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.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference49 articles.
1. Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase.
2. Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.
3. Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase
4. Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers.
5. Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains.
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