Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase
- 13 February 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (6) , 1444-1451
- https://doi.org/10.1021/bi00458a015
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 36 references indexed in Scilit:
- Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: Effect of active-site ligands on the regulatory chainsProceedings of the National Academy of Sciences, 1980
- Conformational states of aspartate transcarbamoylase stabilized with a cross-linking reagent.Journal of Biological Chemistry, 1979
- Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate.Proceedings of the National Academy of Sciences, 1978
- The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coliJournal of Biological Chemistry, 1978
- Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog N-(phosphonacetyl)-L-aspartateBiochemistry, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sitesBiochemistry, 1976
- The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein SubunitsJournal of Biological Chemistry, 1967
- Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase*Biochemistry, 1965
- The Enzymology of Control by Feedback InhibitionJournal of Biological Chemistry, 1962