PMID:9562556

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Citation

Gallagher, DT, Gilliland, GL, Xiao, G, Zondlo, J, Fisher, KE, Chinchilla, D and Eisenstein, E (1998) Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. Structure 6:465-75

Abstract

Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine, the pathway end-product, and valine, the product of a parallel pathway, serve as allosteric inhibitor and activator, respectively. This enzyme is thus a useful model system for studying the structural basis of allosteric control mechanisms.

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Keywords

Allosteric Regulation/physiology; Binding Sites/physiology; Carbohydrate Dehydrogenases/chemistry; Crystallography, X-Ray; Dimerization; Enzyme Activation/physiology; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Hydrogen Bonding; Models, Molecular; Phosphoglycerate Dehydrogenase; Protein Conformation; Protein Structure, Secondary; Pyridoxal Phosphate/chemistry; Structure-Activity Relationship; Threonine Dehydratase/chemistry; Tryptophan Synthase/chemistry; Valine/pharmacology

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