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5. Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium. Brzović PS, Kayastha AM, Miles EW, Dunn MF. Biochemistry; 1992 Feb 04; 31(4):1180-90. PubMed ID: 1346502 [Abstract] [Full Text] [Related]
7. Circular dichroism studies of the coenzyme environment in the active sites of mutant forms of the beta-subunit in the tryptophan synthase alpha 2 beta 2 complex. Kayastha AM, Sawa Y, Nagata S, Kanzaki H, Miles EW. Indian J Biochem Biophys; 1991 Feb 04; 28(5-6):352-7. PubMed ID: 1812066 [Abstract] [Full Text] [Related]
13. Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits. Kawasaki H, Bauerle R, Zon G, Ahmed SA, Miles EW. J Biol Chem; 1987 Aug 05; 262(22):10678-83. PubMed ID: 3112150 [Abstract] [Full Text] [Related]
16. The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper geometry of the substrate binding site. Nagata S, Hyde CC, Miles EW. J Biol Chem; 1989 Apr 15; 264(11):6288-96. PubMed ID: 2649498 [Abstract] [Full Text] [Related]
17. Site-directed mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Ahmed SA, Kawasaki H, Bauerle R, Morita H, Miles EW. Biochem Biophys Res Commun; 1988 Mar 15; 151(2):672-8. PubMed ID: 3126743 [Abstract] [Full Text] [Related]