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.
journal_name
Proc Natl Acad Sci U S Aauthors
Rosenbusch JP,Weber Kdoi
10.1073/pnas.68.5.1019subject
Has Abstractpub_date
1971-05-01 00:00:00pages
1019-23issue
5eissn
0027-8424issn
1091-6490journal_volume
68pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2015-03-31 00:00:00