MUTANTS OF ESCHERICHIA COLI DEFECTIVE IN THE B PROTEIN OF TRYPTOPHAN SYNTHETASE. II. INTRAGENIC POSITION
Author:
Affiliation:
1. Department of Microbiology, Western Reserve University School of Medicine, Cleveland 6, Ohio
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
http://academic.oup.com/genetics/article-pdf/49/2/267/34897595/genetics0267.pdf
Cited by 11 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. An amino acid switch (Gly281–>Arg) within the “hinge” region of the tryptophan synthase beta subunit creates a novel cleavage site for the OmpT protease and selectively diminishes affinity toward a specific monoclonal antibody;Journal of Biological Chemistry;1993-07
2. Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.;Journal of Biological Chemistry;1992-01
3. Interactions of tryptophan synthetase subunits in Escherichia coli containing mutationally altered beta2 subunits.;Journal of Biological Chemistry;1977-07
4. Purification by Immunoadsorbtion Chromatography of the Normal and a Mutant Form of the B2 Subunit of Escherichia coli Tryptophan Synthase;European Journal of Biochemistry;1976-04
5. Tryptophan synthetase alpha(5.7-S): novel molecular species formed within Escherichia coli;Journal of Bacteriology;1975-11
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