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    Di Martino P, Fursy R, Bret L, Sundararaju B & Phillips RS (2003) Indole can act as an extracellular signal to regulate biofilm formation in Escherichia coli and in other indole-producing bacteria. Can J Microbiol 49, 443449.
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    Phillips RS (1991) The reaction of indole and benzimidazole with amino acid complexes of E. coli tryptophan indole-lyase: detection of a new reaction intermediate. Biochemistry 30, 59275934.
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    Phillips RS, Sundararju B & Faleev NG (2000) Proton transfer and carbon–carbon bond cleavage in the elimination of indole catalyzed by Escherichia coli tryptophan indole-lyase. J Am Chem Soc 122, 11081114.
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    Phillips RS, Miles EW & Cohen LA (1984) Interactions of tryptophan synthase, tryptophanase and pyridoxal phosphate with oxindolyl-l-alanine and 2,3-dihydro-l-tryptophan: support for an indolenine intermediate in tryptophan metabolism. Biochemistry 23, 62286234.
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    Phillips RS, Miles EW & Cohen LA (1985) Differential inhibition of tryptophan synthase and of tryptophanase by the two diastereoisomers of 2,3-dihydro-l-tryptophan: implications for the stereochemistry of the reaction intermediates. J Biol Chem 260, 1466514670.
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    Phillips RS, Johnson N & Kamath AV (2002) Formation in vitro of hybrid dimers of H463F and Y74F mutant Escherichia coli tryptophan indole-lyase rescues activity with l-tryptophan. Biochemistry 41, 40124019.
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    Demidkina TV, Zakomirdina LN, Kulikova VV, Dementieva IS, Faleev NG, Ronda L, Mozzarelli A, Gollnick PD & Phillips RS (2003) Role of aspartate-133 and histidine-458 in the mechanism of tryptophan indole-lyase from Proteus vulgaris. Biochemistry 42, 1116111169.
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    Lima S, Sundararaju B, Huang C, Khristoforov R, Momany C & Phillips RS (2009) The crystal structure of the Pseudomonas dacunhae aspartate-β–decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5′–phosphate-dependent enzyme. J Mol Biol 388, 98108.
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    Phillips RS, Lima S, Khristoforov R & Sudararaju B (2010) Insights into the mechanism of Pseudomonas dacunhae aspartate β-decarboxylase from rapid-scanning stopped-flow kinetics. Biochemistry 49, 50665073.
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    Kiick DM & Phillips RS (1988) Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon–carbon lyases: Escherichia coli tryptophan indole-lyase. Biochemistry 27, 73397344.
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    Milić D, Demidkina TV, Faleev NG, Phillips RS, Matković-Čalogović D & Antson AA (2011) Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage. J Am Chem Soc 133, 1646816476.
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    Phillips RS, Ravichandran K & Von Tersch RL (1989) Synthesis of l-tyrosine from phenol and S-(o-nitrophenyl)-l-cysteine catalyzed by tyrosine phenol-lyase. Enzyme Microb Technol 11, 8083.
  • 31
    Dua RK, Taylor EW & Phillips RS (1993) S–aryl-l–cysteine S, S–dioxides: design and evaluation of a new class of mechanism based inhibitors of kynureninase. J Am Chem Soc 115, 12641270.
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    Heiss C, Anderson J & Phillips RS (2003) Differential effects of bromination on substrates and inhibitors of kynureninase from Pseudomonas fluorescens. Org Biomol Chem 1, 288295.
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    Phillips RS & Gollnick PD (1989) Evidence that cysteine-298 is in the active site of tryptophan indole-lyase. J Biol Chem 254, 1062710632.
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    Cleland WW (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol 63, 103138.
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    Matheson IBC (1987) The method of successive integration: a general technique for recasting kinetic equations in a readily soluble form which is linear in the coefficients and sufficiently rapid for real time instrumental use. Anal Instrum 16, 345373.