The Catalytic Mechanism of Tryptophan Synthase from Escherichia coli
Abstract
The mechanism by which indole condenses with L-serine in the active site of tryptophan synthase was studied by the stopped-flow technique. The single turnover occurs by rapid binding of indole to the pre-formed enzyme--L-serine complex, followed by C--C bond formation, reprotonation of the alpha carbon carbanion of L-tryptophan, and its final release. The effects of isotopic substitution at C-3 of indole, of pH, and of the presence of...
Paper Details
Title
The Catalytic Mechanism of Tryptophan Synthase from Escherichia coli
Published Date
Jan 1, 1983
Volume
129
Issue
3
Pages
571 - 582
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