Subunit interactions in aspartate transcarbamylase. A model for the allosteric mechanism
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference40 articles.
1. A Discussion of the Regulatory Properties of Aspartate Transcarbamylase from Escherichia coli
2. Enzyme-catalyzed Free Radical Reactions with Nicotinamide Adenine Nucleotides
3. Conformational Changes in Aspartate Transcarbamylase
Cited by 26 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. [28] Thermodynamic approaches to understanding aspartate transcarbamylase;Methods in Enzymology;1995
2. Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: Evidence for an uncoupled R state;Protein Science;1993-06
3. Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.;Journal of Biological Chemistry;1992-02
4. Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme.;Journal of Biological Chemistry;1988-05
5. Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli;Journal of Molecular Biology;1987-08
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