Allosteric Interactions Coordinate Covalent Steps in Catalysis and Modulate Indole Transfer Between the α- and β-Sites of the Tryptophan Synthase Bienzyme Complex

Dunn, Michael F.; Brzović, Peter S.; Leja, Catherine A.; Houben, Karl; Roy, M.; Aguilar, Alen; Drewe, William Frederick

doi:10.1016/b978-0-08-040820-0.50055-8

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Allosteric Interactions Coordinate Covalent Steps in Catalysis and Modulate Indole Transfer Between the α- and β-Sites of the Tryptophan Synthase Bienzyme Complex

Cited by 4 publications

References 20 publications

Tryptophan Synthase

Tryptophan Synthase

Tryptophan Synthase

Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

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