Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase
Author:
Affiliation:
1. Department of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi300920m
Reference38 articles.
1. Structure and Mechanisms of Escherichia coli Aspartate Transcarbamoylase
2. The Effect of the Feedback Inhibitor, CTP, on Subunit Interactions in Aspartate Transcarbamylase
3. In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.
4. Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model
5. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-.ANG. resolution
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1. New mechanism-based inhibitors of aspartate transcarbamoylase for anticancer drug development;2019-06-06
2. The Quaternary Structure of the R-State of Escherichia coli Aspartate Transcarbamoylase in Solution Is Different from That in the Crystal and Is Modified by Mg2+·ATP Binding;Biochemistry;2017-05-23
3. Solution NMR Spectroscopy for the Study of Enzyme Allostery;Chemical Reviews;2016-01-06
4. From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases;International Journal of Molecular Sciences;2015-08-12
5. New Paradigm for Allosteric Regulation of Escherichia coli Aspartate Transcarbamoylase;Biochemistry;2013-10-31
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