Characterization of the reaction of L-serine and indole with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00357a032
Reference24 articles.
1. Detection and identification of intermediates in the reaction of L-serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
2. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit
3. Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme
4. Interactions between the Subunits of the Tryptophan Synthetase of Escherichia coli. Optical Properties of an Intermediate Bound to the α2β2 Complex*
5. Fluorescence studies of substrate and subunit interactions of the .beta.2 protein of Escherichia coli tryptophan synthetase
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