Mutagenic Analysis of an Invariant Aspartate Residue in Chorismate Synthase Supports Its Role as an Active Site Base-Reference-Cited by-同舟云学术

Mutagenic Analysis of an Invariant Aspartate Residue in Chorismate Synthase Supports Its Role as an Active Site Base

Published:2007-02-28 Issue:12 Volume:46 Page:3768-3774
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rauch Gernot¹,Ehammer Heidemarie¹,Bornemann Stephen¹,Macheroux Peter¹

Affiliation:

1. Institute of Biochemistry, Graz University of Technology, Graz, Austria, and Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, United Kingdom

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi602420u

Reference24 articles.

1. Experiences with the shikimate-pathway enzymes as targets for rational drug design

2. Stereochemistry of the 3-Deoxy-d-arabino-heptulosonate 7-Phosphate Synthetase Reaction and the Chorismate Synthetase Reaction

3. The Enzymic Synthesis of Chorismic and Prephenic Acids from 3-Enolpyruvylshikimic Acid 5-Phosphate

4. The overexpression, purification and complete amino acid sequence of chorismate synthase from Escherichia coli K12 and its comparison with the enzyme from Neurospora crassa

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