crystallographic Structure of an Escherichia coli Protein from the Phosphotriesterase Gene Family-Reference-Cited by-同舟云学术

Biochemical Characterization and Crystallographic Structure of an Escherichia coli Protein from the Phosphotriesterase Gene Family

Published:1998-03-25 Issue:15 Volume:37 Page:5096-5106
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Buchbinder Jenny L.¹,Stephenson Robert C.¹,Dresser Mark J.¹,Pitera Jed W.¹,Scanlan Thomas S.¹,Fletterick Robert J.¹

Affiliation:

1. Departments of Biochemistry and Biophysics, Pharmaceutical Chemistry, and Cellular and Molecular Pharmacology, University of California, San Francisco, California 94143-0448

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi971707%2B

Reference45 articles.

1. Evidence for an artificially evolved bifunctional 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase-chorismate mutase in Bacillus subtilis.

2. Catalytic consequences of experimental evolution: catalysis by a ‘third-generation’ evolvant of the second beta-galactosidase of Escherichia coli, ebg abcde, and by ebg abcd, a ‘second-generation’ evolvant containing two supposedly ‘kinetically silent’ mutations

3. Purification and Properties of the Phosphotriesterase from Pseudomonas diminuta

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