Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference53 articles.
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1. Structural Investigation of Cold Activity and Regulation of Aspartate Carbamoyltransferase from the Extreme Psychrophilic Bacterium Moritella profunda;Journal of Molecular Biology;2007-01
2. Allosteric Signal Transmission Involves Synergy between Discrete Structural Units of the Regulatory Subunit of Aspartate Transcarbamoylase;Archives of Biochemistry and Biophysics;2000-01
3. Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases 1 1Edited by J. H. Miller;Journal of Molecular Biology;1998-10
4. Role of Allosteric:Zinc Interdomain Region of the Regulatory Subunit in the Allosteric Regulation of Aspartate Transcarbamoylase fromEscherichia coli;Archives of Biochemistry and Biophysics;1998-06
5. Conversion of the Allosteric Regulatory Patterns of Aspartate Transcarbamoylase by Exchange of a Single β-Strand between Diverged Regulatory Chains;Biochemistry;1997-03-01
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