Articles - 2trs mentioned but not cited (1)
- Tryptophan synthase: structure and function of the monovalent cation site. Dierkers AT, Niks D, Schlichting I, Dunn MF. Biochemistry 48 10997-11010 (2009)
Reviews citing this publication (12)
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- On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase. Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I. J Mol Biol 324 677-690 (2002)
- Structure and mechanistic implications of a tryptophan synthase quinonoid intermediate. Barends TR, Domratcheva T, Kulik V, Blumenstein L, Niks D, Dunn MF, Schlichting I. Chembiochem 9 1024-1028 (2008)
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- Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states. Niks D, Hilario E, Dierkers A, Ngo H, Borchardt D, Neubauer TJ, Fan L, Mueller LJ, Dunn MF. Biochemistry 52 6396-6411 (2013)
- On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes. Kulik V, Hartmann E, Weyand M, Frey M, Gierl A, Niks D, Dunn MF, Schlichting I. J Mol Biol 352 608-620 (2005)
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- Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble. Buller AR, van Roye P, Cahn JKB, Scheele RA, Herger M, Arnold FH. J Am Chem Soc 140 7256-7266 (2018)
- Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling. Axe JM, Boehr DD. J Mol Biol 425 1527-1545 (2013)
- The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase. Xiang J, Sun J, Sampson NS. J Mol Biol 307 1103-1112 (2001)
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- Identification of the geometric requirements for allosteric communication between the alpha- and beta-subunits of tryptophan synthase. Raboni S, Bettati S, Mozzarelli A. J Biol Chem 280 13450-13456 (2005)
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- Detection of open and closed conformations of tryptophan synthase by 15N-heteronuclear single-quantum coherence nuclear magnetic resonance of bound 1-15N-L-tryptophan. Osborne A, Teng Q, Miles EW, Phillips RS. J Biol Chem 278 44083-44090 (2003)
- Structural analysis of ligand binding and catalysis in chorismate lyase. Smith N, Roitberg AE, Rivera E, Howard A, Holden MJ, Mayhew M, Kaistha S, Gallagher DT. Arch Biochem Biophys 445 72-80 (2006)
- Characterization of the putative tryptophan synthase beta-subunit from Mycobacterium tuberculosis. Shen H, Yang Y, Wang F, Zhang Y, Ye N, Xu S, Wang H. Acta Biochim Biophys Sin (Shanghai) 41 379-388 (2009)
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- Quantitative effects of allosteric ligands and mutations on conformational equilibria in Salmonella typhimurium tryptophan synthase. Phillips RS, McPhie P, Miles EW, Marchal S, Lange R. Arch Biochem Biophys 470 8-19 (2008)
- Structural, biochemical, and in vivo investigations of the threonine synthase from Mycobacterium tuberculosis. Covarrubias AS, Högbom M, Bergfors T, Carroll P, Mannerstedt K, Oscarson S, Parish T, Jones TA, Mowbray SL. J Mol Biol 381 622-633 (2008)
- Switches of hydrogen bonds during ligand-protein association processes determine binding kinetics. Huang YM, Kang M, Chang CE. J Mol Recognit 27 537-548 (2014)
- The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors. Hioki Y, Ogasahara K, Lee SJ, Ma J, Ishida M, Yamagata Y, Matsuura Y, Ota M, Ikeguchi M, Kuramitsu S, Yutani K. Eur J Biochem 271 2624-2635 (2004)
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- Catalytic roles of βLys87 in tryptophan synthase: (15)N solid state NMR studies. Caulkins BG, Yang C, Hilario E, Fan L, Dunn MF, Mueller LJ. Biochim Biophys Acta 1854 1194-1199 (2015)
- Protonation states and catalysis: Molecular dynamics studies of intermediates in tryptophan synthase. Huang YM, You W, Caulkins BG, Dunn MF, Mueller LJ, Chang CE. Protein Sci 25 166-183 (2016)
- 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 432 233-243 (2004)
- Holo- and apo-cystalysin from Treponema denticola: two different conformations. Cellini B, Montioli R, Bossi A, Bertoldi M, Laurents DV, Voltattorni CB. Arch Biochem Biophys 455 31-39 (2006)
- Mutational scanning of a hairpin loop in the tryptophan synthase beta-subunit implicated in allostery and substrate channeling. Rondard P, Bedouelle H. Biol Chem 381 1185-1193 (2000)
- Putative implication of alpha-amylase loop 7 in the mechanism of substrate binding and reaction products release. André G, Tran V. Biopolymers 75 95-108 (2004)
- Catalytically impaired TrpA subunit of tryptophan synthase from Chlamydia trachomatis is an allosteric regulator of TrpB. Michalska K, Wellington S, Maltseva N, Jedrzejczak R, Selem-Mojica N, Rosas-Becerra LR, Barona-Gómez F, Hung DT, Joachimiak A. Protein Sci 30 1904-1918 (2021)
- Effects of hydrostatic pressure on the conformational equilibrium of tryptophan synthase from Salmonella typhimurium. Phillips RS, Miles EW, McPhie P, Marchal S, Lange R, Holtermann G, Goody RS. Ann N Y Acad Sci 1189 95-103 (2010)
- Engineered Biocatalytic Synthesis of β-N-Substituted-α-Amino Acids. Villalona J, Higgins PM, Buller AR. Angew Chem Int Ed Engl 62 e202311189 (2023)
- Engineered Tryptophan Synthase Balances Equilibrium Effects and Fast Dynamic Effects. Schafer JW, Chen X, Schwartz SD. ACS Catal 12 913-922 (2022)
- PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase. Hilario E, Fan L, Mueller LJ, Dunn MF. J Vis Exp (2020)
- Towards Photochromic Azobenzene-Based Inhibitors for Tryptophan Synthase. Simeth NA, Kinateder T, Rajendran C, Nazet J, Merkl R, Sterner R, König B, Kneuttinger AC. Chemistry 27 2439-2451 (2021)
Related citations provided by authors (1)
- Lysine 87 in the Beta Subunit of Tryptophan Synthase that Forms an Internal Aldimine with Pyridoxal Phosphate Serves Critical Roles in Transimination, Catalysis, and Product Release. Lu Z, Nagata S, Mcphie P, Miles EW J. Biol. Chem. 268 8727- (1993)