Localization of the Zinc Binding Site of Aspartate Transcarbamoylase in the Regulatory Subunit
Open Access
- 1 May 1971
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 68 (5), 1019-1023
- https://doi.org/10.1073/pnas.68.5.1019
Abstract
Aspartate transcarbamoylase (EC 2.1.3.2) from Escherichia coli contains six zinc ions per molecule. Renaturation studies of this allosteric enzyme and its isolated subunits show that the metal binding site is in the regulatory polypeptide chain. Ultraviolet difference spectra of the cadmium and zinc derivatives have been used to show that the sites in the isolated subunit and the full enzyme are similar. Results with an apo derivative of the regulatory subunit suggest that the metal is not required for the binding of the feedback inhibitor, but that it is involved in the structural stability of the protein. A close relationship between the reactivity of the cysteine residues in the regulatory subunit and the metal ion has been found.Keywords
This publication has 11 references indexed in Scilit:
- Subunit Structure of Aspartate Transcarbamylase from Escherichia coliJournal of Biological Chemistry, 1971
- Determination of the number of regulatory and catalytic sites on aspartate transcarbamylaseBiochemistry, 1970
- Ultraviolet difference spectral studies of conalbumin complexes with transition metal ionsBiochemistry, 1969
- New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide ChainNature, 1968
- Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunitsBiochemistry, 1968
- The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein SubunitsJournal of Biological Chemistry, 1967
- Studies on the active center of alkaline phosphatase of E. coli.Proceedings of the National Academy of Sciences, 1966
- Measurement of protein-binding phenomena by gel filtrationBiochimica et Biophysica Acta, 1962
- The Enzymology of Control by Feedback InhibitionJournal of Biological Chemistry, 1962
- Metallothionein: a cadmium and zinc-containign protein from equine renal cortex. II. Physico-chemical properties.1961