Electrostatic and Steric Contributions to Regulation at the Active Site of Isocitrate Dehydrogenase
Author:
Affiliation:
1. Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference20 articles.
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3. BORTHWICK, A.C., ISOLATION OF ACTIVE AND INACTIVE FORMS OF ISOCITRATE DEHYDROGENASE FROM ESCHERICHIA-COLI ML308, EUROPEAN JOURNAL OF BIOCHEMISTRY 141: 393 (1984).
4. DEAN, A.M., PHOSPHORYLATION INACTIVATES ESCHERICHIA-COLI ISOCITRATE DEHYDROGENASE BY PREVENTING ISOCITRATE BINDING, JOURNAL OF BIOLOGICAL CHEMISTRY 264: 20482 (1989).
5. DEAN, A.M., FITNESS EFFECTS OF AMINO-ACID REPLACEMENTS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA-COLI, MOLECULAR BIOLOGY AND EVOLUTION 5: 469 (1988).
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