Structure, Function, and Possible Origin of a Bifunctional Allosteric Enzyme,Escherichia ColiAspartokinase I-Homoserine Dehydrogenase
Author:
Publisher
Informa UK Limited
Subject
Pharmacology (medical)
Link
http://www.tandfonline.com/doi/pdf/10.3109/10409237409105452
Reference52 articles.
1. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. 4. Isolation, Molecular Weight, Amino Acid Analysis and Behaviour of the Sulfhydryl Groups of the Protein Catalyzing the Two Activities
2. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. A Study of the Allosteric Equilibrium
3. Truffa-Bachi P., Cohen G. N. Aspartokinase I and homoserine dehydrogenase I (Escherichia coliK12), inMethods in Enzymology. Academic Press, New York 1970; Vol. XVIIA: 694
4. Two aspartokinases from Escherichia coli. Nature of the inhibition and molecular changes accompanying reversible inactivation
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