Ordered substrate binding and evidence for a thermally induced change in mechanism for E. coli aspartate transcarbamylase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference36 articles.
1. The Enzymology of Control by Feedback Inhibition
2. Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase*
3. CARBAMYL PHOSPHATE, THE CARBAMYL DONOR IN ENZYMATIC CITRULLINE SYNTHESIS1
4. Aspartate Carbamyl Transferase from Escherichia coli.
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1. Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase;Archives of Biochemistry and Biophysics;2012-03
2. Crystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilis;Journal of Molecular Biology;2011-08
3. The Pathway of Product Release from the R State of Aspartate Transcarbamoylase;Journal of Molecular Biology;2010-09
4. Structural Model of the R State of Escherichia coli Aspartate Transcarbamoylase with Substrates Bound;Journal of Molecular Biology;2007-08
5. Structural Investigation of Cold Activity and Regulation of Aspartate Carbamoyltransferase from the Extreme Psychrophilic Bacterium Moritella profunda;Journal of Molecular Biology;2007-01
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