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Volumn 54, Issue 14, 2015, Pages 2372-2384

Conversion of aminodeoxychorismate synthase into anthranilate synthase with janus mutations: Mechanism of pyruvate elimination catalyzed by chorismate enzymes

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINO ACIDS; BIOINFORMATICS; CATALYSIS; ESCHERICHIA COLI; FUNCTIONAL GROUPS; ISOTOPES; MOLECULAR DYNAMICS;

EID: 84927732564     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00013     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0001293075 scopus 로고
    • Molecular Studies on Enzymes in Chorismate Metabolism and the Enterobactin Biosynthetic-Pathway
    • Walsh, C. T., Liu, J., Rusnak, F., and Sakaitani, M. (1990) Molecular Studies on Enzymes in Chorismate Metabolism and the Enterobactin Biosynthetic-Pathway Chem. Rev. 90, 1105-1129
    • (1990) Chem. Rev. , vol.90 , pp. 1105-1129
    • Walsh, C.T.1    Liu, J.2    Rusnak, F.3    Sakaitani, M.4
  • 3
    • 0034951945 scopus 로고    scopus 로고
    • A metabloic node in action: Chorismate-utilizing enzymes in microorganisms
    • Dosselaere, F. and Vanderleyden, J. (2001) A metabloic node in action: Chorismate-utilizing enzymes in microorganisms Crit. Rev. Microbiol. 27, 75-131
    • (2001) Crit. Rev. Microbiol. , vol.27 , pp. 75-131
    • Dosselaere, F.1    Vanderleyden, J.2
  • 4
    • 0023853960 scopus 로고
    • Characterization of aromatic- and purine-dependent Salmonella typhmurium: Attention, persistence, and ability to induce protective immunity in BALB/c mice
    • O'Callaghan, D., Maskell, D., Liew, F. Y., Easmon, C. S., and Dougan, G. (1988) Characterization of aromatic- and purine-dependent Salmonella typhmurium: Attention, persistence, and ability to induce protective immunity in BALB/c mice Infect. Immun. 56, 419-423
    • (1988) Infect. Immun. , vol.56 , pp. 419-423
    • O'Callaghan, D.1    Maskell, D.2    Liew, F.Y.3    Easmon, C.S.4    Dougan, G.5
  • 5
    • 0035123059 scopus 로고    scopus 로고
    • Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium
    • Morollo, A. A. and Eck, K. J. (2001) Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium Nat. Struct. Biol. 8, 243-247
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 243-247
    • Morollo, A.A.1    Eck, K.J.2
  • 6
    • 0037133196 scopus 로고    scopus 로고
    • Structure of Escherichia coli aminodeoxychorismate synthase: Architectural conservation and diversity in chorismate-utilizing enzymes
    • Parsons, J. F., Jensen, P. Y., Pachikara, A. S., Howard, A. J., Eisenstein, E., and Ladner, J. E. (2002) Structure of Escherichia coli aminodeoxychorismate synthase: Architectural conservation and diversity in chorismate-utilizing enzymes Biochemistry 41, 2198-2208
    • (2002) Biochemistry , vol.41 , pp. 2198-2208
    • Parsons, J.F.1    Jensen, P.Y.2    Pachikara, A.S.3    Howard, A.J.4    Eisenstein, E.5    Ladner, J.E.6
  • 7
    • 80052211993 scopus 로고    scopus 로고
    • Pericyclic reactions catalyzed by chorismate-utilizing enzymes
    • Lamb, A. L. (2011) Pericyclic reactions catalyzed by chorismate-utilizing enzymes Biochemistry 50, 7476-7483
    • (2011) Biochemistry , vol.50 , pp. 7476-7483
    • Lamb, A.L.1
  • 8
    • 33846646987 scopus 로고    scopus 로고
    • Structure and Mechanism of MbtI, the Salicylate Synthase from Mycobacterium tuberculosis
    • Zwahlen, J., Kolappan, S., Zhou, R., Kisker, C., and Tonge, P. J. (2007) Structure and Mechanism of MbtI, the Salicylate Synthase from Mycobacterium tuberculosis Biochemistry 46, 954-964
    • (2007) Biochemistry , vol.46 , pp. 954-964
    • Zwahlen, J.1    Kolappan, S.2    Zhou, R.3    Kisker, C.4    Tonge, P.J.5
  • 9
    • 77249104442 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli enterobactin-specific isochorismate synthase (EntC) bound to its reaction product isochorismate: Implications for the enzyme mechanism and differential activity of chorismate-utilizing enzymes
    • Sridharan, S., Howard, N., Kerbarh, O., Blaszczyk, M., Abell, C., and Blundell, T. L. (2010) Crystal structure of Escherichia coli enterobactin-specific isochorismate synthase (EntC) bound to its reaction product isochorismate: Implications for the enzyme mechanism and differential activity of chorismate-utilizing enzymes J. Mol. Biol. 397, 290-300
    • (2010) J. Mol. Biol. , vol.397 , pp. 290-300
    • Sridharan, S.1    Howard, N.2    Kerbarh, O.3    Blaszczyk, M.4    Abell, C.5    Blundell, T.L.6
  • 10
    • 0025647889 scopus 로고
    • Para-Aminobenzoate Synthesis in Escherichia coli: Purification and Characterization of PABB as Aminodeoxychorismate Synthase and Enzyme-X as Aminodeoxychorismate Lyase
    • Ye, Q. Z., Liu, J., and Walsh, C. T. (1990) para-Aminobenzoate Synthesis in Escherichia coli: Purification and Characterization of PABB as Aminodeoxychorismate Synthase and Enzyme-X as Aminodeoxychorismate Lyase Proc. Natl. Acad. Sci. U.S.A. 87, 9391-9395
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9391-9395
    • Ye, Q.Z.1    Liu, J.2    Walsh, C.T.3
  • 11
    • 33645933904 scopus 로고    scopus 로고
    • Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction
    • He, Z. and Toney, M. D. (2006) Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction Biochemistry 45, 5019-5028
    • (2006) Biochemistry , vol.45 , pp. 5019-5028
    • He, Z.1    Toney, M.D.2
  • 12
    • 0035933197 scopus 로고    scopus 로고
    • The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, l -tryptophan
    • Spraggon, G., Kim, C., Nguyen-Huu, X., Yee, M. C., Yanofsky, C., and Mills, S. E. (2001) The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, l -tryptophan Proc. Natl. Acad. Sci. U.S.A. 98, 6021-6026
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6021-6026
    • Spraggon, G.1    Kim, C.2    Nguyen-Huu, X.3    Yee, M.C.4    Yanofsky, C.5    Mills, S.E.6
  • 13
    • 1542306930 scopus 로고    scopus 로고
    • Conservation of mechanism in three chorismate-utilizing enzymes
    • He, Z., Stigers Lavoie, K. D., Bartlett, P. A., and Toney, M. D. (2004) Conservation of mechanism in three chorismate-utilizing enzymes J. Am. Chem. Soc. 126, 2378-2385
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2378-2385
    • He, Z.1    Stigers Lavoie, K.D.2    Bartlett, P.A.3    Toney, M.D.4
  • 14
    • 79955980721 scopus 로고    scopus 로고
    • Ligand binding induces an ammonia channel in 2-amino-2-desoxyiochorismate (ADIC) synthase PhzE
    • Li, Q., Mavrodi, D. V., Thomashow, L. S., Roessle, M., and Blankenfeldt, W. (2011) Ligand binding induces an ammonia channel in 2-amino-2-desoxyiochorismate (ADIC) synthase PhzE J. Biol. Chem. 286, 18213-18221
    • (2011) J. Biol. Chem. , vol.286 , pp. 18213-18221
    • Li, Q.1    Mavrodi, D.V.2    Thomashow, L.S.3    Roessle, M.4    Blankenfeldt, W.5
  • 15
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang, X. Y., Holden, H. M., and Raushel, F. M. (2001) Channeling of substrates and intermediates in enzyme-catalyzed reactions Annu. Rev. Biochem. 70, 149-180
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.Y.1    Holden, H.M.2    Raushel, F.M.3
  • 17
    • 0036959599 scopus 로고    scopus 로고
    • Invasiveness of Pseudomonas aeruginosa and its role in diversity of Pseudomonal Infectious Diseases
    • Hiraka, Y. (2002) Invasiveness of Pseudomonas aeruginosa and its role in diversity of Pseudomonal Infectious Diseases Acta Med. Nagasaki. 47, 89-96
    • (2002) Acta Med. Nagasaki. , vol.47 , pp. 89-96
    • Hiraka, Y.1
  • 18
    • 33344476803 scopus 로고    scopus 로고
    • Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate
    • Kerbarh, O., Chirgadze, D. Y., Blundell, T. L., and Abell, C. (2006) Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate J. Mol. Biol. 357, 524-534
    • (2006) J. Mol. Biol. , vol.357 , pp. 524-534
    • Kerbarh, O.1    Chirgadze, D.Y.2    Blundell, T.L.3    Abell, C.4
  • 19
    • 84870679006 scopus 로고    scopus 로고
    • Expression and characterization of PhzE from P. Aeruginosa PAO1: Aminodeoxyisochorismate synthase involved in pyocyanin and phenazine-1-carboxylate production
    • Culbertson, J. E. and Toney, M. D. (2013) Expression and characterization of PhzE from P. aeruginosa PAO1: Aminodeoxyisochorismate synthase involved in pyocyanin and phenazine-1-carboxylate production Biochim. Biophys. Acta 1834, 240-246
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 240-246
    • Culbertson, J.E.1    Toney, M.D.2
  • 20
    • 0014939659 scopus 로고
    • Mechanism of the antranilate synthetase reaction. Evidence against an intramolecular hydrogen transfer
    • Floss, H. G., Onderka, D. K., and Zalkin, H. (1970) Mechanism of the antranilate synthetase reaction. Evidence against an intramolecular hydrogen transfer Biochim. Biophys. Acta 206, 449-456
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 449-456
    • Floss, H.G.1    Onderka, D.K.2    Zalkin, H.3
  • 21
    • 0014805964 scopus 로고
    • Studies of the mechanism of anthranilate synthase reaction
    • Tamir, H. and Srinivasan, P. R. (1970) Studies of the mechanism of anthranilate synthase reaction Proc. Natl. Acad. Sci. U.S.A. 66, 547-551
    • (1970) Proc. Natl. Acad. Sci. U.S.A. , vol.66 , pp. 547-551
    • Tamir, H.1    Srinivasan, P.R.2
  • 22
    • 77950391649 scopus 로고    scopus 로고
    • Nucleophile Specificity in Anthranilate Synthase, Aminodeoxychorismate Synthase, Isochorismate Synthase, and Salicylate Synthase
    • Ziebart, K. T. and Toney, M. D. (2010) Nucleophile Specificity in Anthranilate Synthase, Aminodeoxychorismate Synthase, Isochorismate Synthase, and Salicylate Synthase Biochemistry 49, 2851-2859
    • (2010) Biochemistry , vol.49 , pp. 2851-2859
    • Ziebart, K.T.1    Toney, M.D.2
  • 24
    • 0000316121 scopus 로고
    • Chorismic Acid: Purification and some Chemical and Physical Studies
    • Gibson, F. (1963) Chorismic Acid: Purification and some Chemical and Physical Studies Biochem. J. 90, 256-261
    • (1963) Biochem. J. , vol.90 , pp. 256-261
    • Gibson, F.1
  • 25
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA: A self-parameterizing force field
    • Krieger, E., Koraimann, G., and Vriend, G. (2002) Increasing the precision of comparative models with YASARA NOVA: A self-parameterizing force field Proteins 47, 393-402
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 26
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • Krieger, E., Darden, T., Nabuurs, S. B., Finkelstein, A., and Vriend, G. (2004) Making optimal use of empirical energy functions: Force-field parameterization in crystal space Proteins 57, 678-683
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 27
    • 84855945977 scopus 로고    scopus 로고
    • Assignment of protonation states in proteins and ligands: Combining pKa prediction with hydrogen bonding network optimization
    • Krieger, E., Dunbrack, R. L., Jr., Hooft, R. W., and Krieger, B. (2012) Assignment of protonation states in proteins and ligands: Combining pKa prediction with hydrogen bonding network optimization Methods Mol. Biol. 819, 405-421
    • (2012) Methods Mol. Biol. , vol.819 , pp. 405-421
    • Krieger, E.1    Dunbrack, R.L.2    Hooft, R.W.3    Krieger, B.4
  • 28
    • 0014939659 scopus 로고
    • Mechanism of the anthranilate synthetase reaction. Evidence against an intramolecular hydrogen transfer
    • Floss, H. G., Onderka, D. K., and Zalkin, H. (1970) Mechanism of the anthranilate synthetase reaction. Evidence against an intramolecular hydrogen transfer Biochim. Biophys. Acta 206, 449-456
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 449-456
    • Floss, H.G.1    Onderka, D.K.2    Zalkin, H.3
  • 29
    • 0014365162 scopus 로고
    • Oxaloacetate decarboxylase from cod. Catalysis of hydrogen-deuterium exchange in pyruvate
    • Kosicki, G. W. (1968) Oxaloacetate decarboxylase from cod. Catalysis of hydrogen-deuterium exchange in pyruvate Biochemistry 7, 4310-4314
    • (1968) Biochemistry , vol.7 , pp. 4310-4314
    • Kosicki, G.W.1
  • 30
    • 84881293048 scopus 로고    scopus 로고
    • Exploration of swapping enzymatic function between two proteins: A simulation study of chorismate mutase and isochorismate pyruvate lyase
    • Choutko, A., Eichenberger, A. P., van Gunsteren, W. F., and Dolenc, J. (2013) Exploration of swapping enzymatic function between two proteins: A simulation study of chorismate mutase and isochorismate pyruvate lyase Protein Sci. 22, 809-822
    • (2013) Protein Sci. , vol.22 , pp. 809-822
    • Choutko, A.1    Eichenberger, A.P.2    Van Gunsteren, W.F.3    Dolenc, J.4
  • 31
    • 80051712349 scopus 로고    scopus 로고
    • PH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: Implications for transition state stabilization and the role of lysine 42
    • Olucha, J., Ouellette, A. N., Luo, Q., and Lamb, A. L. (2011) pH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: Implications for transition state stabilization and the role of lysine 42 Biochemistry 50, 7198-7207
    • (2011) Biochemistry , vol.50 , pp. 7198-7207
    • Olucha, J.1    Ouellette, A.N.2    Luo, Q.3    Lamb, A.L.4
  • 32
    • 79955685286 scopus 로고    scopus 로고
    • Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB
    • Luo, Q., Meneely, K. M., and Lamb, A. L. (2011) Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB J. Am. Chem. Soc. 133, 7229-7233
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7229-7233
    • Luo, Q.1    Meneely, K.M.2    Lamb, A.L.3
  • 33
    • 70450195270 scopus 로고    scopus 로고
    • Mechanism and plasticity of isochorismate pyruvate lyase: A computational study
    • Marti, S., Andres, J., Moliner, V., Silla, E., Tunon, I., and Bertran, J. (2009) Mechanism and plasticity of isochorismate pyruvate lyase: A computational study J. Am. Chem. Soc. 131, 16156-16161
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16156-16161
    • Marti, S.1    Andres, J.2    Moliner, V.3    Silla, E.4    Tunon, I.5    Bertran, J.6
  • 34
    • 67049134258 scopus 로고    scopus 로고
    • Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme
    • Luo, Q., Olucha, J., and Lamb, A. L. (2009) Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme Biochemistry 48, 5239-5245
    • (2009) Biochemistry , vol.48 , pp. 5239-5245
    • Luo, Q.1    Olucha, J.2    Lamb, A.L.3
  • 35
    • 30444444229 scopus 로고    scopus 로고
    • The allosteric mechanism of yeast chorismate mutase: A dynamic analysis
    • Kong, Y., Ma, J., Karplus, M., and Lipscomb, W. N. (2006) The allosteric mechanism of yeast chorismate mutase: A dynamic analysis J. Mol. Biol. 356, 237-247
    • (2006) J. Mol. Biol. , vol.356 , pp. 237-247
    • Kong, Y.1    Ma, J.2    Karplus, M.3    Lipscomb, W.N.4
  • 36
    • 23244446189 scopus 로고    scopus 로고
    • A definitive mechanism for chorismate mutase
    • Zhang, X. and Bruice, T. C. (2005) A definitive mechanism for chorismate mutase Biochemistry 44, 10443-10448
    • (2005) Biochemistry , vol.44 , pp. 10443-10448
    • Zhang, X.1    Bruice, T.C.2
  • 37
    • 0037022251 scopus 로고    scopus 로고
    • The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme
    • Hur, S. and Bruice, T. C. (2002) The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme Proc. Natl. Acad. Sci. U.S.A. 99, 1176-1181
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1176-1181
    • Hur, S.1    Bruice, T.C.2
  • 38
    • 0035979270 scopus 로고    scopus 로고
    • Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism
    • Guo, H., Cui, Q., Lipscomb, W. N., and Karplus, M. (2001) Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism Proc. Natl. Acad. Sci. U.S.A. 98, 9032-9037
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9032-9037
    • Guo, H.1    Cui, Q.2    Lipscomb, W.N.3    Karplus, M.4
  • 39
    • 84861557986 scopus 로고    scopus 로고
    • Understanding the different activities of highly promiscuous MbtI by computational methods
    • Ferrer, S., Marti, S., Moliner, V., Tunon, I., and Bertran, J. (2012) Understanding the different activities of highly promiscuous MbtI by computational methods Phys. Chem. Chem. Phys. 14, 3482-3489
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 3482-3489
    • Ferrer, S.1    Marti, S.2    Moliner, V.3    Tunon, I.4    Bertran, J.5
  • 40
    • 0023666970 scopus 로고
    • Chorismate aminations: Partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase
    • Walsh, C. T., Erion, M. D., Walts, A. E., Delany, J. J., III, and Berchtold, G. A. (1987) Chorismate aminations: Partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase Biochemistry 26, 4734-4745
    • (1987) Biochemistry , vol.26 , pp. 4734-4745
    • Walsh, C.T.1    Erion, M.D.2    Walts, A.E.3    Delany, J.J.4    Berchtold, G.A.5


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