Computational insights into substrate binding and catalytic mechanism of the glutaminase domain of glucosamine-6-phosphate synthase (GlmS)
Author:
Affiliation:
1. Department of Chemistry and Biochemistry
2. University of Windsor
3. Windsor
4. Canada
5. Université de Lorraine
6. UMR 7565 SRSMC
7. F-54506 Vandoeuvre-les-Nancy
8. France
Abstract
The mechanistic cysteinyl of GlmS can activate its thiol using its own α-amine without the need for a bridging water.
Funder
Natural Sciences and Engineering Research Council of Canada
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA04906D
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4. Structure–function studies of glutamate synthases: A class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation
5. The Active Conformation of Glutamate Synthase and its Binding to Ferredoxin
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