Identification of the regulatory domain of the mammalian multifunctional protein CAD by the construction of an Escherichia coli hamster hybrid carbamyl-phosphate synthetase.-Reference-Cited by-同舟云学术

Identification of the regulatory domain of the mammalian multifunctional protein CAD by the construction of an Escherichia coli hamster hybrid carbamyl-phosphate synthetase.

Published:1994-11 Issue:44 Volume:269 Page:27747-27755
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Liu X,Guy H I,Evans D R

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference81 articles.

1. Evidence for an Activated Form of Carbon Dioxide in the Reaction Catalyzed by Escherichia coli Carbamyl Phosphate Synthetase*

2. Bicarbonate-Dependent Cleavage of Adenosine Triphosphate and Other Reactions Catalyzed by Escherichia coli Carbamyl Phosphate Synthetase*

3. Identification of enzyme-bound activated CO2 as carbonic-phosphoric anhydride: isolation of the corresponding trimethyl derivative from the active site of glutamine-dependent carbamyl phosphate synthetase.

4. Mechanism of the reaction catalyzed by carbamyl phosphate synthetase. Binding of ATP to the two functionally different ATP sites.

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1. Allosteric regulation of CAD modulates de novo pyrimidine synthesis during the cell cycle;Nature Metabolism;2023-02-06

2. The cell cycle loops UTP around CAD;Nature Metabolism;2023-02-06

3. A Tailored Strategy to Crosslink the Aspartate Transcarbamoylase Domain of the Multienzymatic Protein CAD;Molecules;2023-01-09

4. Deciphering CAD : Structure and function of a mega‐enzymatic pyrimidine factory in health and disease;Protein Science;2021-07-22

5. CAD, A Multienzymatic Protein at the Head of de Novo Pyrimidine Biosynthesis;Subcellular Biochemistry;2019