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3. The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel. Dunn MF, Aguilar V, Brzović P, Drewe WF, Houben KF, Leja CA, Roy M. Biochemistry; 1990 Sep 18; 29(37):8598-607. PubMed ID: 2271543 [Abstract] [Full Text] [Related]
4. Application of rapid-scanning, stopped-flow spectroscopy to the characterization of intermediates formed in the reactions of L- and D-tryptophan and beta-mercaptoethanol with Escherichia coli tryptophan synthase. Drewe WF, Koerber SC, Dunn MF. Biochimie; 1989 Apr 18; 71(4):509-19. PubMed ID: 2503056 [Abstract] [Full Text] [Related]
5. Allosteric regulation of tryptophan synthase: effects of pH, temperature, and alpha-subunit ligands on the equilibrium distribution of pyridoxal 5'-phosphate-L-serine intermediates. Peracchi A, Bettati S, Mozzarelli A, Rossi GL, Miles EW, Dunn MF. Biochemistry; 1996 Feb 13; 35(6):1872-80. PubMed ID: 8639669 [Abstract] [Full Text] [Related]
6. Characterization of the reaction of L-serine and indole with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy. Drewe WF, Dunn MF. Biochemistry; 1986 May 06; 25(9):2494-501. PubMed ID: 3087420 [Abstract] [Full Text] [Related]
7. Allosteric effects acting over a distance of 20-25 A in the Escherichia coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediates. Houben KF, Dunn MF. Biochemistry; 1990 Mar 06; 29(9):2421-9. PubMed ID: 2186812 [Abstract] [Full Text] [Related]
8. Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analogues. Tschopp J, Kirschner K. Biochemistry; 1980 Sep 16; 19(19):4514-21. PubMed ID: 6996720 [Abstract] [Full Text] [Related]
9. Proton transfers in the beta-reaction catalyzed by tryptophan synthase. Hur O, Niks D, Casino P, Dunn MF. Biochemistry; 2002 Aug 06; 41(31):9991-10001. PubMed ID: 12146963 [Abstract] [Full Text] [Related]
10. Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex. Brzović PS, Ngo K, Dunn MF. Biochemistry; 1992 Apr 21; 31(15):3831-9. PubMed ID: 1567839 [Abstract] [Full Text] [Related]
11. A single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product. Zhao GP, Somerville RL. J Biol Chem; 1993 Jul 15; 268(20):14921-31. PubMed ID: 8325869 [Abstract] [Full Text] [Related]
12. The mechanism of binding of L-serine to tryptophan synthase from Escherichia coli. Lane AN, Kirschner K. Eur J Biochem; 1983 Jan 01; 129(3):561-70. PubMed ID: 6402361 [Abstract] [Full Text] [Related]
13. pH dependence of tryptophan synthase catalytic mechanism: I. The first stage, the beta-elimination reaction. Schiaretti F, Bettati S, Viappiani C, Mozzarelli A. J Biol Chem; 2004 Jul 09; 279(28):29572-82. PubMed ID: 15117965 [Abstract] [Full Text] [Related]
14. Evidence of a low-barrier hydrogen bond in the tryptophan synthase catalytic mechanism. Hur O, Leja C, Dunn MF. Biochemistry; 1996 Jun 11; 35(23):7378-86. PubMed ID: 8652514 [Abstract] [Full Text] [Related]
15. Tryptophan synthase: structure and function of the monovalent cation site. Dierkers AT, Niks D, Schlichting I, Dunn MF. Biochemistry; 2009 Nov 24; 48(46):10997-1010. PubMed ID: 19848417 [Abstract] [Full Text] [Related]
16. Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase. Phillips RS, Holtermann G. Biochemistry; 2005 Nov 01; 44(43):14289-97. PubMed ID: 16245945 [Abstract] [Full Text] [Related]
17. Stereoelectronic control of bond formation in Escherichia coli tryptophan synthase: substrate specificity and enzymatic synthesis of the novel amino acid dihydroisotryptophan. Roy M, Keblawi S, Dunn MF. Biochemistry; 1988 Sep 06; 27(18):6698-704. PubMed ID: 3058204 [Abstract] [Full Text] [Related]
20. BetaQ114N and betaT110V mutations reveal a critically important role of the substrate alpha-carboxylate site in the reaction specificity of tryptophan synthase. Blumenstein L, Domratcheva T, Niks D, Ngo H, Seidel R, Dunn MF, Schlichting I. Biochemistry; 2007 Dec 11; 46(49):14100-16. PubMed ID: 18004874 [Abstract] [Full Text] [Related] Page: [Next] [New Search]