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Volumn 46, Issue 19, 2007, Pages 5741-5753

Interaction of benzoate pyrimidine analogues with class 1A dihydroorotate dehydrogenase from Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; ENZYME INHIBITION; ENZYME KINETICS; HYDROGEN BONDS; MOLECULAR INTERACTIONS; OXIDATION;

EID: 34248577146     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7001554     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 0031423109 scopus 로고    scopus 로고
    • Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis
    • Björnberg, O., Rowland, P., Larsen, S., and Jensen, K. F. (1997) Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis, Biochemistry 36, 16197-16205.
    • (1997) Biochemistry , vol.36 , pp. 16197-16205
    • Björnberg, O.1    Rowland, P.2    Larsen, S.3    Jensen, K.F.4
  • 2
    • 0026668882 scopus 로고
    • Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts
    • Nagy, M., Lacroute, F., and Thomas, D. (1992) Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts, Proc. Natl. Acad. Sci. U.S.A. 89, 8966-8970.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 8966-8970
    • Nagy, M.1    Lacroute, F.2    Thomas, D.3
  • 3
    • 0029800334 scopus 로고    scopus 로고
    • The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers
    • Nielsen, F. S., Anderson, P. S., and Jensen, K. F. (1996) The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers, J. Biol. Chem. 271, 29359-29365.
    • (1996) J. Biol. Chem , vol.271 , pp. 29359-29365
    • Nielsen, F.S.1    Anderson, P.S.2    Jensen, K.F.3
  • 4
    • 0039021706 scopus 로고    scopus 로고
    • Activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis
    • Björnberg, O., Grüner, A. C., Roepstorff, P., and Jensen, K. F. (1999) Activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis, Biochemistry 38, 2899-2908.
    • (1999) Biochemistry , vol.38 , pp. 2899-2908
    • Björnberg, O.1    Grüner, A.C.2    Roepstorff, P.3    Jensen, K.F.4
  • 5
    • 2642708353 scopus 로고    scopus 로고
    • The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function
    • Rowland, P., Björnberg, O., Nielsen, F. S., Jensen, K. F., Larsen, S. (1998) The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function, Protein Sci. 7, 1269-1279.
    • (1998) Protein Sci , vol.7 , pp. 1269-1279
    • Rowland, P.1    Björnberg, O.2    Nielsen, F.S.3    Jensen, K.F.4    Larsen, S.5
  • 6
    • 0010184353 scopus 로고    scopus 로고
    • Structure of dihydroorotate dehydrogenase B: Electron transfer between two flavin groups bridged by an iron-sulphur cluster
    • Rowland, P., Nørager, S., Jensen, K. F., and Larsen, S. (2000) Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster, Structure 8, 1227-1238.
    • (2000) Structure , vol.8 , pp. 1227-1238
    • Rowland, P.1    Nørager, S.2    Jensen, K.F.3    Larsen, S.4
  • 7
    • 0034650342 scopus 로고    scopus 로고
    • Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents
    • Liu, S., Neidhardt, E. A., Grossman, T. H., Ocain, T., and Clardy, J. (2000) Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents, Structure 8, 25-33.
    • (2000) Structure , vol.8 , pp. 25-33
    • Liu, S.1    Neidhardt, E.A.2    Grossman, T.H.3    Ocain, T.4    Clardy, J.5
  • 8
    • 0041433824 scopus 로고    scopus 로고
    • Nørager, S., Jensen, K. F., Björnberg, O., and Larsen, S. (2002) E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases, Structure 10, 1211-1223.
    • Nørager, S., Jensen, K. F., Björnberg, O., and Larsen, S. (2002) E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases, Structure 10, 1211-1223.
  • 9
    • 1842559337 scopus 로고    scopus 로고
    • Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain
    • Hansen, M., Le Nours, J., Johansson, E., Antal, T., Ullrich, A., Loffler, M., and Larsen, S. (2004) Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain, Protein Sci. 13, 1031-1042.
    • (2004) Protein Sci , vol.13 , pp. 1031-1042
    • Hansen, M.1    Le Nours, J.2    Johansson, E.3    Antal, T.4    Ullrich, A.5    Loffler, M.6    Larsen, S.7
  • 10
    • 0035836526 scopus 로고    scopus 로고
    • Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase obtained by rapid reaction studies
    • Palfey, B. A., Björnberg, O., and Jensen, K. F. (2001) Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase obtained by rapid reaction studies, Biochemistry 40, 4381-4390.
    • (2001) Biochemistry , vol.40 , pp. 4381-4390
    • Palfey, B.A.1    Björnberg, O.2    Jensen, K.F.3
  • 11
    • 0035974643 scopus 로고    scopus 로고
    • Specific inhibition of a family 1A dihydroorotate dehydrogenase by benzoate pyrimidine analogues
    • Palfey, B. A., Björnberg, O., and Jensen, K. F. (2001) Specific inhibition of a family 1A dihydroorotate dehydrogenase by benzoate pyrimidine analogues, J. Med. Chem. 44, 2861-2864.
    • (2001) J. Med. Chem , vol.44 , pp. 2861-2864
    • Palfey, B.A.1    Björnberg, O.2    Jensen, K.F.3
  • 12
    • 0029970387 scopus 로고    scopus 로고
    • Purification and characterization of dihydroorotate dehydrogenase A from Lactococcus lactis, crystallization and preliminary X-ray diffraction studies of the enzyme
    • Nielsen, F. S., Rowland, P., Larsen, S., and Jensen, K. F. (1996) Purification and characterization of dihydroorotate dehydrogenase A from Lactococcus lactis, crystallization and preliminary X-ray diffraction studies of the enzyme, Protein Sci. 5, 852-856.
    • (1996) Protein Sci , vol.5 , pp. 852-856
    • Nielsen, F.S.1    Rowland, P.2    Larsen, S.3    Jensen, K.F.4
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0043209013 scopus 로고    scopus 로고
    • Nørager, S., Arent, S., Björnberg, O., Ottosen, Leggio, L. L., Jensen, K. J., and Larsen, S. (2003) Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function, J. Biol. Chem. 278, 28812-28822.
    • Nørager, S., Arent, S., Björnberg, O., Ottosen, Leggio, L. L., Jensen, K. J., and Larsen, S. (2003) Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function, J. Biol. Chem. 278, 28812-28822.
  • 15
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N, Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr., Sect. D 53, 240-255.
    • (1997) Acta Crystallogr., Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 16
    • 34248519789 scopus 로고    scopus 로고
    • Lamzin, V.S., Perrakis, A., and Wilson, K. S. (2001) in International Tables for Crystallography: Crystallography of Biological Macromolecules (Rossmann, M. G., and Arnold, E., Eds.) F, pp 720-722, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Lamzin, V.S., Perrakis, A., and Wilson, K. S. (2001) in International Tables for Crystallography: Crystallography of Biological Macromolecules (Rossmann, M. G., and Arnold, E., Eds.) Vol. F, pp 720-722, Kluwer Academic Publishers, Dordrecht, The Netherlands.
  • 17
  • 18
    • 0003638901 scopus 로고    scopus 로고
    • Dean, J. A, Ed, 15th ed, McGraw-Hill, Inc, New York
    • Dean, J. A., Ed. (1999) Lange's Handbook of Chemistry, 15th ed., McGraw-Hill, Inc., New York.
    • (1999) Lange's Handbook of Chemistry
  • 19
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in proteinbinding reactions using isothermal titration calorimetry
    • Baker, B. M., and Murphy, K. P. (1996) Evaluation of linked protonation effects in proteinbinding reactions using isothermal titration calorimetry, Biophys. J. 71, 2049-2055.
    • (1996) Biophys. J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 21
    • 0016749447 scopus 로고
    • Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data
    • Strickland, S., Palmer, G., and Massey, V. (1975) Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data, J. Biol. Chem. 250, 4048-4052.
    • (1975) J. Biol. Chem , vol.250 , pp. 4048-4052
    • Strickland, S.1    Palmer, G.2    Massey, V.3
  • 22
    • 0024290407 scopus 로고
    • Determination of the rate-limiting segment of aminoglycoside nucleotidyltransferase 2″-I by pH- and viscosity-dependent kinetics
    • Gates, C. A., and Northrop, D. B. (1988) Determination of the rate-limiting segment of aminoglycoside nucleotidyltransferase 2″-I by pH- and viscosity-dependent kinetics, Biochemistry 27, 3834-3842.
    • (1988) Biochemistry , vol.27 , pp. 3834-3842
    • Gates, C.A.1    Northrop, D.B.2
  • 23
    • 0022546047 scopus 로고
    • Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis
    • Howell, E. E., Villafranca, J. E., Warren, M. S., Oatley, J. S., and Kraut, J. (1986) Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis, Science 231, 1123-1128.
    • (1986) Science , vol.231 , pp. 1123-1128
    • Howell, E.E.1    Villafranca, J.E.2    Warren, M.S.3    Oatley, J.S.4    Kraut, J.5
  • 24
    • 0023204278 scopus 로고
    • The catalytic role of the active site aspartic acid in serine proteases
    • Craik, C. S., Roczniak, S., Largman, C., and Rutter, W. J. (1987) The catalytic role of the active site aspartic acid in serine proteases, Science 237, 909-913.
    • (1987) Science , vol.237 , pp. 909-913
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., and Thornton J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF: A molecular modeling and drug design program, J. Mol. Graphics 8, 52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 28
    • 0031568812 scopus 로고    scopus 로고
    • The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis
    • Rowland, P., Nielsen, F. S., Jensen, K. F., and Larsen, S. (1997) The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis, Structure 5, 239-252.
    • (1997) Structure , vol.5 , pp. 239-252
    • Rowland, P.1    Nielsen, F.S.2    Jensen, K.F.3    Larsen, S.4
  • 29
    • 0034898757 scopus 로고    scopus 로고
    • Comparison of resonance Raman spectra of flavin-3,4-dihydroxybenzoate charge-transfer complexes in three flavoenzymes
    • Zheng, Y., Massey, V., Schaller, A., Palfey, B. A., and Carey, P. R. (2001) Comparison of resonance Raman spectra of flavin-3,4-dihydroxybenzoate charge-transfer complexes in three flavoenzymes, J. Raman Spedrosc. 32, 579-586.
    • (2001) J. Raman Spedrosc , vol.32 , pp. 579-586
    • Zheng, Y.1    Massey, V.2    Schaller, A.3    Palfey, B.A.4    Carey, P.R.5
  • 30
    • 0036839243 scopus 로고    scopus 로고
    • The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers
    • Ottosen, M. B., Björnberg, O., Nørager, S., Larsen, S., Palfey, B. A., and Jensen, K. F. (2002) The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers, Protein Sci. 11, 2575-2583.
    • (2002) Protein Sci , vol.11 , pp. 2575-2583
    • Ottosen, M.B.1    Björnberg, O.2    Nørager, S.3    Larsen, S.4    Palfey, B.A.5    Jensen, K.F.6
  • 31
    • 0034193174 scopus 로고    scopus 로고
    • A second dihydroorotate dehydrogenase (type A) of the human pathogen Enterococcus faecalis: Expression, purification, and steady-state kinetic mechanism
    • Marcinkeviciene, J., Jiang, W., Locke, G., Kophcho, L. M., Rogers, M. J., and Copeland, R. A. (2000) A second dihydroorotate dehydrogenase (type A) of the human pathogen Enterococcus faecalis: expression, purification, and steady-state kinetic mechanism, Arch. Biochem. Biophys. 377, 178-186.
    • (2000) Arch. Biochem. Biophys , vol.377 , pp. 178-186
    • Marcinkeviciene, J.1    Jiang, W.2    Locke, G.3    Kophcho, L.M.4    Rogers, M.J.5    Copeland, R.A.6
  • 34
    • 14644431768 scopus 로고    scopus 로고
    • The origin of dihydroorotate dehydrogenase genes of kinetoplastids, with special reference to their biological significance and adaptation to anaerobic, parasitic conditions
    • Annoura, T., Nara, T., Makiuchi, T., Hashimoto, T., and Aoki, T. (2005) The origin of dihydroorotate dehydrogenase genes of kinetoplastids, with special reference to their biological significance and adaptation to anaerobic, parasitic conditions, J. Mol. Evol. 60, 113-127.
    • (2005) J. Mol. Evol , vol.60 , pp. 113-127
    • Annoura, T.1    Nara, T.2    Makiuchi, T.3    Hashimoto, T.4    Aoki, T.5
  • 35
    • 33744489087 scopus 로고    scopus 로고
    • Expression, purification and crystallization of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with orotate
    • Inaoka, D. K., Takashima, E., Osanai, A., Shimizu, H., Nara, T., Aoki, T., Harada, S., and Kita, K. (2005) Expression, purification and crystallization of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with orotate, Acta Crystallogr., Sect. F 61, 875-878.
    • (2005) Acta Crystallogr., Sect. F , vol.61 , pp. 875-878
    • Inaoka, D.K.1    Takashima, E.2    Osanai, A.3    Shimizu, H.4    Nara, T.5    Aoki, T.6    Harada, S.7    Kita, K.8
  • 36
    • 33749525304 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase
    • Cordeiro, A. T., Feliciano, P. R., and Nonato, M. C. (2006) Crystallization and preliminary X-ray diffraction analysis of Leishmania major dihydroorotate dehydrogenase, Acta Crystallogr., Sect. F 62, 1049-1051.
    • (2006) Acta Crystallogr., Sect. F , vol.62 , pp. 1049-1051
    • Cordeiro, A.T.1    Feliciano, P.R.2    Nonato, M.C.3
  • 37
    • 13844276417 scopus 로고    scopus 로고
    • Inhibitory action of marine algae extracts on the Trypanosoma cruzi dihydroorotate dehydrogenase activity and on the protozoan growth in mammalian cells
    • Nara, T., Kamei, Y., Tsubouchi, A., Annoura, T., Hirota, K., Iizumi, K., Dohmoto, Y., Ono, T., and Aoki, T. (2005) Inhibitory action of marine algae extracts on the Trypanosoma cruzi dihydroorotate dehydrogenase activity and on the protozoan growth in mammalian cells, Parasitol. Int. 54, 59-64.
    • (2005) Parasitol. Int , vol.54 , pp. 59-64
    • Nara, T.1    Kamei, Y.2    Tsubouchi, A.3    Annoura, T.4    Hirota, K.5    Iizumi, K.6    Dohmoto, Y.7    Ono, T.8    Aoki, T.9
  • 39
    • 0642315208 scopus 로고    scopus 로고
    • Johnson, K. A. (1992) Transient-State Kinetic Analysis of Enzyme Reaction Pathways, in The Enzymes (Sigman, D. S., Ed.) 3rd ed., XX, pp. 1-61, Academic Press, New York.
    • Johnson, K. A. (1992) Transient-State Kinetic Analysis of Enzyme Reaction Pathways, in The Enzymes (Sigman, D. S., Ed.) 3rd ed., Vol. XX, pp. 1-61, Academic Press, New York.
  • 40
    • 0014429144 scopus 로고
    • A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state
    • Cha, S. (1968) A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state, J. Biol Chem. 243, 820-825.
    • (1968) J. Biol Chem , vol.243 , pp. 820-825
    • Cha, S.1
  • 41
    • 0000209495 scopus 로고
    • The competitive inhibition of uricase by oxonate and by related derivatives of s-triazines
    • Fridovich, I. (1965) The competitive inhibition of uricase by oxonate and by related derivatives of s-triazines, J. Biol. Chem. 240, 2491-2494.
    • (1965) J. Biol. Chem , vol.240 , pp. 2491-2494
    • Fridovich, I.1


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