A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference34 articles.
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3. In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamylase;Wild;Proc. Natl Acad. Sci. USA,1989
4. Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8Å resolution and neutral pH;Gouaux;Biochemistry,1990
5. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6Å resolution;Stevens;Biochemistry,1990
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