The Mechanism of Binding of L-Serine to Tryptophan Synthase from Escherichia coli
Abstract
The mechanism of binding of L-serine to tryptophan synthase, which is the initial phase of the catalytic mechanism, has been studied by steady-state and stopped-flow kinetic techniques. The dependence of three separable rate processes on the concentration of L-serine is compatible with four different enzyme-substrate complexes, one of which lies on a branch in the pathway. By use of L-serine deuterated at the alpha carbon, it is possible to...
Paper Details
Title
The Mechanism of Binding of L-Serine to Tryptophan Synthase from Escherichia coli
Published Date
Jan 1, 1983
Volume
129
Issue
3
Pages
561 - 570
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