Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference37 articles.
1. Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides.
2. Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis
3. Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.
4. The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein, CAD.
5. The aspartate transcarbamylase domain of a mammalian multifunctional protein expressed as an independent enzyme in Escherichia coli
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1. Allosteric regulation of CAD modulates de novo pyrimidine synthesis during the cell cycle;Nature Metabolism;2023-02-06
2. A Tailored Strategy to Crosslink the Aspartate Transcarbamoylase Domain of the Multienzymatic Protein CAD;Molecules;2023-01-09
3. Deciphering CAD : Structure and function of a mega‐enzymatic pyrimidine factory in health and disease;Protein Science;2021-07-22
4. UMP inhibition and sequential firing in aspartate transcarbamoylase open ways to regulate plant growth;2020-07-17
5. CAD, A Multienzymatic Protein at the Head of de Novo Pyrimidine Biosynthesis;Subcellular Biochemistry;2019
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