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Volumn 24, Issue 2, 2009, Pages 350-355

New tryptophanase inhibitors: Towards prevention of bacterial biofilm formation

Author keywords

Indole; Inhibition; L tryptophan; Quasi substrates

Indexed keywords

ALPHA AMINO 2 (9,10 ANTHRAQUINONE)PROPANOIC ACID; ALPHA AMINO 9,10 DIHYDRO 9,10 DIOXO 2 ANTHRACENEPROPANOIC ACID; BACTERIAL ENZYME; BACTERIAL RNA; ENZYME INHIBITOR; INDOLE; N ACETYLTRYPTOPHAN; PHENYLBENZOQUINONE TRYPTOPHAN; TRYPTOPHAN ETHYL ESTER; TRYPTOPHANASE; TRYPTOPHANASE INHIBITOR; UNCLASSIFIED DRUG; 9,10-ANTHRAQUINONE; ANTHRAQUINONE; ANTHRAQUINONE DERIVATIVE; BACTERIAL DNA; INDOLE DERIVATIVE; TRYPTOPHAN;

EID: 68049086742     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756360802187612     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 0029893583 scopus 로고    scopus 로고
    • Interactions of Escherichia coli tryptophanase with quasisubstrates and monovalent cations studied by the circular dichroism and fluorescence methods
    • Ben-Kasus T, Markel A, Gdalevsky G, Torchinsky YM, Phillips RS, Parola AH. Interactions of Escherichia coli tryptophanase with quasisubstrates and monovalent cations studied by the circular dichroism and fluorescence methods. Biochim Biophys Acta 1996;1294:147-152.
    • (1996) Biochim Biophys Acta , vol.1294 , pp. 147-152
    • Ben-Kasus, T.1    Markel, A.2    Gdalevsky, G.3    Torchinsky, Y.M.4    Phillips, R.S.5    Parola, A.H.6
  • 2
    • 73649171549 scopus 로고
    • Comparison between some pyridoxal-dependent enzymatic and non-enzymatic reactions
    • Snell EE. Comparison between some pyridoxal-dependent enzymatic and non-enzymatic reactions. Brookhaven Symp Biol 1962;15:32-51.
    • (1962) Brookhaven Symp Biol , vol.15 , pp. 32-51
    • Snell, E.E.1
  • 3
    • 0025834941 scopus 로고
    • Equilibria and absorption spectra of tryptophanase
    • Metzler CM, Viswanath R, Metzler DEJ. Equilibria and absorption spectra of tryptophanase. Biol Chem 1991;266: 9374-9381.
    • (1991) Biol Chem , vol.266 , pp. 9374-9381
    • Metzler, C.M.1    Viswanath, R.2    Metzler, D.E.J.3
  • 4
    • 0016693908 scopus 로고
    • Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 50-phosphate and monovalent cations
    • Hogberg-Raibaud A, Raibaud O, Goldberg ME. Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 50-phosphate and monovalent cations. J Biol Chem 1975;250:3352-3358.
    • (1975) J Biol Chem , vol.250 , pp. 3352-3358
    • Hogberg-Raibaud, A.1    Raibaud, O.2    Goldberg, M.E.3
  • 5
    • 0017342650 scopus 로고
    • Monovalent cation activation of tryptophanase
    • Suelter CH, Snell EE. Monovalent cation activation of tryptophanase. J Biol Chem 1977;252:1852-1857.
    • (1977) J Biol Chem , vol.252 , pp. 1852-1857
    • Suelter, C.H.1    Snell, E.E.2
  • 6
    • 0017146185 scopus 로고
    • Pyridoxal-50-phosphatesensitized photoinactivation of tryptophanase and evidence for essential histidyl residues in the active sites
    • Toraya T, Nihira T, Fukui S. Pyridoxal-50-phosphatesensitized photoinactivation of tryptophanase and evidence for essential histidyl residues in the active sites. Eur J Biochem 1976;69:411-419.
    • (1976) Eur J Biochem , vol.69 , pp. 411-419
    • Toraya, T.1    Nihira, T.2    Fukui, S.3
  • 7
    • 46749089070 scopus 로고    scopus 로고
    • A structural insight into cold inactivation of tryptophanase and cold adaptation of S41: Minireview
    • Almog O, Kogan A, de Leeuw M, Cohen-Luria R, Parola AH. A structural insight into cold inactivation of tryptophanase and cold adaptation of S41: Minireview. Biopolymers 2008;89: 354-359.
    • (2008) Biopolymers , vol.89 , pp. 354-359
    • Almog, O.1    Kogan, A.2    De Leeuw, M.3    Cohen-Luria, R.4    Parola, A.H.5
  • 8
    • 0001596087 scopus 로고
    • An inducible tryptophan synthase in tryptophan auxotrophs of Escherichia coli
    • Newton WA, Snell EE. An inducible tryptophan synthase in tryptophan auxotrophs of Escherichia coli. Proc Natl Acad Sci USA 1962;48:1431-1439.
    • (1962) Proc Natl Acad Sci USA , vol.48 , pp. 1431-1439
    • Newton, W.A.1    Snell, E.E.2
  • 10
    • 0034966692 scopus 로고    scopus 로고
    • Indole can act as an extracellular signal in Escherichia coli
    • Wang D, Ding X, Rather PN. Indole can act as an extracellular signal in Escherichia coli. J Bacteriol 2001;183:4210-4216.
    • (2001) J Bacteriol , vol.183 , pp. 4210-4216
    • Wang, D.1    Ding, X.2    Rather, P.N.3
  • 11
    • 0242552360 scopus 로고    scopus 로고
    • Indole can act as an extracellular signal to regulate biofilm formation in Escherichia coli and in other indole-producing bacteria
    • DiMartino P, Fursy R, Bret L, Sundararaju B, Phillips RS. Indole can act as an extracellular signal to regulate biofilm formation in Escherichia coli and in other indole-producing bacteria. Can J Microbiol 2003;49(7):443-449.
    • (2003) Can J Microbiol , vol.49 , Issue.7 , pp. 443-449
    • Dimartino, P.1    Fursy, R.2    Bret, L.3    Sundararaju, B.4    Phillips, R.S.5
  • 12
  • 13
    • 34247850885 scopus 로고    scopus 로고
    • YcfR (BhsA) influences Escherichia coli biofilm formation through stress response and surface hydrophobicity
    • Zhang X, García-Contreras R, Wood TK. YcfR (BhsA) influences Escherichia coli biofilm formation through stress response and surface hydrophobicity. J Bacteriol 2007;189(8): 3051-3062.
    • (2007) J Bacteriol , vol.189 , Issue.8 , pp. 3051-3062
    • Zhang, X.1    García-Contreras, R.2    Wood, T.K.3
  • 14
    • 33646092295 scopus 로고    scopus 로고
    • YliH (BssR) and YceP (BssS) regulate Escherichia coli K-12 biofilm formation by influencing cell signaling
    • Domka J, Lee J, Wood TK. YliH (BssR) and YceP (BssS) regulate Escherichia coli K-12 biofilm formation by influencing cell signaling. Appl Environ Microbiol 2006;72(4): 2449-2459.
    • (2006) Appl Environ Microbiol , vol.72 , Issue.4 , pp. 2449-2459
    • Domka, J.1    Lee, J.2    Wood, T.K.3
  • 15
    • 34347237865 scopus 로고    scopus 로고
    • Indole is an inter-species biofilm signal mediated by SdiA
    • doi doi:10.1186/1471-2180-7-42
    • Lee J, Jayaraman A, Wood TK. Indole is an inter-species biofilm signal mediated by SdiA. BMC Microbiol 2007;7:42, (doi:10.1186/1471-2180-7-42).
    • (2007) BMC Microbiol , vol.7 , pp. 42
    • Lee, J.1    Jayaraman, A.2    Wood, T.K.3
  • 16
    • 34447519333 scopus 로고    scopus 로고
    • Enterohemorrhagic Escherichia coli biofilms are inhibited by 7- hydroxyindole and stimulated by isatin
    • Lee J, Bansal T, Jayaraman A, Bentley WE, Wood TK. Enterohemorrhagic Escherichia coli biofilms are inhibited by 7- hydroxyindole and stimulated by isatin. Appl Environ Microbiol 2007;73:4100-4109.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4100-4109
    • Lee, J.1    Bansal, T.2    Jayaraman, A.3    Bentley, W.E.4    Wood, T.K.5
  • 17
    • 33846104333 scopus 로고    scopus 로고
    • Temporal geneexpression in Escherichia coli K-12 biofilms
    • Domka J, Lee J, Bansal T, Wood TK. Temporal geneexpression in Escherichia coli K-12 biofilms. Environ Microbiol 2007;9(2):332-346.
    • (2007) Environ Microbiol , vol.9 , Issue.2 , pp. 332-346
    • Domka, J.1    Lee, J.2    Bansal, T.3    Wood, T.K.4
  • 18
    • 0024608635 scopus 로고
    • Synthesis of Ltyrosine from phenol and S-(o-nitrophenyl)-L-cysteine catalysed by tyrosine phenol-lyase
    • Phillips RS, Ravichandran K, Von Tersch RL. Synthesis of Ltyrosine from phenol and S-(o-nitrophenyl)-L-cysteine catalysed by tyrosine phenol-lyase. Enzyme Microb Technol 1989; 11:80-83.
    • (1989) Enzyme Microb Technol , vol.11 , pp. 80-83
    • Phillips, R.S.1    Ravichandran, K.2    Von Tersch, R.L.3
  • 19
    • 33845708038 scopus 로고    scopus 로고
    • Indole signalling contributes to the stable maintenance of Escherichia coli multicopy plasmids
    • Chant EL, Summers DK. Indole signalling contributes to the stable maintenance of Escherichia coli multicopy plasmids. Molec Microbiol 2007;63(1):35-43.
    • (2007) Molec Microbiol , vol.63 , Issue.1 , pp. 35-43
    • Chant, E.L.1    Summers, D.K.2
  • 20
    • 0021672622 scopus 로고
    • 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
    • Phillips RS, Miles EW, Cohen LA. 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 1984;23:6228-6234.
    • (1984) Biochemistry , vol.23 , pp. 6228-6234
    • Phillips, R.S.1    Miles, E.W.2    Cohen, L.A.3
  • 21
    • 77956916116 scopus 로고
    • Schiff base intermediates in enzyme catalysis
    • Boyer PD editor
    • Snell EE, Mari SJ. Schiff base intermediates in enzyme catalysis. In: Boyer PD, editor. The Enzymes., vol.2 1970. p 335-370.
    • (1970) The Enzymes , vol.2 , pp. 335-370
    • Snell, E.E.1    Mari, S.J.2
  • 22
    • 21644477579 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the apo formof Escherichia coli tryptophanase
    • Kogan A,Gdalevsky GY,Cohen-Luria R,Parola AH,Goldgur Y. Crystallization and preliminary X-ray analysis of the apo formof Escherichia coli tryptophanase. Acta Cryst sec B 2004;60: 273-275.
    • (2004) Acta Cryst Sec B , vol.60 , pp. 273-275
    • Kogan, A.1    Gdalevsky, G.Y.2    Cohen-Luria, R.3    Parola, A.H.4    Goldgur, Y.5
  • 23
    • 0031554222 scopus 로고    scopus 로고
    • Synthesis and conformation of poly(L-2-anthraquinonylalanine)
    • Matsubara T, Shinohara H, Sisido M. Synthesis and conformation of poly(L-2-anthraquinonylalanine). Macromolecules 1997;30:2651-2656.
    • (1997) Macromolecules , vol.30 , pp. 2651-2656
    • Matsubara, T.1    Shinohara, H.2    Sisido, M.3
  • 24
    • 71049154761 scopus 로고
    • Action of thiophenols on quinines
    • Dimroth O, Kraft L, Aichinger K. Action of thiophenols on quinines. Ann Chem 1940;54:5124-5139.
    • (1940) Ann Chem , vol.54 , pp. 5124-5139
    • Dimroth, O.1    Kraft, L.2    Aichinger, K.3
  • 25
    • 0017099896 scopus 로고
    • Application of a direct spectrophotometric assay employing a chromogenic substrate for tryptophanase to the determination of pyridoxal and pyridoxamine 50-phosphate
    • Suelter CH, Wang J, Snell EE. Application of a direct spectrophotometric assay employing a chromogenic substrate for tryptophanase to the determination of pyridoxal and pyridoxamine 50-phosphate. Anal Biochem 1976;76:221-232.
    • (1976) Anal Biochem , vol.76 , pp. 221-232
    • Suelter, C.H.1    Wang, J.2    Snell, E.E.3
  • 27
    • 33745673372 scopus 로고    scopus 로고
    • Structure of Escherichia coli tryptophanase
    • Ku SY, Yip P, Howell LP. Structure of Escherichia coli tryptophanase. Acta Cryst D 2006;62(7):814-823.
    • (2006) Acta Cryst D , vol.62 , Issue.7 , pp. 814-823
    • Ku, S.Y.1    Yip, P.2    Howell, L.P.3
  • 29
    • 33745125692 scopus 로고    scopus 로고
    • Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K p ions
    • Milic D, Matkovic-Calogovic D, Demidkina TV, Kulikova VV, Sunitzina NI, Antson AA. Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K p ions. Biochemistry 2006;45(24):7544-17522
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7544-17522
    • Milic, D.1    Matkovic-Calogovic, D.2    Demidkina, T.V.3    Kulikova, V.V.4    Sunitzina, N.I.5    Antson, A.A.6
  • 31
    • 24044545862 scopus 로고    scopus 로고
    • Floxuridine amino acid ester prodrugs: Enhancing Caco-2 permeability and resistance to glycosidic bond metabolism
    • Landowski CP, Song X, Lorenzi PL, Hifinger JM, Amidon G. Floxuridine amino acid ester prodrugs: Enhancing Caco-2 permeability and resistance to glycosidic bond metabolism. Pharm Res 2005;22(9):1510-1518.
    • (2005) Pharm Res , vol.22 , Issue.9 , pp. 1510-1518
    • Landowski, C.P.1    Song, X.2    Lorenzi, P.L.3    Hifinger, J.M.4    Amidon, G.5
  • 32
    • 71049195026 scopus 로고
    • Quinones as anticancer agents: Potential bioreductive alkylating agents
    • Lin AJ, Coby LA, Sartorelli AC. Quinones as anticancer agents: Potential bioreductive alkylating agents. J Toxicol Environ Health 1985;16(5):665-672.
    • (1985) J Toxicol Environ Health , vol.16 , Issue.5 , pp. 665-672
    • Lin, A.J.1    Coby, L.A.2    Sartorelli, A.C.3
  • 33
    • 0023203399 scopus 로고
    • Polycyclic aromatic hydrocarbon quinones and glutathione thioethers as substrates and inhibitors of the human placental NADP-linked 15-hydroxyprostaglandin dehydrogenase
    • Chung H, Harvey RG, Armstrong RN, Jarabak J. Polycyclic aromatic hydrocarbon quinones and glutathione thioethers as substrates and inhibitors of the human placental NADP-linked 15-hydroxyprostaglandin dehydrogenase. J Biol Chem 1987; 262(26):12448-12451.
    • (1987) J Biol Chem , vol.262 , Issue.26 , pp. 12448-12451
    • Chung, H.1    Harvey, R.G.2    Armstrong, R.N.3    Jarabak, J.4
  • 35
    • 0035795179 scopus 로고    scopus 로고
    • Heterocyclic orthoquinones, a novel type of photosystem II inhibitors
    • Oettmeier W, Masson K, Hecht H. Heterocyclic orthoquinones, a novel type of photosystem II inhibitors. Biochim Biophys Acta 2001;1504(2-3):346-351.
    • (2001) Biochim Biophys Acta , vol.1504 , Issue.2-3 , pp. 346-351
    • Oettmeier, W.1    Masson, K.2    Hecht, H.3


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