메뉴 건너뛰기




Volumn 46, Issue 28, 2007, Pages 8379-8391

Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis

Author keywords

[No Author keywords available]

Indexed keywords

CRYPTOSPORIDIUM HOMINIS; FOLATE-BINDING HELIX; MUTANT ENZYME; PHENYLALANINE;

EID: 34447566115     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700531r     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 0029036377 scopus 로고
    • The catalytic mechanism and structure of thymidylate synthase
    • Carreras, C. W., and Santi, D. V. (1995) The catalytic mechanism and structure of thymidylate synthase, Annu. Rev. Biochem. 64, 721-762.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 721-762
    • Carreras, C.W.1    Santi, D.V.2
  • 2
    • 0041821836 scopus 로고    scopus 로고
    • A perspective on enzyme catalysis
    • Benkovic, S. J., and Hammes-Schiffer, S. (2003) A perspective on enzyme catalysis, Science 301, 1196-1202.
    • (2003) Science , vol.301 , pp. 1196-1202
    • Benkovic, S.J.1    Hammes-Schiffer, S.2
  • 3
    • 0037457982 scopus 로고    scopus 로고
    • Conformational dynamics along an enzymatic reaction pathway: Thymidylate synthase, the movie
    • Stroud, R. M., and Finer-Moore, J. S. (2003) Conformational dynamics along an enzymatic reaction pathway: Thymidylate synthase, "the movie", Biochemistry 42, 239-247.
    • (2003) Biochemistry 42 , pp. 239-247
    • Stroud, R.M.1    Finer-Moore, J.S.2
  • 4
    • 0023667703 scopus 로고
    • Kinetics and thermodynamics of the interaction of 5-fluoro-2′- deoxyuridylate with thymidylate synthase
    • Santi, D. V., McHenry, C. S., Raines, R. T., and Ivanetich, K. M. (1987) Kinetics and thermodynamics of the interaction of 5-fluoro-2′- deoxyuridylate with thymidylate synthase, Biochemistry 26, 8606-8613.
    • (1987) Biochemistry , vol.26 , pp. 8606-8613
    • Santi, D.V.1    McHenry, C.S.2    Raines, R.T.3    Ivanetich, K.M.4
  • 5
    • 0033369958 scopus 로고    scopus 로고
    • Mapping and expression of a bifunctional thymidylate synthase, dihydrofolate reductase gene from maize
    • Cox, K., Robertson, D., and Fites, R. (1999) Mapping and expression of a bifunctional thymidylate synthase, dihydrofolate reductase gene from maize, Plant Mol. Biol. 41, 733-739.
    • (1999) Plant Mol. Biol , vol.41 , pp. 733-739
    • Cox, K.1    Robertson, D.2    Fites, R.3
  • 6
    • 0032872139 scopus 로고    scopus 로고
    • Fundamental mechanisms of substrate channeling
    • Anderson, K. S. (1999) Fundamental mechanisms of substrate channeling, Methods Enzymol. 308, 111-145.
    • (1999) Methods Enzymol , vol.308 , pp. 111-145
    • Anderson, K.S.1
  • 7
    • 0032167808 scopus 로고    scopus 로고
    • Substrate channeling and domain-domain interactions in bifunctional thymidylate synthase-dihydrofolate reductase
    • Liang, P. H., and Anderson, K. S. (1998) Substrate channeling and domain-domain interactions in bifunctional thymidylate synthase-dihydrofolate reductase, Biochemistry 37, 12195-12205.
    • (1998) Biochemistry , vol.37 , pp. 12195-12205
    • Liang, P.H.1    Anderson, K.S.2
  • 8
    • 2442601490 scopus 로고    scopus 로고
    • Kinetic Characterization of Bifunctional Thymidylate Synthase-Dihydrofolate Reductase (TS-DHFR) from Cryptosporidium hominis: A Paradigm Shift for TS Activity and Channeling Behavior
    • Atreya, C. E., and Anderson, K. S. (2004) Kinetic Characterization of Bifunctional Thymidylate Synthase-Dihydrofolate Reductase (TS-DHFR) from Cryptosporidium hominis: A Paradigm Shift for TS Activity and Channeling Behavior, J. Biol. Chem. 279, 18314-18322.
    • (2004) J. Biol. Chem , vol.279 , pp. 18314-18322
    • Atreya, C.E.1    Anderson, K.S.2
  • 9
    • 0032552965 scopus 로고    scopus 로고
    • Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis
    • Stout, T. J., Schellenberger, U., Santi, D. V., and Stroud, R. M. (1998) Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis, Biochemistry 37, 14736-14747.
    • (1998) Biochemistry , vol.37 , pp. 14736-14747
    • Stout, T.J.1    Schellenberger, U.2    Santi, D.V.3    Stroud, R.M.4
  • 10
    • 0034996721 scopus 로고    scopus 로고
    • Approaches to solving the rigid receptor problem by identifying a minimal set of flexible residues during ligand docking
    • Anderson, A. C., O'Neil, R. H., Surti, T. S., and Stroud, R. M. (2001) Approaches to solving the rigid receptor problem by identifying a minimal set of flexible residues during ligand docking, Chem. Biol. 8, 445-457.
    • (2001) Chem. Biol , vol.8 , pp. 445-457
    • Anderson, A.C.1    O'Neil, R.H.2    Surti, T.S.3    Stroud, R.M.4
  • 11
    • 0034737311 scopus 로고    scopus 로고
    • The crystal structure of thymidylate synthase from Pneumocystis carinii reveals a fungal insert important for drug design
    • Anderson, A. C., Perry, K. M., Freymann, D. M., and Stroud, R. M. (2000) The crystal structure of thymidylate synthase from Pneumocystis carinii reveals a fungal insert important for drug design, J. Mol. Biol. 297, 645-657.
    • (2000) J. Mol. Biol , vol.297 , pp. 645-657
    • Anderson, A.C.1    Perry, K.M.2    Freymann, D.M.3    Stroud, R.M.4
  • 12
    • 0347993050 scopus 로고    scopus 로고
    • Phylogenic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase- thymidylate synthase
    • O'Neil, R. H., Lilien, R. H., Donald, B. R., Stroud, R. M., and Anderson, A. C. (2003) Phylogenic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase- thymidylate synthase, J. Biol. Chem. 278, 52980-52987.
    • (2003) J. Biol. Chem , vol.278 , pp. 52980-52987
    • O'Neil, R.H.1    Lilien, R.H.2    Donald, B.R.3    Stroud, R.M.4    Anderson, A.C.5
  • 13
    • 0028091707 scopus 로고
    • Isolation of a covalent steady-state intermediate in glutamate 60 mutants of thymidylate synthase
    • Huang, W., and Santi, D. V. (1994) Isolation of a covalent steady-state intermediate in glutamate 60 mutants of thymidylate synthase, J. Biol. Chem. 269, 31327-31329.
    • (1994) J. Biol. Chem , vol.269 , pp. 31327-31329
    • Huang, W.1    Santi, D.V.2
  • 14
    • 0027102178 scopus 로고
    • Cofactor triggers the conformational change in thymidylate synthase: Implications for an ordered binding mechanism
    • Kamb, A., Finer-Moore, J. S., and Stroud, R. M. (1992) Cofactor triggers the conformational change in thymidylate synthase: Implications for an ordered binding mechanism, Biochemistry 31, 12876-12884.
    • (1992) Biochemistry , vol.31 , pp. 12876-12884
    • Kamb, A.1    Finer-Moore, J.S.2    Stroud, R.M.3
  • 15
    • 0036674124 scopus 로고    scopus 로고
    • Cryptosporidiosis: Epidemiology and impact
    • Dillingham, R., Lima, A., and Guerrant, R. (2002) Cryptosporidiosis: Epidemiology and impact, Microbes Infect. 4, 1059-1066.
    • (2002) Microbes Infect , vol.4 , pp. 1059-1066
    • Dillingham, R.1    Lima, A.2    Guerrant, R.3
  • 16
    • 0000099770 scopus 로고
    • Enzymic preparation of the L,L-diastereoisomer of tetrahydrofolic acid
    • Mathews, C. K., and Huennekens, F. M. (1960) Enzymic preparation of the L,L-diastereoisomer of tetrahydrofolic acid, J. Biol. Chem. 235, 3304-3308.
    • (1960) J. Biol. Chem , vol.235 , pp. 3304-3308
    • Mathews, C.K.1    Huennekens, F.M.2
  • 17
    • 0015500798 scopus 로고    scopus 로고
    • 2)tetrahydropteroyltriglutamate, J. Biol. Chem. 247, 1959-1964.
    • 2)tetrahydropteroyltriglutamate, J. Biol. Chem. 247, 1959-1964.
  • 18
    • 0014028229 scopus 로고
    • The dissociation constants of tetrahydrofolic acid
    • Kallen, R. G., and Jencks, W. P. (1966) The dissociation constants of tetrahydrofolic acid, J. Biol. Chem. 241, 5845-5850.
    • (1966) J. Biol. Chem , vol.241 , pp. 5845-5850
    • Kallen, R.G.1    Jencks, W.P.2
  • 19
    • 0037044746 scopus 로고    scopus 로고
    • Mechanistic characterization of Toxoplasma gondii thymidylate synthase (TS-DHFR)-dihydrofolate reductase. Evidence for a TS intermediate and TS half-sites reactivity
    • Johnson, E. F., Hinz, W., Atreya, C. E., Maley, F., and Anderson, K. S. (2002) Mechanistic characterization of Toxoplasma gondii thymidylate synthase (TS-DHFR)-dihydrofolate reductase. Evidence for a TS intermediate and TS half-sites reactivity, J. Biol. Chem. 277, 43126-43136.
    • (2002) J. Biol. Chem , vol.277 , pp. 43126-43136
    • Johnson, E.F.1    Hinz, W.2    Atreya, C.E.3    Maley, F.4    Anderson, K.S.5
  • 20
    • 0021912893 scopus 로고
    • Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica
    • Meek, T. D., Garvey, E. P., and Santi, D. V. (1985) Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica, Biochemistry 24, 678-686.
    • (1985) Biochemistry , vol.24 , pp. 678-686
    • Meek, T.D.1    Garvey, E.P.2    Santi, D.V.3
  • 21
    • 0026747630 scopus 로고
    • Thymidylate synthase with a C-terminal deletion catalyzes partial reactions but is unable to catalyze thymidylate formation
    • Carreras, C. W., Climie, S. C., and Santi, D. V. (1992) Thymidylate synthase with a C-terminal deletion catalyzes partial reactions but is unable to catalyze thymidylate formation, Biochemistry 31, 6038-6044.
    • (1992) Biochemistry , vol.31 , pp. 6038-6044
    • Carreras, C.W.1    Climie, S.C.2    Santi, D.V.3
  • 22
    • 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
  • 23
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. D50, 760-763.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. D50, 760-763.
  • 24
    • 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. D53, 240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47 (Part 2), 110-119.
    • (1991) Acta Crystallogr , vol.A47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-Building Tools for Molecular Graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: Model-Building Tools for Molecular Graphics, Acta Crystallogr. D60, 2126-2132.
    • (2004) Acta Crystallogr , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 28
    • 0345426287 scopus 로고    scopus 로고
    • The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits
    • Anderson, A. C., O'Neil, R. H., DeLano, W. L., and Stroud, R. M. (1999) The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits, Biochemistry 38, 13829-13836.
    • (1999) Biochemistry , vol.38 , pp. 13829-13836
    • Anderson, A.C.1    O'Neil, R.H.2    DeLano, W.L.3    Stroud, R.M.4
  • 29
    • 0030466872 scopus 로고    scopus 로고
    • An essential role for water in an enzyme reaction mechanism: The crystal structure of the thymidylate synthase mutant E58Q
    • Sage, C. R., Rutenber, E. E., Stout, T. J., and Stroud, R. M. (1996) An essential role for water in an enzyme reaction mechanism: The crystal structure of the thymidylate synthase mutant E58Q, Biochemistry 35, 16270-16281.
    • (1996) Biochemistry , vol.35 , pp. 16270-16281
    • Sage, C.R.1    Rutenber, E.E.2    Stout, T.J.3    Stroud, R.M.4
  • 30
    • 0035957952 scopus 로고    scopus 로고
    • Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors
    • Phan, J., Steadman, D. J., Koli, S., Ding, W. C., Minor, W., Dunlap, R. B., Berger, S. H., and Lebioda, L. (2001) Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors, J. Biol. Chem. 276, 14170-14177.
    • (2001) J. Biol. Chem , vol.276 , pp. 14170-14177
    • Phan, J.1    Steadman, D.J.2    Koli, S.3    Ding, W.C.4    Minor, W.5    Dunlap, R.B.6    Berger, S.H.7    Lebioda, L.8
  • 31
    • 0029619543 scopus 로고
    • Crystal structure of human thymidylate synthase: A structural mechanism for guiding substrates into the active site
    • Schiffer, C. A., Clifton, I. J., Davisson, V. J., Santi, D. V., and Stroud, R. M. (1995) Crystal structure of human thymidylate synthase: A structural mechanism for guiding substrates into the active site, Biochemistry 34, 16279-16287.
    • (1995) Biochemistry , vol.34 , pp. 16279-16287
    • Schiffer, C.A.1    Clifton, I.J.2    Davisson, V.J.3    Santi, D.V.4    Stroud, R.M.5
  • 33
    • 0025324512 scopus 로고
    • Development of a trichloroacetic acid precipitation assay for covalent adducts of thymidylate synthase
    • Cisneros, R. J., and Dunlap, R. B. (1990) Development of a trichloroacetic acid precipitation assay for covalent adducts of thymidylate synthase, Anal. Biochem. 186, 202-208.
    • (1990) Anal. Biochem , vol.186 , pp. 202-208
    • Cisneros, R.J.1    Dunlap, R.B.2
  • 34
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - a flexible, portable system
    • Barshop, B. A., Wrenn, R. F., and Frieden, C. (1983) Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - a flexible, portable system, Anal. Biochem. 130, 134-145.
    • (1983) Anal. Biochem , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 35
    • 0022518273 scopus 로고
    • Kinetics and mechanism of interaction of 10-propargyl-5,8-dideazafolate with thymidylate synthase
    • Pogolotti, A. L., Jr., Danenberg, P. V., and Santi, D. V. (1986) Kinetics and mechanism of interaction of 10-propargyl-5,8-dideazafolate with thymidylate synthase, J. Med. Chem. 29, 478-482.
    • (1986) J. Med. Chem , vol.29 , pp. 478-482
    • Pogolotti Jr., A.L.1    Danenberg, P.V.2    Santi, D.V.3
  • 36
    • 0025295135 scopus 로고
    • Pairwise specificity and sequential binding in enzyme catalysis: Thymidylate synthase
    • Finer-Moore, J. S., Montfort, W. R., and Stroud, R. M. (1990) Pairwise specificity and sequential binding in enzyme catalysis: Thymidylate synthase, Biochemistry 29, 6977-6986.
    • (1990) Biochemistry , vol.29 , pp. 6977-6986
    • Finer-Moore, J.S.1    Montfort, W.R.2    Stroud, R.M.3
  • 37
    • 0030221884 scopus 로고    scopus 로고
    • Potential antifolate resistance determinants and genotypic variation in the bifunctional dihydrofolate reductase-thymidylate synthase gene from human and bovine isolates of Cryptosporidium parvum
    • Vasquez, J. R., Gooze, L., Kim, K., Gut, J., Petersen, C., and Nelson, R. G. (1996) Potential antifolate resistance determinants and genotypic variation in the bifunctional dihydrofolate reductase-thymidylate synthase gene from human and bovine isolates of Cryptosporidium parvum, Mol. Biochem. Parasitol 79, 153-165.
    • (1996) Mol. Biochem. Parasitol , vol.79 , pp. 153-165
    • Vasquez, J.R.1    Gooze, L.2    Kim, K.3    Gut, J.4    Petersen, C.5    Nelson, R.G.6
  • 38
    • 0030899509 scopus 로고    scopus 로고
    • Kinetic scheme for thymidylate synthase from Escherichia coli: Determination from measurements of ligand binding, primary and secondary isotope effects, and pre-steady-state catalysis
    • Spencer, H. T., Villafranca, J. E., and Appleman, J. R. (1997) Kinetic scheme for thymidylate synthase from Escherichia coli: Determination from measurements of ligand binding, primary and secondary isotope effects, and pre-steady-state catalysis, Biochemistry 36, 4212-4222.
    • (1997) Biochemistry , vol.36 , pp. 4212-4222
    • Spencer, H.T.1    Villafranca, J.E.2    Appleman, J.R.3
  • 39
    • 0031892050 scopus 로고    scopus 로고
    • The separate effects of E60Q in Lactobacillus casei thymidylate synthase delineate between mechanisms for formation of intermediates in catalysis
    • Birdsall, D. L., Huang, W., Santi, D. V., Stroud, R. M., and Finer-Moore, J. (1998) The separate effects of E60Q in Lactobacillus casei thymidylate synthase delineate between mechanisms for formation of intermediates in catalysis, Protein Eng. 11, 171-183.
    • (1998) Protein Eng , vol.11 , pp. 171-183
    • Birdsall, D.L.1    Huang, W.2    Santi, D.V.3    Stroud, R.M.4    Finer-Moore, J.5
  • 40
    • 0029077908 scopus 로고
    • Electrostatic guidance of catalysis by a conserved glutamic acid in Escherichia coli dTMP synthase and bacteriophage T4 dCMP hydroxymethylase
    • Hardy, L. W., Graves, K. L., and Nalivaika, E. (1995) Electrostatic guidance of catalysis by a conserved glutamic acid in Escherichia coli dTMP synthase and bacteriophage T4 dCMP hydroxymethylase, Biochemistry 34, 8422-8432.
    • (1995) Biochemistry , vol.34 , pp. 8422-8432
    • Hardy, L.W.1    Graves, K.L.2    Nalivaika, E.3
  • 41
    • 0032578430 scopus 로고    scopus 로고
    • D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidine
    • Sage, C. R., Michelitsch, M. D., Stout, T. J., Biermann, D., Nissen, R., Finer-Moore, J., and Stroud, R. M. (1998) D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidine, Biochemistry 37, 13893-13901.
    • (1998) Biochemistry , vol.37 , pp. 13893-13901
    • Sage, C.R.1    Michelitsch, M.D.2    Stout, T.J.3    Biermann, D.4    Nissen, R.5    Finer-Moore, J.6    Stroud, R.M.7
  • 42
    • 0027318435 scopus 로고
    • Studies of 5-fluorodeoxyuridine 5′-monophosphate binding to carboxypeptidase A-inactivated thymidylate synthase from Lactobacillus casei
    • Cisneros, R. J., Zapf, J. W., and Dunlap, R. B. (1993) Studies of 5-fluorodeoxyuridine 5′-monophosphate binding to carboxypeptidase A-inactivated thymidylate synthase from Lactobacillus casei, J. Biol. Chem. 268, 10102-10108.
    • (1993) J. Biol. Chem , vol.268 , pp. 10102-10108
    • Cisneros, R.J.1    Zapf, J.W.2    Dunlap, R.B.3
  • 44
    • 0033609036 scopus 로고    scopus 로고
    • Substitution at residue 214 of human thymidylate synthase alters nucleotide binding and isomerization of ligand-protein complexes
    • Steadman, D. J., Spencer, H. T., Dunlap, R. B., and Berger, S. H. (1999) Substitution at residue 214 of human thymidylate synthase alters nucleotide binding and isomerization of ligand-protein complexes, Biochemistry 38, 5582-5587.
    • (1999) Biochemistry , vol.38 , pp. 5582-5587
    • Steadman, D.J.1    Spencer, H.T.2    Dunlap, R.B.3    Berger, S.H.4
  • 45
    • 0036674105 scopus 로고    scopus 로고
    • Cryptosporidiosis: Biology, pathogenesis and disease
    • Tzipori, S., and Ward, H. (2002) Cryptosporidiosis: Biology, pathogenesis and disease, Microbes Infect. 4, 1047-1058.
    • (2002) Microbes Infect , vol.4 , pp. 1047-1058
    • Tzipori, S.1    Ward, H.2
  • 48
    • 0035933350 scopus 로고    scopus 로고
    • Differential expression of two plant-like enolases with distinct enzymatic and antigenic properties during stage conversion of the protozoan parasite Toxoplasma gondii
    • Dzierszinski, F., Mortuaire, M., Dendouga, N., Popescu, O., and Tomavo, S. (2001) Differential expression of two plant-like enolases with distinct enzymatic and antigenic properties during stage conversion of the protozoan parasite Toxoplasma gondii, J. Mol. Biol. 309, 1017-1027.
    • (2001) J. Mol. Biol , vol.309 , pp. 1017-1027
    • Dzierszinski, F.1    Mortuaire, M.2    Dendouga, N.3    Popescu, O.4    Tomavo, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.