메뉴 건너뛰기




Volumn 52, Issue 22, 2013, Pages 3881-3887

Effect of dimerization on dihydrofolate reductase catalysis

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC ABILITY; DIHYDROFOLATE REDUCTASE; DIMER INTERFACE; DIMERIC ENZYME; ELECTROSTATIC ENVIRONMENTS; HYPERTHERMOPHILES; LOOP REGIONS; THERMOTOGA MARITIMA;

EID: 84878660583     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4005073     Document Type: Article
Times cited : (9)

References (55)
  • 1
    • 38949175472 scopus 로고
    • Thermophilic bacteria
    • Bergey, D. H. (1919) Thermophilic bacteria J. Bacteriol. 4, 301-306
    • (1919) J. Bacteriol. , vol.4 , pp. 301-306
    • Bergey, D.H.1
  • 2
    • 0030970741 scopus 로고    scopus 로고
    • Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus
    • Haney, P., Konisky, J., Koretke, K. K., Luthey-Schulten, Z., and Wolynes, P. G. (1997) Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus Proteins 28, 117-130
    • (1997) Proteins , vol.28 , pp. 117-130
    • Haney, P.1    Konisky, J.2    Koretke, K.K.3    Luthey-Schulten, Z.4    Wolynes, P.G.5
  • 3
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic Archaeon pyrococcus furiosus at 1.9 Å resolution
    • Russell, R. J. M., Ferguson, J. M. C., Hough, D. W., Danson, M. J., and Taylor, G. L. (1997) The crystal structure of citrate synthase from the hyperthermophilic Archaeon pyrococcus furiosus at 1.9 Å resolution Biochemistry 36, 9983-9994
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.J.M.1    Ferguson, J.M.C.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 4
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe, K., Hata, Y., Kizaki, H., Katsube, Y., and Suzuki, Y. (1997) The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization J. Mol. Biol. 269, 142-153
    • (1997) J. Mol. Biol. , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 5
    • 0031837178 scopus 로고    scopus 로고
    • Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase
    • Bogin, O., Peretz, M., Hacham, Y., Korkhin, Y., Frolow, F., Kalb, A. J., and Burstein, Y. (1998) Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase Protein Sci. 7, 1156-1163
    • (1998) Protein Sci. , vol.7 , pp. 1156-1163
    • Bogin, O.1    Peretz, M.2    Hacham, Y.3    Korkhin, Y.4    Frolow, F.5    Kalb, A.J.6    Burstein, Y.7
  • 6
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing?
    • Vogt, G. and Argos, P. (1997) Protein thermal stability: Hydrogen bonds or internal packing? Folding Des. 2, S40-S46
    • (1997) Folding Des. , vol.2
    • Vogt, G.1    Argos, P.2
  • 7
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G., Woell, S., and Argos, P. (1997) Protein thermal stability, hydrogen bonds, and ion pairs J. Mol. Biol. 269, 631-643
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 8
    • 0029896617 scopus 로고    scopus 로고
    • An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic prophosphatases
    • Salminen, T., Teplyakov, A., Kankare, J., Cooperman, B. S., Lahti, R., and Goldman, A. (1996) An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic prophosphatases Protein Sci. 5, 1014-1025
    • (1996) Protein Sci. , vol.5 , pp. 1014-1025
    • Salminen, T.1    Teplyakov, A.2    Kankare, J.3    Cooperman, B.S.4    Lahti, R.5    Goldman, A.6
  • 9
    • 78049461379 scopus 로고    scopus 로고
    • Some applications of thermophilies and their enzymes for protein processing
    • Synowiecki, J. (2010) Some applications of thermophilies and their enzymes for protein processing Afr. J. Biotechnol. 9, 7020-7025
    • (2010) Afr. J. Biotechnol. , vol.9 , pp. 7020-7025
    • Synowiecki, J.1
  • 10
    • 77953386194 scopus 로고    scopus 로고
    • Temperature denpendence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency
    • Oyeyemi, O. A., Sours, K. M., Lee, T., Resing, K. A., Ahn, N. G., and Klinman, J. P. (2010) Temperature denpendence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency Proc. Natl. Acad. Sci. U.S.A. 107, 10074-10079
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10074-10079
    • Oyeyemi, O.A.1    Sours, K.M.2    Lee, T.3    Resing, K.A.4    Ahn, N.G.5    Klinman, J.P.6
  • 11
    • 79953823548 scopus 로고    scopus 로고
    • A dynamic knockout reveals that conformational fluctuation influence the chemical step of enzyme catalysis
    • Bhabha, G., Lee, J., Ekiert, D. C., Gam, J., Wilson, I. A., Dyson, H. J., Benkovic, S. J., and Wright, P. E. (2011) A dynamic knockout reveals that conformational fluctuation influence the chemical step of enzyme catalysis Science 332, 234-238
    • (2011) Science , vol.332 , pp. 234-238
    • Bhabha, G.1    Lee, J.2    Ekiert, D.C.3    Gam, J.4    Wilson, I.A.5    Dyson, H.J.6    Benkovic, S.J.7    Wright, P.E.8
  • 12
    • 80052149070 scopus 로고    scopus 로고
    • Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions
    • Adamczyk, A. J., Cao, J., Kamerlin, S. C. L., and Warshel, A. (2011) Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions Proc. Natl. Acad. Sci. U.S.A. 108, 14115-14120
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14115-14120
    • Adamczyk, A.J.1    Cao, J.2    Kamerlin, S.C.L.3    Warshel, A.4
  • 13
    • 0141596172 scopus 로고    scopus 로고
    • Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases
    • Georlette, D., Damien, B., Blaise, V., Depiereux, E., Uversky, V. N., Gerday, C., and Feller, G. (2003) Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases J. Biol. Chem. 278, 37015-37023
    • (2003) J. Biol. Chem. , vol.278 , pp. 37015-37023
    • Georlette, D.1    Damien, B.2    Blaise, V.3    Depiereux, E.4    Uversky, V.N.5    Gerday, C.6    Feller, G.7
  • 14
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, and thermophilic adenylate kinases
    • Bae, E. and Phillips, G. N. (2004) Structures and analysis of highly homologous psychrophilic, and thermophilic adenylate kinases J. Biol. Chem. 279, 28202-28208
    • (2004) J. Biol. Chem. , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips, G.N.2
  • 15
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky, P., Kardos, J., Svingor, A., and Petsko, G. A. (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins Proc. Natl. Acad. Sci. U.S.A. 95, 7406-7411
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 18
    • 78649358299 scopus 로고    scopus 로고
    • The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed H-transfer
    • Stojković, V., Perissinotti, L. L., Lee, J., Benkovic, S. J., and Kohen, A. (2010) The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed H-transfer Chem. Commun. 46, 8974-8976
    • (2010) Chem. Commun. , vol.46 , pp. 8974-8976
    • Stojković, V.1    Perissinotti, L.L.2    Lee, J.3    Benkovic, S.J.4    Kohen, A.5
  • 19
    • 0041761262 scopus 로고    scopus 로고
    • Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima
    • Maglia, G., Javed, M. H., and Allemann, R. K. (2003) Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima Biochem. J. 374, 529-535
    • (2003) Biochem. J. , vol.374 , pp. 529-535
    • Maglia, G.1    Javed, M.H.2    Allemann, R.K.3
  • 20
    • 0345647102 scopus 로고    scopus 로고
    • Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability
    • Dams, T., Bohm, G., Auerbach, G., Bader, G., Schuring, H., and Jaenicke, R. (1998) Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability Biol. Chem. 379, 367-371
    • (1998) Biol. Chem. , vol.379 , pp. 367-371
    • Dams, T.1    Bohm, G.2    Auerbach, G.3    Bader, G.4    Schuring, H.5    Jaenicke, R.6
  • 21
    • 0033551438 scopus 로고    scopus 로고
    • Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima
    • Dams, T. and Jaenicke, R. (1999) Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima Biochemistry 38, 9169-9178
    • (1999) Biochemistry , vol.38 , pp. 9169-9178
    • Dams, T.1    Jaenicke, R.2
  • 23
    • 71749090188 scopus 로고    scopus 로고
    • The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer
    • Pijning, T., van Pouderoyen, G., Kluskens, L., van der Oost, J., and Dijkstra, B. W. (2009) The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer FEBS Lett. 583, 3665-3670
    • (2009) FEBS Lett. , vol.583 , pp. 3665-3670
    • Pijning, T.1    Van Pouderoyen, G.2    Kluskens, L.3    Van Der Oost, J.4    Dijkstra, B.W.5
  • 24
    • 77953879146 scopus 로고    scopus 로고
    • The temperature dependence of the kinetic isotope effects of dihydrofolate reductase from Thermotoga maritima is influenced by intersubunit interactions
    • Loveridge, E. J. and Allemann, R. K. (2010) The temperature dependence of the kinetic isotope effects of dihydrofolate reductase from Thermotoga maritima is influenced by intersubunit interactions Biochemistry 49, 5390-5396
    • (2010) Biochemistry , vol.49 , pp. 5390-5396
    • Loveridge, E.J.1    Allemann, R.K.2
  • 25
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • Dams, T., Auerbach, G., Bader, G., Jacob, U., Ploom, T., Huber, R., and Jaenicke, R. (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability J. Mol. Biol. 297, 659-672
    • (2000) J. Mol. Biol. , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 26
    • 67649610422 scopus 로고    scopus 로고
    • Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritima
    • Loveridge, E. J., Rodriguez, R. J., Swanwick, R. S., and Allemann, R. K. (2009) Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritima Biochemistry 48, 5922-5933
    • (2009) Biochemistry , vol.48 , pp. 5922-5933
    • Loveridge, E.J.1    Rodriguez, R.J.2    Swanwick, R.S.3    Allemann, R.K.4
  • 27
    • 33846889293 scopus 로고    scopus 로고
    • Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR
    • Pang, J. Y. and Allemann, R. K. (2007) Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR Phys. Chem. Chem. Phys. 9, 711-718
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 711-718
    • Pang, J.Y.1    Allemann, R.K.2
  • 28
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • Radkiewicz, J. L. and Brooks, C. L. (2000) Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase J. Am. Chem. Soc. 122, 225-231
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 225-231
    • Radkiewicz, J.L.1    Brooks, C.L.2
  • 30
    • 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
  • 31
    • 33745362450 scopus 로고    scopus 로고
    • Hydride transfer reaction catalyzed by hyperthermophilic dihydrofolate reductase is dominated by quantum mechanical tunneling and is promoted by both inter- and intramonomeric correlated motions
    • Pang, J. Y., Pu, J. Z., Gao, J. L., Truhlar, D. G., and Allemann, R. K. (2006) Hydride transfer reaction catalyzed by hyperthermophilic dihydrofolate reductase is dominated by quantum mechanical tunneling and is promoted by both inter- and intramonomeric correlated motions J. Am. Chem. Soc. 128, 8015-8023
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8015-8023
    • Pang, J.Y.1    Pu, J.Z.2    Gao, J.L.3    Truhlar, D.G.4    Allemann, R.K.5
  • 32
    • 70350561103 scopus 로고    scopus 로고
    • The role of arginine 28 in catalysis by dihydrofolate reductase from the hyperthermophile Thermotoga maritima
    • Loveridge, E. J., Maglia, G., and Allemann, R. K. (2009) The role of arginine 28 in catalysis by dihydrofolate reductase from the hyperthermophile Thermotoga maritima ChemBioChem 10, 2624-2627
    • (2009) ChemBioChem , vol.10 , pp. 2624-2627
    • Loveridge, E.J.1    Maglia, G.2    Allemann, R.K.3
  • 33
    • 79955972786 scopus 로고    scopus 로고
    • Effect of pH on hydride transfer by Escherichia coli dihydrofolate reductase
    • Loveridge, E. J. and Allemann, R. K. (2011) Effect of pH on hydride transfer by Escherichia coli dihydrofolate reductase ChemBioChem 12, 1258-1262
    • (2011) ChemBioChem , vol.12 , pp. 1258-1262
    • Loveridge, E.J.1    Allemann, R.K.2
  • 34
    • 0014027643 scopus 로고
    • On mechanism of chemical and enzymatic reduction of folate and dihydrofolate
    • Zakrzewski, S. F. (1966) On mechanism of chemical and enzymatic reduction of folate and dihydrofolate J. Biol. Chem. 241, 2962-2967
    • (1966) J. Biol. Chem. , vol.241 , pp. 2962-2967
    • Zakrzewski, S.F.1
  • 35
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C. A., Johnson, K. A., and Benkovic, S. J. (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli Biochemistry 26, 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 36
    • 32944457660 scopus 로고    scopus 로고
    • Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase
    • Swanwick, R. S., Maglia, G., Tey, L.-H., and Allemann, R. K. (2006) Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase Biochem. J. 394, 259-265
    • (2006) Biochem. J. , vol.394 , pp. 259-265
    • Swanwick, R.S.1    Maglia, G.2    Tey, L.-H.3    Allemann, R.K.4
  • 37
    • 0020466628 scopus 로고
    • Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli
    • Stone, S. R. and Morrison, J. F. (1982) Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli Biochemistry 21, 3757-3765
    • (1982) Biochemistry , vol.21 , pp. 3757-3765
    • Stone, S.R.1    Morrison, J.F.2
  • 38
    • 0020441466 scopus 로고
    • Crystal-structures of Escherichia coli and Lactobacillus casei dihydrofolate-reductase refined at 1.7 Å resolution. 1. General features and binding of methotrexate
    • Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C., and Kraut, J. (1982) Crystal-structures of Escherichia coli and Lactobacillus casei dihydrofolate-reductase refined at 1.7 Å resolution. 1. General features and binding of methotrexate J. Biol. Chem. 257, 3650-3662
    • (1982) J. Biol. Chem. , vol.257 , pp. 3650-3662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 39
    • 77749255402 scopus 로고    scopus 로고
    • Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms
    • Goihberg, E., Peretz, M., Tel-Or, S., Dym, O., Shimon, L., Frolow, F., and Burstein, Y. (2010) Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms Biochemistry 49, 1943-1953
    • (2010) Biochemistry , vol.49 , pp. 1943-1953
    • Goihberg, E.1    Peretz, M.2    Tel-Or, S.3    Dym, O.4    Shimon, L.5    Frolow, F.6    Burstein, Y.7
  • 40
    • 1842531419 scopus 로고    scopus 로고
    • Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: The altered structure of a mutant enzyme may form the basis of its diminished catalytic performance
    • Swanwick, R. S., Shrimpton, P. J., and Allemann, R. K. (2004) Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: The altered structure of a mutant enzyme may form the basis of its diminished catalytic performance Biochemistry 43, 4119-4127
    • (2004) Biochemistry , vol.43 , pp. 4119-4127
    • Swanwick, R.S.1    Shrimpton, P.J.2    Allemann, R.K.3
  • 41
    • 0037083390 scopus 로고    scopus 로고
    • Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway
    • Sham, Y. Y., Ma, B. Y., Tsai, C. J., and Nussinov, R. (2002) Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway Proteins 46, 308-320
    • (2002) Proteins , vol.46 , pp. 308-320
    • Sham, Y.Y.1    Ma, B.Y.2    Tsai, C.J.3    Nussinov, R.4
  • 42
    • 0025373255 scopus 로고
    • Refolding of Escherichia coli dihydrofolate reductase: Sequential formation of substrate binding sites
    • Frieden, C. (1990) Refolding of Escherichia coli dihydrofolate reductase: Sequential formation of substrate binding sites Proc. Natl. Acad. Sci. U.S.A. 87, 4413-4416
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4413-4416
    • Frieden, C.1
  • 43
    • 23644442411 scopus 로고    scopus 로고
    • Incresed thermal stability of site-selectively glycosylated dihydrofolate reductase
    • Swanwick, R. S., Daines, A. M., Tey, L. H., Flitsch, S. L., and Allemann, R. K. (2005) Incresed thermal stability of site-selectively glycosylated dihydrofolate reductase ChemBioChem 6, 1338-1340
    • (2005) ChemBioChem , vol.6 , pp. 1338-1340
    • Swanwick, R.S.1    Daines, A.M.2    Tey, L.H.3    Flitsch, S.L.4    Allemann, R.K.5
  • 44
    • 77951209387 scopus 로고    scopus 로고
    • Highly site-selective stability increases by glycosylation of dihydrofolate reductase
    • Tey, L. H., Loveridge, E. J., Swanwick, R. S., Flitsch, S. L., and Allemann, R. K. (2010) Highly site-selective stability increases by glycosylation of dihydrofolate reductase FEBS J. 277, 2171-2179
    • (2010) FEBS J. , vol.277 , pp. 2171-2179
    • Tey, L.H.1    Loveridge, E.J.2    Swanwick, R.S.3    Flitsch, S.L.4    Allemann, R.K.5
  • 45
    • 0242267579 scopus 로고    scopus 로고
    • Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis
    • Maglia, G. and Allemann, R. K. (2003) Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis J. Am. Chem. Soc. 125, 13372-13373
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13372-13373
    • Maglia, G.1    Allemann, R.K.2
  • 46
    • 0028305058 scopus 로고
    • Determination by raman spectroscopy of the pKa of N5 of dihydrofolate bond to dihydrofolate reductase: Mechanistic implications
    • Chen, Y.-Q., Kraut, J., Blakely, R. L., and Callender, R. (1994) Determination by raman spectroscopy of the pKa of N5 of dihydrofolate bond to dihydrofolate reductase: Mechanistic implications Biochemistry 33, 7021-7026
    • (1994) Biochemistry , vol.33 , pp. 7021-7026
    • Chen, Y.-Q.1    Kraut, J.2    Blakely, R.L.3    Callender, R.4
  • 47
    • 76149110500 scopus 로고    scopus 로고
    • Solvent effects on catalysis by Escherichia coli dihydrofolate reductase
    • Loveridge, E. J., Tey, L.-H., and Allemann, R. K. (2010) Solvent effects on catalysis by Escherichia coli dihydrofolate reductase J. Am. Chem. Soc. 132, 1137-1143
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1137-1143
    • Loveridge, E.J.1    Tey, L.-H.2    Allemann, R.K.3
  • 49
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M. R. and Kraut, J. (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence Biochemistry 36, 586-603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 51
    • 84858758329 scopus 로고    scopus 로고
    • Evidence that a 'dynamic knockout' in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis
    • Loveridge, E. J., Behiry, E. M., Guo, J., and Allemann, R. K. (2012) Evidence that a 'dynamic knockout' in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis Nat. Chem. 4, 292-297
    • (2012) Nat. Chem. , vol.4 , pp. 292-297
    • Loveridge, E.J.1    Behiry, E.M.2    Guo, J.3    Allemann, R.K.4
  • 54
    • 0034625317 scopus 로고    scopus 로고
    • Strengthening the dimerisation interface of Lac repressor increases its thermostability by 40 C
    • Gerk, L. P., Levon, O., and Muller-Hill, B. (2000) Strengthening the dimerisation interface of Lac repressor increases its thermostability by 40 C J. Mol. Biol. 299, 805-812
    • (2000) J. Mol. Biol. , vol.299 , pp. 805-812
    • Gerk, L.P.1    Levon, O.2    Muller-Hill, B.3
  • 55
    • 0034654087 scopus 로고    scopus 로고
    • Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
    • Thoma, R., Hennig, M., Sterner, R., and Kirschner, K. (2000) Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima Structure 8, 265-276
    • (2000) Structure , vol.8 , pp. 265-276
    • Thoma, R.1    Hennig, M.2    Sterner, R.3    Kirschner, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.