Ahmed SA, Kawasaki H, Bauerle R, Morita H, Miles EW. Site-directed mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Biochem. Biophys. Res. Commun. 151: 672-678 (1988).

Ahmed SA, Martin B, Miles EW. Beta-elimination of indole from L-tryptophan catalyzed by bacterial tryptophan synthase: a comparison between reactions catalyzed by tryptophanase and tryptophan synthase. Biochemistry 25: 4233-4240 (1986).

Ahmed SA, Ruvinov SB, Kayastha AM, Miles EW. Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit. J. Biol. Chem. 266: 21548-21557 (1991).

Akers JC, Tan M. Molecular mechanism of tryptophan-dependent transcriptional regulation in Chlamydia trachomatis. J. Bacteriol. 188: 4236-4243 (2006).

Allers T, Ngo HP, Mevarech M, Lloyd RG. Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes. Appl. Environ. Microbiol. 70: 943-953 (2004).

Anderson KS, Kim AY, Quillen JM, Sayers E, Yang XJ, Miles EW. Kinetic characterization of channel impaired mutants of tryptophan synthase. J. Biol. Chem. 270: 29936-29944 (1995).

Anderson KS, Miles EW, Johnson KA. Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism. J. Biol. Chem. 266: 8020-8033 (1991).

Asada Y, Sawano M, Ogasahara K, Nakamura J, Ota M, Kuroishi C, Sugahara M, Yutani K, Kunishima N. Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry. J. Biochem. (Tokyo) 138: 343-353 (2005).

Bahar I, Jernigan RL. Cooperative fluctuations and subunit communication in tryptophan synthase. Biochemistry 38: 3478-3490 (1999).

Barczak AJ, Zhao J, Pruitt KD, Last RL. 5-Fluoroindole resistance identifies tryptophan synthase beta subunit mutants in Arabidopsis thaliana. Genetics 140: 303-313 (1995).

Barends TR, Dunn MF, Schlichting I. Tryptophan synthase, an allosteric molecular factory. Curr. Opin. Chem. Biol. 12: 593-600 (2008).

Berlyn MB, Last RL, Fink GR. A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana. Proc. Natl. Acad. Sci. U.S.A. 86: 4604-4608 (1989).

Bilsel O, Yang L, Zitzewitz JA, Beechem JM, Matthews CR. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry 38: 4177-4187 (1999).

Bilsel O, Zitzewitz JA, Bowers KE, Matthews CR. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry 38: 1018-1029 (1999).

Blumenstein L, Domratcheva T, Niks D, Ngo H, Seidel R, Dunn MF, Schlichting I. BetaQ114N and betaT110V mutations reveal a critically important role of the substrate alpha-carboxylate site in the reaction specificity of tryptophan synthase. Biochemistry 46: 14100-14116 (2007).

Bork P, Rohde K. Sequence similarities between tryptophan synthase beta subunit and other pyridoxal-phosphate-dependent enzymes. Biochem. Biophys. Res. Commun. 171: 1319-1325 (1990).

Brzovic PS, Sawa Y, Hyde CC, Miles EW, Dunn MF. 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. J. Biol. Chem. 267: 13028-13038 (1992).

Byrne KM, Smith SK, Ondeyka JG. Biosynthesis of nodulisporic acid A: Precursor studies. J. Am. Chem. Soc. 124: 7055-7060 (2002).

Carlson JH, Wood H, Roshick C, Caldwell HD, McClarty G. In vivo and in vitro studies of Chlamydia trachomatis TrpR:DNA interactions. Mol. Microbiol. 59: 1678-1691 (2006).

Cash MT, Miles EW, Phillips RS. 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. Arch. Biochem. Biophys. 432: 233-243 (2004).

Casino P, Niks D, Ngo H, Pan P, Brzovic P, Blumenstein L, Barends TR, Schlichting I, Dunn MF. Allosteric regulation of tryptophan synthase channeling: the internal aldimine probed by trans-3-indole-3'-acrylate binding. Biochemistry 46: 7728-7739 (2007).

Cohn W, Crawford IP. Regulation of enzyme synthesis in the tryptophan pathway of Acinetobacter calcoaceticus. J. Bacteriol. 127: 367-379 (1976).

Conrado RJ, Varner JD, Delisa MP. Engineering the spatial organization of metabolic enzymes: mimicking nature's synergy. Curr. Opin. Biotechnol. 19: 492-499 (2008).

Crawford IP, Eberly L. DNA sequence of the tryptophan synthase genes of Pseudomonas putida. Biochimie 71: 521-531 (1989).

Denessiouk KA, Denesyuk AI, Lehtonen JV, Korpela T, Johnson MS. Common structural elements in the architecture of the cofactor-binding domains in unrelated families of pyridoxal phosphate-dependent enzymes. Proteins 35: 250-261 (1999).

Dias MV, Canduri F, da Silveira NJ, Czekster CM, Basso LA, Palma MS, Santos DS, de Azevedo WF Jr. Molecular models of tryptophan synthase from Mycobacterium tuberculosis complexed with inhibitors. Cell. Biochem. Biophys. 44: 375-384 (2006).

Ding Y, Williams RM, Sherman DH. Molecular analysis of a 4-dimethylallyltryptophan synthase from Malbranchea aurantiaca. J. Biol. Chem. 283: 16068-16076 (2008).

Dosselaere F, Lambrecht M, Vanderleyden J. Isolation and sequence analysis of the trpBA gene cluster, encoding tryptophan synthase, from Azospirillum brasilense. DNA Seq. 11: 287-293 (2000).

Dunn MF, Aguilar V, Brzovic P, Drewe WF Jr, Houben KF, Leja CA, Roy M. The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel. Biochemistry 29: 8598-8607 (1990).

Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I. Tryptophan synthase: the workings of a channeling nanomachine. Trends Biochem. Sci. 33: 254-264 (2008).

Eckert SE, Kubler E, Hoffmann B, Braus GH. The tryptophan synthase-encoding trpB gene of Aspergillus nidulans is regulated by the cross-pathway control system. Mol. Gen. Genet. 263: 867-876 (2000).

Facchini PJ, DiCosmo F. Secondary metabolite biosynthesis in cultured cells of Catharanthus roseus (L.) G. Don immobilized by adhesion to glass fibres. Appl. Microbiol. Biotechnol. 35: 382-392 (1991).

Fan YX, McPhie P, Miles EW. Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects. Biochemistry 39: 4692-4703 (2000).

Fan YX, McPhie P, Miles EW. Thermal repair of tryptophan synthase mutations in a regulatory intersubunit salt bridge. Evidence from arrhenius plots, absorption spectra, and primary kinetic isotope effects. J. Biol. Chem. 275: 20302-20307 (2000).

Fan YX, McPhie P, Miles EW. Guanidine hydrochloride exerts dual effects on the tryptophan synthase alpha 2 beta 2 complex as a cation activator and as a modulator of the active site conformation. Biochemistry 38: 7881-7890 (1999).

Ferrari D, Niks D, Yang LH, Miles EW, Dunn MF. Allosteric communication in the tryptophan synthase bienzyme complex: roles of the beta-subunit aspartate 305-arginine 141 salt bridge. Biochemistry 42: 7807-7818 (2003).

Ferrari D, Yang LH, Miles EW, Dunn MF. Beta D305a mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity. Biochemistry 40: 7421-7432 (2001).

Finke JM, Onuchic JN. Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape. Biophys. J. 89: 488-505 (2005).

Frey M, Chomet P, Glawischnig E, Stettner C, Grun S, Winklmair A, Eisenreich W, Bacher A, Meeley RB, Briggs SP, Simcox K, Gierl A. Analysis of a chemical plant defense mechanism in grasses. Science 277: 696-699 (1997).

Frey M, Stettner C, Pare PW, Schmelz EA, Tumlinson JH, Gierl A. An herbivore elicitor activates the gene for indole emission in maize. Proc. Natl. Acad. Sci. U.S.A. 97: 14801-14806 (2000).

Fujiwara K, Okamura-Ikeda K, Motokawa Y. Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system. Biochem. Biophys. Res. Commun. 149: 621-627 (1987).

Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic S, Huber R, Laber B, Bourenkov GP, Clausen T. Structure and function of threonine synthase from yeast. J. Biol. Chem. 277: 12396-12405 (2002).

Gast DA, Jenal U, Wasserfallen A, Leisinger T. Regulation of tryptophan biosynthesis in Methanobacterium thermoautotrophicum Marburg. J. Bacteriol. 176: 4590-4596 (1994).

Gast DA, Wasserfallen A, Pfister P, Ragettli S, Leisinger T. Characterization of Methanobacterium thermoautotrophicum Marburg mutants defective in regulation of L-tryptophan biosynthesis. J. Bacteriol. 179: 3664-3669 (1997).

Goss RJ, Newill PL. A convenient enzymatic synthesis of L-halotryptophans. Chem. Commun. (Camb.) 47: 4924-4925 (2006).

Grenville-Briggs LJ, Avrova AO, Bruce CR, Williams A, Whisson SC, Birch PR, van West P. Elevated amino acid biosynthesis in Phytophthora infestans during appressorium formation and potato infection. Fungal Genet. Biol. 42: 244-256 (2005).

Gu Z, Zitzewitz JA, Matthews CR. Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus. J. Mol. Biol. 368: 582-594 (2007).

Hadero A, Crawford IP. Nucleotide sequence of the genes for tryptophan synthase in Pseudomonas aeruginosa. Mol. Biol. Evol. 3: 191-204 (1986).

Hardin A, Villalta CF, Doan M, Jabri M, Chockalingham V, White SJ, Fowler RG. A molecular characterization of spontaneous frameshift mutagenesis within the trpA gene of Escherichia coli. DNA Repair (Amst.) 6: 177-189 (2007).

Harris RM, Ngo H, Dunn MF. Synergistic effects on escape of a ligand from the closed tryptophan synthase bienzyme complex. Biochemistry 44: 16886-16895 (2005).

Hettwer S, Sterner R. A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima - Quaternary structure, steady-state kinetics, and putative physiological role. J. Biol. Chem. 277: 8194-8201 (2002).

Hioki Y, Ogasahara K, Lee SJ, Ma J, Ishida M, Yamagata Y, Matsuura Y, Ota M, Ikeguchi M, Kuramitsu S, Yutani K. The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors. Eur. J. Biochem. 271: 2624-2635 (2004).

Hiraga K, Yamagishi A, Oshima T. Mapping of unit boundaries of a protein: exhaustive search for permissive sites for duplication by complementation analysis of random fragment libraries of tryptophan synthase alpha subunit. J. Mol. Biol. 335: 1093-1104 (2004).

Hiraga K, Yutani K. Roles of hydrogen bonding residues in the interaction between the alpha and beta subunits in the tryptophan synthase complex. Asn-104 of the alpha subunit is especially important. J. Biol. Chem. 272: 4935-4940 (1997).

Hocker B, Beismann-Driemeyer S, Hettwer S, Lustig A, Sterner R. Dissection of a (beta alpha)(8)-barrel enzyme into two folded halves. Nat. Struct. Biol. 8: 32-36 (2001).

Hsiao P, Sanjaya, Su RC, Teixeira da Silva JA, Chan MT. Plant native tryptophan synthase beta 1 gene is a non-antibiotic selection marker for plant transformation. Planta 225: 897-906 (2007).

Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H. Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms. J. Biol. Chem. 276: 38210-38216 (2001).

Huang X, Holden HM, Raushel FM. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70: 149-180 (2001).

Hurle MR, Tweedy NB, Matthews CR. Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. Biochemistry 25: 6356-6360 (1986).

Hyde CC, Miles EW. The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis. Biotechnology (N.Y.) 8: 27-32 (1990).

Ishiwata K, Fukuhara N, Shimada M, Makiguchi N, Soda K. Enzymatic production of L-tryptophan from DL-serine and indole by a coupled reaction of tryptophan synthase and amino acid racemase. Biotechnol. Appl. Biochem. 12: 141-149 (1990).

Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH. Crystal structure of tryptophanase. J. Mol. Biol. 276: 603-623 (1998).

Jacobs DI, Gaspari M, van der Greef J, van der Heijden R, Verpoorte R. Proteome analysis of the medicinal plant Catharanthus roseus. Planta 221: 690-704 (2005).

Jansonius JN. Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8: 759-769 (1998).

Jeong MS, Jang SB. Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli. Mol. Cells 19: 219-222 (2005).

Jeong MS, Jeong JK, Lim WK, Jang SB. Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli. Biochem. Biophys. Res. Commun. 323: 1257-1264 (2004).

Jeong MS, Jeong JK, Park KS, Kim HT, Lee KM, Lim WK, Jang SB. Crystallization and preliminary X-ray analysis of tryptophan synthase alpha-subunits from Escherichia coli. Acta Crystallogr. D. Biol. Crystallogr. 60: 132-134 (2004).

Jhee KH, McPhie P, Miles EW. Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein. J. Biol. Chem. 275: 11541-11544 (2000).

Jhee KH, Niks D, McPhie P, Dunn MF, Miles EW. The reaction of yeast cystathionine beta-synthase is rate-limited by the conversion of aminoacrylate to cystathionine. Biochemistry 40: 1087-10880 (2001).

Jhee KH, Yang LH, Ahmed SA, McPhie P, Rowlett R, Miles EW. Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry. J. Biol. Chem. 273: 11417-11422 (1998).

Kato A, Yutani K. Correlation of surface properties with conformational stabilities of wild-type and six mutant tryptophan synthase alpha-subunits substituted at the same position. Protein Eng. 2: 153-156 (1988).

Kawasaki H, Bauerle R, Zon G, Ahmed SA, Miles EW. 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. J. Biol. Chem. 262: 10678-10683 (1987).

Kayastha AM, Sawa Y, Nagata S, Kanzaki H, Miles EW. 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. Indian J. Biochem. Biophys. 28: 352-357 (1991).

Kayastha AM, Sawa Y, Nagata S, Miles EW. Site-directed mutagenesis of the beta subunit of tryptophan synthase from Salmonella typhimurium. Role of active site glutamic acid 350. J. Biol. Chem. 266: 7618-7625 (1991).

Kim JW, Kim EY, Park HH, Jung JE, Kim HD, Shin HJ, Lim WK. Homodimers of mutant tryptophan synthase alpha-subunits in Escherichia coli. Biochem. Biophys. Res. Commun. 289: 568-572 (2001).

Kisaka H, Kisaka M, Lee HY, Kameya T. Isolation of a cDNA for tryptophan synthase beta from rice and studies of its expression in a 5-methyltryptophan-resistant mutant of rice. Plant Mol. Biol. 38: 875-878 (1998).

Knaggs AR. The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 18: 334-355 (2001).

Kramer VC, Koziel MG. Structure of a maize tryptophan synthase alpha subunit gene with pith enhanced expression. Plant Mol. Biol. 27: 1183-1188 (1995).

Kremer A, Li SM. Potential of a 7-dimethylallyltryptophan synthase as a tool for production of prenylated indole derivatives. Appl. Microbiol. Biotechnol. 79: 951-961 (2008).

Kremer A, Westrich L, Li SM. A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization. Microbiology 153: 3409-3416 (2007).

Kriechbaumer V, Weigang L, Fiesselmann A, Letzel T, Frey M, Gierl A, Glawischnig E. Characterisation of the tryptophan synthase alpha subunit in maize. BMC Plant Biol. 8: 44 (2008).

Kulik V, Hartmann E, Weyand M, Frey M, Gierl A, Niks D, Dunn MF, Schlichting I. 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. J. Mol. Biol. 352: 608-620 (2005).

Last RL, Bissinger PH, Mahoney DJ, Radwanski ER, Fink GR. Tryptophan mutants in Arabidopsis: the consequences of duplicated tryptophan synthase beta genes. Plant Cell 3: 345-358 (1991).

Lee SJ, Ogasahara K, Ma J, Nishio K, Ishida M, Yamagata Y, Tsukihara T, Yutani K. Conformational changes in the tryptophan synthase from a hyperthermophile upon alpha(2)beta(2) complex formation: crystal structure of the complex. Biochemistry 44: 11417-11427 (2005).

Leopoldseder S, Hettwer S, Sterner R. Evolution of multi-enzyme complexes: the case of tryptophan synthase. Biochemistry 45: 14111-14119 (2006).

Levy S, Danchin A. Phylogeny of metabolic pathways: O-acetylserine sulphydrylase A is homologous to the tryptophan synthase beta subunit. Mol. Microbiol. 2: 777-783 (1988).

Li SM. Evolution of aromatic prenyltransferases in the biosynthesis of indole derivatives. Phytochemistry Apr 25 [Epub ahead of print] (2009).

Lim WK, Sarkar SK, Hardman JK. Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits. J. Biol. Chem. 266: 20205-20212 (1991).

Lim WK, Shin HJ, Milton DL, Hardman JK. Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. J. Bacteriol. 173: 1886-1893 (1991).

Ljung K, Hull AK, Kowalczyk M, Marchant A, Celenza J, Cohen JD, Sandberg G. Biosynthesis, conjugation, catabolism and homeostasis of indole-3-acetic acid in Arabidopsis thaliana. Plant Mol. Biol. 49: 249-272 (2002).

Loeffler C, Berger S, Guy A, Durand T, Bringmann G, Dreyer M, von Rad U, Durner J, Mueller MJ. B1-phytoprostanes trigger plant defense and detoxification responses. Plant Physiol. 137: 328-340 (2005).

Lu H, Gorman E, McKnight TD. Molecular characterization of two anthranilate synthase alpha subunit genes in Camptotheca acuminata. Planta 221: 352-360 (2005).

Lu H, McKnight TD. Tissue-specific expression of the beta-subunit of tryptophan synthase in Camptotheca acuminata, an indole alkaloid-producing plant. Plant Physiol. 120: 43-52 (1999).

Marabotti A, Cozzini P, Mozzarelli A. Novel allosteric effectors of the tryptophan synthase alpha(2)beta(2) complex identified by computer-assisted molecular modeling. Biochim. Biophys. Acta 1476: 287-299 (2000).

Marabotti A, De Biase D, Tramonti A, Bettati S, Mozzarelli A. Allosteric communication of tryptophan synthase. Functional and regulatory properties of the beta S178P mutant. J. Biol. Chem. 276: 17747-17753 (2001).

Matchett WH, Lacy AM, DeMoss JA. Orientation of enzymic domains in tryptophan synthase of Neurospora crassa: an immunoblot analysis of TRP3 mutant products. Mol. Gen. Genet. 208: 398-407 (1987).

Meier M, Janosik M, Kery V, Kraus JP, Burkhard P. Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 20: 3910-3916 (2001).

Melanson D, Chilton MD, Masters-Moore D, Chilton WS. A deletion in an indole synthase gene is responsible for the DIMBOA-deficient phenotype of bxbx maize. Proc. Natl. Acad. Sci. U.S.A. 94: 13345-13350 (1997).

Merkl R. Modelling the evolution of the archeal tryptophan synthase. BMC Evol. Biol. 7: 59 (2007).

Miles EW, Kawasaki H, Ahmed SA, Morita H, Morita H, Nagata S. The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230. J. Biol. Chem. 264: 6280-6287 (1989).

Miles EW, McPhie P, Yutani K. Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit. J. Biol. Chem. 263: 8611-8614 (1988).

Milton DL, Napier ML, Myers RM, Hardman JK. In vitro mutagenesis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant alpha-subunits. J. Biol. Chem. 261: 16604-16615 (1986).

Mosteller RD. Improved method for measuring the catalytic activity of tryptophan synthase alpha subunit in cell extracts. Biochimie 72: 881-884 (1990).

Mozzarelli A, Bettati S. Exploring the pyridoxal 5'-phosphate-dependent enzymes. Chem. Rec. 6: 275-287 (2006).

Mozzarelli A, Peracchi A, Rovegno B, Dale G, Rossi GL, Dunn MF. Effect of pH and monovalent cations on the formation of quinonoid intermediates of the tryptophan synthase alpha(2)beta(2) complex in solution and in the crystal. J. Biol. Chem. 275: 6956-6962 (2000).

Muller A, Weiler EW. Indolic constituents and indole-3-acetic acid biosynthesis in the wild-type and a tryptophan auxotroph mutant of Arabidopsis thaliana. Planta 211: 855-863 (2000).

Murry-Brelier A, Goldberg ME. Mechanism of inactivation of the beta 2 subunit of Escherichia coli tryptophan synthase by monoclonal antibodies. J. Biol. Chem. 265: 7987-7993 (1990).

Navon A, Schulze AJ, Guillou Y, Zylinski CA, Baleux F, Expert-Bezancon N, Friguet B, Djavadi-Ohaniance L, Goldberg ME. Importance of residues 2-9 in the immunoreactivity, subunit interactions, and activity of the beta 2 subunit of Escherichia coli tryptophan synthase. J. Biol. Chem. 270: 4255-4261 (1995).

Nelson DE, Virok DP, Wood H, Roshick C, Johnson RM, Whitmire WM, Crane DD, Steele-Mortimer O, Kari L, McClarty G, Caldwell HD. Chlamydial IFN-gamma immune evasion is linked to host infection tropism. Proc. Natl. Acad. Sci. U.S.A. 102: 10658-10663 (2005).

Ngo H, Harris R, Kimmich N, Casino P, Niks D, Blumenstein L, Barends TR, Kulik V, Weyand M, Schlichting I, Dunn MF. Synthesis and characterization of allosteric probes of substrate channeling in the tryptophan synthase bienzyme complex. Biochemistry 46: 7713-7727 (2007).

Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF. 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. Biochemistry 46: 7740-7753 (2007).

Nibeilliu ME, Malthouse JP. The stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acids. Biochem. J. 381: 847-852 (2004).

Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. Biochemistry 44: 1184-1192 (2005).

O'Gara JP, Dunican LK. Direct evidence for a constitutive internal promoter in the tryptophan operon of Corynebacterium glutamicum. Biochem. Biophys. Res. Commun. 203: 820-827 (1994).

Ogasahara K, Hiraga K, Ito W, Miles EW, Yutani K. Origin of the mutual activation of the alpha and beta 2 subunits in the alpha 2 beta 2 complex of tryptophan synthase. Effect of alanine or glycine substitutions at proline residues in the alpha subunit. J. Biol. Chem. 267: 5222-5228 (1992).

Osborne A, Teng Q, Miles EW, Phillips RS. Detection of open and closed conformations of tryptophan synthase by 15N-heteronuclear single-quantum coherence nuclear magnetic resonance of bound 1-15N-L-tryptophan. J. Biol. Chem. 278: 44083-44090 (2003).

Palombella AL, Dutcher SK. Identification of the gene encoding the tryptophan synthase beta-subunit from Chlamydomonas reinhardtii. Plant Physiol. 117: 455-464 (1998).

Pan P, Woehl E, Dunn MF. Protein architecture, dynamics and allostery in tryptophan synthase channeling. Trends Biochem. Sci. 22: 22-27 (1997).

Parsot C. A common origin for enzymes involved in the terminal step of the threonine and tryptophan biosynthetic pathways. Proc. Natl. Acad. Sci. U.S.A. 84: 5207-5210 (1987).

Phillips RS, Dua RK. Indole protects tryptophan indole-lyase, but not tryptophan synthase, from inactivation by trifluoroalanine. Arch. Biochem. Biophys. 296: 489-496 (1992).

Phillips RS, McPhie P, Miles EW, Marchal S, Lange R. Quantitative effects of allosteric ligands and mutations on conformational equilibria in Salmonella typhimurium tryptophan synthase. Arch. Biochem. Biophys. 470: 8-19 (2008).

Phillips RS, Miles EW, Holtermann G, Goody RS. Hydrostatic pressure affects the conformational equilibrium of Salmonella typhimurium tryptophan synthase. Biochemistry 44: 7921-7928 (2005).

Pioselli B, Bettati S, Mozzarelli A. Confinement and crowding effects on tryptophan synthase alpha2beta2 complex. FEBS Lett. 579: 2197-2202 (2005).

Prasad CK, Vineetha KE, Hassani R, Gupta R, Randhawa GS. Isolation and symbiotic characterization of aromatic amino acid auxotrophs of Sinorhizobium meliloti. Indian J. Exp. Biol. 38: 1041-1049 (2000).

Proctor AR, Crawford IP. Autogenous regulation of the inducible tryptophan synthase of Pseudomonas putida. Proc. Natl. Acad. Sci. U.S.A. 72: 1249-1253 (1975).

Pruitt KD, Last RL. Expression patterns of duplicate tryptophan synthase beta genes in Arabidopsis thaliana. Plant Physiol. 102: 1019-1026 (1993).

Rabeh WM, Mather T, Cook PF. A three-dimensional homology model of the O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Protein Pept. Lett. 13: 7-13 (2006).

Raboni S, Bettati S, Mozzarelli A. Identification of the geometric requirements for allosteric communication between the alpha- and beta-subunits of tryptophan synthase. J. Biol. Chem. 280: 13450-13456 (2005).

Raboni S, Mozzarelli A, Cook PF. Control of ionizable residues in the catalytic mechanism of tryptophan synthase from Salmonella typhimurium. Biochemistry 46: 13223-13234 (2007).

Radwanski ER, Barczak AJ, Last RL. Characterization of tryptophan synthase alpha subunit mutants of Arabidopsis thaliana. Mol. Gen. Genet. 253: 353-361 (1996).

Radwanski ER, Zhao J, Last RL. Arabidopsis thaliana tryptophan synthase alpha: gene cloning, expression, and subunit interaction. Mol. Gen. Genet. 248: 657-667 (1995).

Raushel FM, Thoden JB, Holden HM. Enzymes with molecular tunnels. Acc. Chem. Res. 36: 539-548 (2003).

Raushel FM, Thoden JB, Holden HM. The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia. Biochemistry 38: 7891-7899 (1999).

Rekoslavskaya NI, Kuznetsova EV, Vysotskaya EF, Salyaev RK. Tryptophan synthase from Agrobacterium tumefaciens 8628: isolation and properties. Biochemistry (Mosc.) 62: 433-439 (1997).

Ro HS, Miles EW. Catalytic mechanism of the tryptophan synthase alpha(2)beta(2) complex. Effects of pH, isotopic substitution, and allosteric ligands. J. Biol. Chem. 274: 31189-31194 (1999).

Rohr J, Sarkar N, Balenger S, Jeong BR, Cerutti H. Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas. Plant J. 40: 611-621 (2004).

Rojsajjakul T, Wintrode P, Vadrevu R, Robert Matthews C, Smith DL. Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry. J. Mol. Biol. 341: 241-253 (2004).

Rondard P, Bedouelle H. Mutational scanning of a hairpin loop in the tryptophan synthase beta-subunit implicated in allostery and substrate channeling. Biol. Chem. 381: 1185-1193 (2000).

Rutherford R, Gallois P, Masson PH. Mutations in Arabidopsis thaliana genes involved in the tryptophan biosynthesis pathway affect root waving on tilted agar surfaces. Plant J. 16: 145-154 (1998).

Ruvinov SB, Miles EW. Subunit communication in the tryptophan synthase alpha 2 beta 2 complex. Effects of beta subunit ligands on proteolytic cleavage of a flexible loop in the alpha subunit. FEBS Lett. 299: 197-200 (1992).

Saab-Rincon G, Juarez VR, Osuna J, Sanchez F, Soberon X. Different strategies to recover the activity of monomeric triosephosphate isomerase by directed evolution. Protein Eng. 14: 149-155 (2001).

Salvini M, Boccardi TM, Sani E, Bernardi R, Tozzi S, Pugliesi C, Durante M. Alpha-tryptophan synthase of Isatis tinctoria: gene cloning and expression. Plant Physiol. Biochem. 46: 715-723 (2008).

Sanjayae , Hsiao PY, Su RC, Ko SS, Tong CG, Yang RY, Chan MT. Overexpression of Arabidopsis thaliana tryptophan synthase beta 1 (AtTSB1) in Arabidopsis and tomato confers tolerance to cadmium stress. Plant Cell Environ. 31: 1074-1085 (2008).

Schiaretti F, Bettati S, Viappiani C, Mozzarelli A. pH dependence of tryptophan synthase catalytic mechanism: I. The first stage, the beta-elimination reaction. J. Biol. Chem. 279: 29572-29582 (2004).

Schlichting I, Yang XJ, Miles EW, Kim AY, Anderson KS. Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthase. J. Biol. Chem. 269: 26591-26593 (1994).

Schneider B, Knochel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R. Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity. Biochemistry 44: 16405-16412 (2005).

Shaw AC, Christiansen G, Roepstorff P, Birkelund S. Genetic differences in the Chlamydia trachomatis tryptophan synthase alpha-subunit can explain variations in serovar pathogenesis. Microbes Infect. 2: 581-592 (2000).

Spiteller P, Steglich W. Biosynthesis of 2-aminobenzaldehyde in flowers of Robinia pseudoacacia and Philadelphus coronarius. Phytochemistry 57: 361-363 (2001).

Spyrakis F, Raboni S, Cozzini P, Bettati S, Mozzarelli A. Allosteric communication between alpha and beta subunits of tryptophan synthase: modelling the open-closed transition of the alpha subunit. Biochim. Biophys. Acta 1764: 1102-1109 (2006).

Swift S, Kuhn J, Stewart GS. Selection and analysis of non-interactive mutants in the Escherichia coli tryptophan synthase alpha subunit. Mol. Gen. Genet. 233: 129-135 (1992).

Tai CH, Cook PF. O-acetylserine sulfhydrylase. Advan. Enzymol. Relat. Areas Mol. Biol. 74: 185-239 (2000).

Tang X, Ezaki S, Fujiwara S, Takagi M, Atomi H, Imanaka T. The tryptophan biosynthesis gene cluster trpCDEGFBA from Pyrococcus kodakaraensis KOD1 is regulated at the transcriptional level and expressed as a single mRNA. Mol. Gen. Genet. 262: 815-821 (1999).

Tang XF, Ezaki S, Atomi H, Imanaka T. Biochemical analysis of a thermostable tryptophan synthase from a hyperthermophilic archaeon. Eur. J. Biochem. 267: 6369-6377 (2000).

Tsai CJ, Ma BY, Kumar S, Wolfson H, Nussinov R. Protein folding: Binding of conformationally fluctuating building blocks via population selection. Crit. Rev. Biochem. Mol. Biol. 36: 399-433 (2001).

Tudzynski P, Holter K, Correia T, Arntz C, Grammel N, Keller U. Evidence for an ergot alkaloid gene cluster in Claviceps purpurea. Mol. Gen. Genet. 261: 133-141 (1999).

Usha R, Savithri HS, Rao NA. The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases. Biochim. Biophys. Acta 1204: 75-83 (1994).

Vadrevu R, Wu Y, Matthews CR. NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein. J. Mol. Biol. 377: 294-306 (2008).

Wallace W. Comparison of a nitrate reductase-inactivating enzyme from the maize root with a protease form yeast which inactivates tryptophan synthase. Biochim. Biophys. Acta 524: 418-427 (1978).

Watkins EB, Phillips RS. Inhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine. Biochemistry 40: 14862-14868 (2001).

Weber-Ban E, Hur O, Bagwell C, Banik U, Yang LH, Miles EW, Dunn MF. Investigation of allosteric linkages in the regulation of tryptophan synthase: the roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics. Biochemistry 40: 3497-3511 (2001).

Weigent DA, Nester EW. Regulation of histidinol phosphate aminotransferase synthesis by tryptophan in Bacillus subtilis. J. Bacteriol. 128: 202-211 (1976).

Weischet WO, Kirschner K. The binding of indole to the alpha-subunit and beta2-subunit and to the alpha2beta2-complex of tryptophan synthase from Escherichia coli. Identification of a second indole-binding site on the alpha-subunit. Eur. J. Biochem. 64: 313-320 (1976).

Welch M, Phillips RS. Enzymatic syntheses of 6-(4H-selenolo[3,2-b]pyrrolyl)-L-alanine, 4-(6H-selenolo[2,3-b]pyrrolyl)-L-alanine, and 6-(4H-furo[3,2-b]pyrrolyl-L-alanine. Bioorg. Med. Chem. Lett. 9: 637-640 (1999).

Weyand M, Schlichting I. Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase. J. Biol. Chem. 275: 41058-41063 (2000).

Weyand M, Schlichting I, Herde P, Marabotti A, Mozzarelli A. Crystal structure of the beta Ser(178) -> Pro mutant of tryptophan synthase - A "knock-out" allosteric enzyme. J. Biol. Chem. 277: 10653-10660 (2002).

Weyand M, Schlichting I, Marabotti A, Mozzarelli A. Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase. J. Biol. Chem. 277: 10647-10652 (2002).

Wilmanns M, Hyde CC, Davies DR, Kirschner K, Jansonius JN. Structural conservation in parallel beta/alpha-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry 30: 9161-9169 (1991).

Winn M, Roy AD, Gruschow S, Parameswaran RS, Goss RJ. A convenient one-step synthesis of L-aminotryptophans and improved synthesis of 5-fluorotryptophan. Bioorg. Med. Chem. Lett. 18: 4508-4510 (2008).

Wintrode PL, Rojsajjakul T, Vadrevu R, Matthews CR, Smith DL. An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein. J. Mol. Biol. 347: 911-919 (2005).

Woehl E, Dunn MF. Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions. Biochemistry 38: 7131-7141 (1999).

Woehl E, Dunn MF. Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reaction. Biochemistry 38: 7118-7130 (1999).

Wood H, Fehlner-Gardner C, Berry J, Fischer E, Graham B, Hackstadt T, Roshick C, McClarty G. Regulation of tryptophan synthase gene expression in Chlamydia trachomatis. Mol. Microbiol. 49: 1347-1359 (2003).

Woolridge EM, Rokita SE. The use of 6-(difluoromethyl)indole to study the activation of indole by tryptophan synthase. Arch. Biochem. Biophys. 286: 473-480 (1991).

Wright AD, Moehlenkamp CA, Perrot GH, Neuffer MG, Cone KC. The maize auxotrophic mutant orange pericarp is defective in duplicate genes for tryptophan synthase beta. Plant Cell 4: 711-719 (1992).

Wu Y, Matthews CR. Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein. J. Mol. Biol. 330: 1131-1144 (2003).

Wu Y, Vadrevu R, Yang X, Matthews CR. Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein. J. Mol. Biol. 351: 445-452 (2005).

Xu Y, Abeles RH. Inhibition of tryptophan synthase by (1-fluorovinyl)glycine. Biochemistry 32: 806-811 (1993).

Yamagata Y, Ogasahara K, Hioki Y, Lee SJ, Nakagawa A, Nakamura H, Ishida M, Kuramitsu S, Yutani K. Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry. J. Biol. Chem. 276: 11062-11071 (2001).

Yang Lh, Ahmed SA, Miles EW. PCR mutagenesis and overexpression of tryptophan synthase from Salmonella typhimurium: on the roles of beta2 subunit Lys-382. Protein Expr. Purif. 8: 126-136 (1996).

Yang X, Vadrevu R, Wu Y, Matthews CR. Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase. Protein Sci. 16: 1398-1409 (2007).

Yang XJ, Miles EW. A novel intersubunit repair mechanism in the tryptophan synthase alpha 2 beta 2 complex. Critical role of the beta subunit lysine 167 in intersubunit communication. J. Biol. Chem. 268: 22269-22272 (1993).

Yang XJ, Ruvinov SB, Miles EW. Overexpression and purification of the separate tryptophan synthase alpha and beta subunits from Salmonella typhimurium. Protein Expr. Purif. 3: 347-354 (1992).

Yanofsky C. The favorable features of tryptophan synthase for proving Beadle and Tatum's one gene-one enzyme hypothesis. Genetics 169: 511-516 (2005).

Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I. Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus. J. Biol. Chem. 275: 34557-34565 (2000).

Yutani K, Ogasahara K, Tsujita T, Kanemoto K, Matsumoto M, Tanaka S, Miyashita T, Matsushiro A, Sugino Y, Miles EW. Tryptophan synthase alpha subunit glutamic acid 49 is essential for activity. Studies with 19 mutants at position 49. J. Biol. Chem. 262: 13429-13433 (1987).

Zalkin H, Yanofsky C. Yeast gene TRP5: structure, function, regulation. J. Biol. Chem. 257: 1491-1500 (1982).

Zhao GP, Somerville RL. Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility. J. Biol. Chem. 267: 526-541 (1992).

Zhao GP, Somerville RL. 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. J. Biol. Chem. 268: 14921-14931 (1993).

Zhao GP, Somerville RL, Chitnis PR. Synechocystis PCC 6803 contains a single gene for the beta subunit of tryptophan synthase with strong homology to the trpB genes of Arabidopsis and maize (Zea mays L.). Plant Physiol. 104: 461-466 (1994).

Zhao J, Last RL. Immunological characterization and chloroplast localization of the tryptophan biosynthetic enzymes of the flowering plant Arabidopsis thaliana. J. Biol. Chem. 270: 6081-6087 (1995).

Zitzewitz JA, Gualfetti PJ, Perkons IA, Wasta SA, Matthews CR. Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. Protein Sci. 8: 1200-1209 (1999).

Zook M. Biosynthesis of camalexin from tryptophan pathway intermediates in cell-suspension cultures of Arabidopsis. Plant Physiol. 118: 1389-1393 (1998).

Number of references = 192