메뉴 건너뛰기




Volumn 44, Issue 51, 2005, Pages 16886-16895

Synergistic effects on escape of a ligand from the closed tryptophan synthase bienzyme complex

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; COMPLEXATION; ENZYME KINETICS; PHOSPHATES; SUBSTRATES;

EID: 29344444790     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0516881     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 77956903741 scopus 로고
    • Tryptophan synthase
    • (Boyer, P. D., Ed.), Academic Press, New York
    • Yanofsky, C., and Crawford, I. P. (1972) Tryptophan synthase, in The Enzymes (Boyer, P. D., Ed.) Vol. 7, pp 1-31, Academic Press, New York.
    • (1972) Enzymes , vol.7 , pp. 1-31
    • Yanofsky, C.1    Crawford, I.P.2
  • 2
    • 0018657645 scopus 로고
    • Tryptophan synthase: Structure, function and subunit interaction
    • Miles, E. W. (1979) Tryptophan synthase: Structure, function and subunit interaction. Adv. Enzymol. Relat. Areas Mol. Biol. 49, 127-186.
    • (1979) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.49 , pp. 127-186
    • Miles, E.W.1
  • 3
    • 0026086276 scopus 로고
    • Structural basis for catalysis by tryptophan synthase
    • Miles, E. W. (1991) Structural basis for catalysis by tryptophan synthase, Adv. Enzymol. Relat. Areas Mol. Biol. 64, 93-172.
    • (1991) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.64 , pp. 93-172
    • Miles, E.W.1
  • 4
    • 0029204814 scopus 로고
    • Proteins: Structure, function and protein engineering
    • (Biswas, B. B., and Roy, S., Eds.), Plenum Press, New York
    • Miles, E. W. (1995) Proteins: structure, function and protein engineering, in Subcellular Biochemistry (Biswas, B. B., and Roy, S., Eds.) Vol. 24, pp 207-254, Plenum Press, New York.
    • (1995) Subcellular Biochemistry , vol.24 , pp. 207-254
    • Miles, E.W.1
  • 5
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles, E. W., Rhee, S., and Davies, D. R. (1999) The molecular basis of substrate channeling, J. Biol. Chem. 274, 12193-12196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12193-12196
    • Miles, E.W.1    Rhee, S.2    Davies, D.R.3
  • 7
    • 0025006579 scopus 로고
    • The tryptophan synthase bienzyme complex transfers indole between the α- and β-sites via a 25-30 Å-long tunnel
    • Dunn, M. F., Aguilar, V., Brzovic', P., Drewe, W. F., Houben, K. F., Leja, C. A., and Roy, M. (1990) The tryptophan synthase bienzyme complex transfers indole between the α- and β-sites via a 25-30 Å-long tunnel, Biochemistry 29, 8598-8607.
    • (1990) Biochemistry , vol.29 , pp. 8598-8607
    • Dunn, M.F.1    Aguilar, V.2    Brzovic, P.3    Drewe, W.F.4    Houben, K.F.5    Leja, C.A.6    Roy, M.7
  • 8
    • 0026715868 scopus 로고
    • Evidence that mutations in a loop region of the α-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex
    • Brzovic, P. S., Sawa, Y., Miles, E. W., and Dunn, M. F. (1992) Evidence that mutations in a loop region of the α-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex, J. Biol. Chem. 267, 13028-13038.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13028-13038
    • Brzovic, P.S.1    Sawa, Y.2    Miles, E.W.3    Dunn, M.F.4
  • 9
    • 0027440693 scopus 로고
    • Characterization of the functional role of a flexible loop in the α-subunit of tryptophan synthase from S. typhimurium by rapid-scanning stopped-flow spectroscopy and site-directed mutagenesis
    • Brzovic, P. S., Hyde, C. C., Miles, E. W., and Dunn, M. F. (1993) Characterization of the functional role of a flexible loop in the α-subunit of tryptophan synthase from S. typhimurium by rapid-scanning stopped-flow spectroscopy and site-directed mutagenesis. Biochemistry 32, 10404-10413.
    • (1993) Biochemistry , vol.32 , pp. 10404-10413
    • Brzovic, P.S.1    Hyde, C.C.2    Miles, E.W.3    Dunn, M.F.4
  • 10
    • 0025975619 scopus 로고
    • Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli
    • Lane, A. N., and Kirschner, K. (1991) Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli, Biochemistry 30, 479-484.
    • (1991) Biochemistry , vol.30 , pp. 479-484
    • Lane, A.N.1    Kirschner, K.2
  • 11
    • 0025916089 scopus 로고
    • Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism
    • Anderson, K. S., Miles, E. W., and Johnson, K. A. (1991) Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism. J. Biol. Chem. 266, 8020-8033.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8020-8033
    • Anderson, K.S.1    Miles, E.W.2    Johnson, K.A.3
  • 12
    • 0031028212 scopus 로고    scopus 로고
    • Protein architecture, dynamics, and allostery in tryptophan synthase channeling
    • Pan, P., Woehl, E., and Dunn, M. F. (1997) Protein architecture, dynamics, and allostery in tryptophan synthase channeling, Trends Biochem. Sci. 22, 22-27.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 22-27
    • Pan, P.1    Woehl, E.2    Dunn, M.F.3
  • 13
    • 0026764475 scopus 로고
    • Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex
    • Brzovic, P. S., Ngo, K., and Dunn, M. F. (1992) Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex, Biochemistry 31, 3831-3839.
    • (1992) Biochemistry , vol.31 , pp. 3831-3839
    • Brzovic, P.S.1    Ngo, K.2    Dunn, M.F.3
  • 14
    • 0035957229 scopus 로고    scopus 로고
    • 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
    • Weber-Ban, E., Hur, O., Bagwell, C., Banik, U., Yang, L.-H., Miles, E. E., and Dunn, M. F. (2001) 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) Biochemistry , vol.40 , pp. 3497-3511
    • Weber-Ban, E.1    Hur, O.2    Bagwell, C.3    Banik, U.4    Yang, L.-H.5    Miles, E.E.6    Dunn, M.F.7
  • 15
    • 0029978425 scopus 로고    scopus 로고
    • β-site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex
    • Pan, P., and Dunn, M. F. (1996) β-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex, Biochemistry 35, 5002-5013.
    • (1996) Biochemistry , vol.35 , pp. 5002-5013
    • Pan, P.1    Dunn, M.F.2
  • 16
    • 0030800147 scopus 로고    scopus 로고
    • 2 complex with ligands bound to the active sites of the α and β subunits reveal ligand-induced conformational changes
    • 2 complex with ligands bound to the active sites of the α and β subunits reveal ligand-induced conformational changes, Biochemistry 36, 7664-7680.
    • (1997) Biochemistry , vol.36 , pp. 7664-7680
    • Rhee, S.1    Parris, K.D.2    Hyde, C.C.3    Ahmed, S.A.4    Miles, E.W.5    Davies, D.R.6
  • 17
    • 0037031265 scopus 로고    scopus 로고
    • + activated tryptophan synthase bienzyme complex
    • + activated tryptophan synthase bienzyme complex, Biochemistry 41, 9982-9990.
    • (2002) Biochemistry , vol.41 , pp. 9982-9990
    • Harris, R.M.1    Dunn, M.F.2
  • 18
    • 0023782859 scopus 로고
    • 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., and Dunn, M. F. (1988) Stereoelectronic control of bond formation in Escherichia coli tryptophan synthase: Substrate specificity and enzymatic synthesis of the novel amino acid dihydroisotryptophan. Biochemistry 27, 6698-6704.
    • (1988) Biochemistry , vol.27 , pp. 6698-6704
    • Roy, M.1    Keblawi, S.2    Dunn, M.F.3
  • 20
    • 0033554845 scopus 로고    scopus 로고
    • Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate
    • Weyand, M., and Schlichting, I. (1999) Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate, Biochemistry 38, 16469-16480.
    • (1999) Biochemistry , vol.38 , pp. 16469-16480
    • Weyand, M.1    Schlichting, I.2
  • 22
    • 0000723390 scopus 로고
    • Serine deamination by the B protein of Escherichia coli tryptophan synthase
    • Crawford, I. P., and Ito, J. (1964) Serine deamination by the B protein of Escherichia coli tryptophan synthase, Proc. Natl. Acad. Sci. U.S.A. 51, 390-397.
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.51 , pp. 390-397
    • Crawford, I.P.1    Ito, J.2
  • 23
    • 0017807301 scopus 로고
    • On the mechanism of action of Escherichia coli tryptophan synthase. Steady-state investigations
    • Heilmann, H. D. (1978) On the mechanism of action of Escherichia coli tryptophan synthase. Steady-state investigations, Biochim. Biophys. Acta 522, 614-624.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 614-624
    • Heilmann, H.D.1
  • 24
    • 0019778638 scopus 로고
    • The mechanism of tryptophan binding to tryptophan synthase from Escherichia coli
    • Lane, A. N., and Kirschner, K. (1981) The mechanism of tryptophan binding to tryptophan synthase from Escherichia coli. Eur. J. Biochem. 120, 379-387.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 379-387
    • Lane, A.N.1    Kirschner, K.2
  • 25
    • 0030432487 scopus 로고    scopus 로고
    • Some novel transcription attenuation mechanisms used by bacteria
    • Yanofsky, C., Konan, K. V., and Sarsero, J. P. (1996) Some novel transcription attenuation mechanisms used by bacteria, Biochimie 78, 1017-1024.
    • (1996) Biochimie , vol.78 , pp. 1017-1024
    • Yanofsky, C.1    Konan, K.V.2    Sarsero, J.P.3
  • 26
    • 0028988975 scopus 로고
    • Allosteric linkages between β-site covalent transformations and α-site activation and deactivation in the tryptophan synthase bienzyme complex
    • Leja, C. A., Woehl, E. U., and Dunn, M. F. (1995) Allosteric linkages between β-site covalent transformations and α-site activation and deactivation in the tryptophan synthase bienzyme complex, Biochemistry 34, 6552-6561.
    • (1995) Biochemistry , vol.34 , pp. 6552-6561
    • Leja, C.A.1    Woehl, E.U.2    Dunn, M.F.3
  • 27
    • 0033151768 scopus 로고    scopus 로고
    • Mechanisms of monovalent cation action in enzyme catalysis: The first stage of the tryptophan synthase β-reaction
    • Woehl, E., and Dunn, M. F. (1999) Mechanisms of monovalent cation action in enzyme catalysis: The first stage of the tryptophan synthase β-reaction, Biochemistry 38, 7118-7130.
    • (1999) Biochemistry , vol.38 , pp. 7118-7130
    • Woehl, E.1    Dunn, M.F.2
  • 28
    • 0033152545 scopus 로고    scopus 로고
    • Mechanisms of monovalent cation action in enzyme catalysis: The tryptophan synthase α-, β- and αβ-reactions
    • Woehl, E., and Dunn, M. F. (1999) Mechanisms of monovalent cation action in enzyme catalysis: The tryptophan synthase α-, β- and αβ-reactions, Biochemistry 38, 7131-7141.
    • (1999) Biochemistry , vol.38 , pp. 7131-7141
    • Woehl, E.1    Dunn, M.F.2
  • 29
    • 0033596908 scopus 로고    scopus 로고
    • Cooperative fluctuations and subunit communication in tryptophan synthase
    • Bahar, I., and Jemigan, R. L. (1999) Cooperative fluctuations and subunit communication in tryptophan synthase, Biochemistry 38, 3478-3490.
    • (1999) Biochemistry , vol.38 , pp. 3478-3490
    • Bahar, I.1    Jemigan, R.L.2
  • 30
    • 0021379507 scopus 로고
    • The mechanism of self-assembly of the multi-enzyme complex tryptophan synthase from Escherichia coli
    • Lane, A. N., Paul, C. H., and Kirschner, K. (1984) The mechanism of self-assembly of the multi-enzyme complex tryptophan synthase from Escherichia coli, EMBO J. 3, 279-287.
    • (1984) EMBO J. , vol.3 , pp. 279-287
    • Lane, A.N.1    Paul, C.H.2    Kirschner, K.3
  • 31
    • 0025216256 scopus 로고
    • Allosteric effects acting over a distance of 20-25 Å in the Escherichia coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediates
    • Houben, K. F., and Dunn, M. F. (1990) Allosteric effects acting over a distance of 20-25 Å in the Escherichia coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediates, Biochemistry 29, 2421-2429.
    • (1990) Biochemistry , vol.29 , pp. 2421-2429
    • Houben, K.F.1    Dunn, M.F.2
  • 32
    • 0032502775 scopus 로고    scopus 로고
    • 2 complex reveals the correct orientation of active site αGlu49
    • 2 complex reveals the correct orientation of active site αGlu49, J. Biol. Chem. 273, 8553-8555.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8553-8555
    • Rhee, S.1    Miles, E.W.2    Davies, D.R.3
  • 34
    • 0033613244 scopus 로고    scopus 로고
    • Crystallographic studies of phosphonate-based α-reaction transition-state analogues complexed to tryptophan synthase
    • Sachpatzidis, A., Dealwis, C., Lubetsky, J. B., Liang, P. H., Anderson, K. S., and Lolis, E. (1999) Crystallographic studies of phosphonate-based α-reaction transition-state analogues complexed to tryptophan synthase, Biochemistry 38, 12665-12674.
    • (1999) Biochemistry , vol.38 , pp. 12665-12674
    • Sachpatzidis, A.1    Dealwis, C.2    Lubetsky, J.B.3    Liang, P.H.4    Anderson, K.S.5    Lolis, E.6
  • 35
    • 0037155812 scopus 로고    scopus 로고
    • Crystal structures of a new class of allosteric effectors completed to tryptophan synthase
    • Weyand, M., Schlichting, I., Marabotti, A., and Mozzarelli, A. (2002) Crystal structures of a new class of allosteric effectors completed to tryptophan synthase, J. Biol. Chem. 277, 10647-10652.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10647-10652
    • Weyand, M.1    Schlichting, I.2    Marabotti, A.3    Mozzarelli, A.4
  • 36
    • 0036882159 scopus 로고    scopus 로고
    • On the role of αThr 183 in the allosteric regulation and catalytic mechanism of tryptophan synthase
    • Kulik, V., Weyand, M., Seidel, R., Niks, D., Arac, D., Dunn, M. F., and Schlickting, I. (2002) On the role of αThr 183 in the allosteric regulation and catalytic mechanism of tryptophan synthase. J. Mol. Biol. 324, 677-690.
    • (2002) J. Mol. Biol. , vol.324 , pp. 677-690
    • Kulik, V.1    Weyand, M.2    Seidel, R.3    Niks, D.4    Arac, D.5    Dunn, M.F.6    Schlickting, I.7
  • 37
    • 0022344850 scopus 로고
    • Detection and identification of intermediates in the reaction of L-serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
    • Drewe, W. F., Jr., and Dunn, M. F. (1985) Detection and identification of intermediates in the reaction of L-serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy, Biochemistry 24, 3977-3987.
    • (1985) Biochemistry , vol.24 , pp. 3977-3987
    • Drewe Jr., W.F.1    Dunn, M.F.2
  • 38
    • 0026794575 scopus 로고
    • Conformational changes and subunit communication in tryptophan synthase: Effect of substrates and substrate analogs
    • Strambini, G. B., Cioni, P., Peracchi, A., and Mozzarelli, A. (1992) Conformational changes and subunit communication in tryptophan synthase: effect of substrates and substrate analogs, Biochemistry 31, 7535-42.
    • (1992) Biochemistry , vol.31 , pp. 7535-7542
    • Strambini, G.B.1    Cioni, P.2    Peracchi, A.3    Mozzarelli, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.