Regulation of aspartate carbamoyltransferase of Escherichia coli by the interrelationship of magnesium and nucleotides
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Elsevier BV
Reference18 articles.
1. Aspartate transcarbamylase from Escherichia coli. II. Interaction of metal ions with substrates, inhibitors and activators
2. Über die intrazelluläre Mg-Ionenaktivität von E. coli-Zellen
3. Stability Constants of Metal Complexes with Mononucleotides.
4. Thermodynamic Studies of the Formation and Ionization of the Magnesium(II) Complexes of ADP and ATP over the pH Range 5 to 91
5. The Enzymology of Control by Feedback Inhibition
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1. New Paradigm for Allosteric Regulation of Escherichia coli Aspartate Transcarbamoylase;Biochemistry;2013-10-31
2. Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase;Biochemistry;2012-08-24
3. The Allosteric activator Mg-ATP Modifies the Quaternary Structure of the R-state of Escherichia coli Aspartate Transcarbamylase Without Altering the T↔R Equilibrium;Journal of Molecular Biology;2001-06
4. X-ray Scattering Titration of the Quaternary Structure Transition of Aspartate Transcarbamylase with a Bisubstrate Analogue: Influence of Nucleotide Effectors;Journal of Molecular Biology;1995-08
5. Simplified 14C-carbamoyl phosphate-based array of Aspartate carbamoyltransferase;Biochemical Education;1988-07
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