Steady-State Kinetic Studies of the Synthesis of Indoleglycerol Phosphate Catalyzed by the alpha Subunit of Tryptophan Synthase from Escherichia coli. Comparison with the alpha2beta2-Complex-Reference-Cited by-同舟云学术

Steady-State Kinetic Studies of the Synthesis of Indoleglycerol Phosphate Catalyzed by the alpha Subunit of Tryptophan Synthase from Escherichia coli. Comparison with the alpha2beta2-Complex

Published:1976-06 Issue:2 Volume:65 Page:375-385
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

WEISCHET Wolfgang O.,KIRSCHNER Kasper

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10351.x/fullpdf

Reference31 articles.

1. The Mechanism of the Synthesis of Indoleglycerol Phosphate Catalyzed by Tryptophan Synthase from Escherichia coli. Steady-State Kinetic Studies

2. 2. C. Yanofskv, I. P. Crawford, and P. D. Boyer (1972 ) inThe Enzymes , 3rd edn () vol. 7 , pp. 1 -31 Academic Press, New York.

3. Studies on the Active Site of the A Protein Subunit of the Escherichia coli Tryptophan Synthetase

4. Structural and Functional Roles of the Cysteine Residues in the α Subunit of the Escherichia coli Tryptophan Synthetase

5. The Tryptophan Synthase from Escherichia coli. An Improved Purification Procedure for the alpha-Subunit and Binding Studies with Substrate Analogues

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