Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1972.tb01938.x/fullpdf
Reference44 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. Subunit Structure of the Protein Catalyzing the Two Activities
3. Active subunits of the aspartokinase-homoserine dehydrogenase I complex from Escherichia coli
4. Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 λ. Subunit molecular weight and nicotinamide-adenine dinucleotide phosphate binding
5. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. Binding of Threonine and of Pyridine Nucleotides: Stoichiometry and Optical Effects
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