Orientation of enzymic domains in tryptophan synthase of Neurospora crassa: An immunoblot analysis of TRP3 mutant products
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics,Molecular Biology
Link
http://link.springer.com/content/pdf/10.1007/BF00328130.pdf
Reference32 articles.
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2. Crawford I, Ito J (1964) Serine deamination by the B protein of Escherichia coli tryptophan synthetase. Proc Natl Acad Sci USA 15:390–397
3. Creighton TE (1970) A steady state kinetic investigation of the reaction mechanism of the tryptophan synthetase of Escherichia coli. Eur J Biochem 13:1–10
4. DeMoss JA (1962) Studies on the mechanism of the tryptophan synthetase reaction. Biochim Biophys Acta 62:279–293
5. Dettwiler M, Kirschner K (1979) Tryptophan synthase from Saccharomyces cerevisiae is a dimer of two polypeptide chains of MW 76000 each. Eur J Biochem 102:159–165
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1. Molecular analysis of intragenic recombination at the tryptophan synthetase locus in Neurospora crassa;Journal of Genetics;2013-12
2. Structural Basis for Catalysis by Tryptophan Synthase;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. References;The Neurospora Compendium;2001
4. Deletion analysis of domain independence in the TRP1 gene product of Neurospora crassa;Molecular and General Genetics MGG;1990-08
5. Evolution of the tryptophan synthetase of fungi. Analysis of experimentally fused Escherichia coli tryptophan synthetase alpha and beta chains.;Journal of Biological Chemistry;1990-02
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