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Journal Abstract Search

134 related items for PubMed ID: 3087420

  • 1. 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
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  • 2. Detection and identification of intermediates in the reaction of L-serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy.
    Drewe WF, Dunn MF.
    Biochemistry; 1985 Jul 16; 24(15):3977-87. PubMed ID: 3931672
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  • 3. 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 16; 71(4):509-19. PubMed ID: 2503056
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  • 4. 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
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  • 5. Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism.
    Anderson KS, Miles EW, Johnson KA.
    J Biol Chem; 1991 May 05; 266(13):8020-33. PubMed ID: 1902468
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  • 9. The reaction of indole with the aminoacrylate intermediate of Salmonella typhimurium tryptophan synthase: observation of a primary kinetic isotope effect with 3-[(2)H]indole.
    Cash MT, Miles EW, Phillips RS.
    Arch Biochem Biophys; 2004 Dec 15; 432(2):233-43. PubMed ID: 15542062
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  • 12. Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex.
    Woehl EU, Dunn MF.
    Biochemistry; 1995 Jul 25; 34(29):9466-76. PubMed ID: 7626617
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  • 14. Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli.
    Lane AN, Kirschner K.
    Biochemistry; 1991 Jan 15; 30(2):479-84. PubMed ID: 1899028
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  • 15. 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
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  • 16. Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands.
    Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF.
    Biochemistry; 2007 Jul 03; 46(26):7740-53. PubMed ID: 17559232
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  • 17. Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.
    Brzović PS, Sawa Y, Hyde CC, Miles EW, Dunn MF.
    J Biol Chem; 1992 Jun 25; 267(18):13028-38. PubMed ID: 1618800
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  • 18. 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
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  • 19. The mechanism of Escherichia coli tryptophan indole-lyase: substituent effects on steady-state and pre-steady-state kinetic parameters for aryl-substituted tryptophan derivatives.
    Lee M, Phillips RS.
    Bioorg Med Chem; 1995 Feb 04; 3(2):195-205. PubMed ID: 7796054
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  • 20. The reaction of yeast cystathionine beta-synthase is rate-limited by the conversion of aminoacrylate to cystathionine.
    Jhee KH, Niks D, McPhie P, Dunn MF, Miles EW.
    Biochemistry; 2001 Sep 11; 40(36):10873-80. PubMed ID: 11535064
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