The Mechanism of the Synthesis of Indoleglycerol Phosphate Catalyzed by Tryptophan Synthase from Escherichia coli. Steady-State Kinetic Studies
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10350.x/fullpdf
Reference24 articles.
1. 1. C. Yanofsky, I. P. Crawford, and P. D. Buyer (1972 ) inThe Enzymes , 3rd edn () pp. 1 -31 Academic Press, New York.
2. Structural and Functional Roles of the Cysteine Residues in the α Subunit of the Escherichia coli Tryptophan Synthetase
3. A Steady-State Kinetic Investigation of the Reaction Mechanism of the Tryptophan Synthetase of Escherichia coli
4. The Tryptophan Synthase from Escherichia coli. An Improved Purification Procedure for the alpha-Subunit and Binding Studies with Substrate Analogues
5. The Binding of Indole to the alpha-Subunit and beta2-Subunit and to the alpha2beta2-Complex of Tryptophan Synthase from Escherichia coli. Identification of a Second Indole-Binding Site on the alpha-Subunit
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