Domain Closure in the Catalytic Chains of Escherichia coli Aspartate Transcarbamoylase Influences the Kinetic Mechanism
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Aspartate Transcarbamylase
2. Can a simple model account for the allosteric transition of aspartate transcarbamoylase?
3. Escherichia coli Aspartate Transcarbamoylase: Structure, Energetics, and Catalytic and Regulatory Mechanisms
4. Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition
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1. Dihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis;Biochemistry;2009-01-07
2. Monitoring the Transition from the T to the R State in E.coli Aspartate Transcarbamoylase by X-ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States;Journal of Molecular Biology;2004-08
3. Products in the T-State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-l-aspartate Ligated Enzyme,;Biochemistry;2004-05-06
4. Stabilization of the R Allosteric Structure of Escherichia coli Aspartate Transcarbamoylase by Disulfide Bond Formation;Journal of Biological Chemistry;2002-12
5. Allosteric Regulation of Catalytic Activity: Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate Mutase;Microbiology and Molecular Biology Reviews;2001-09
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