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Volumn 53, Issue 17, 2014, Pages 2855-2863

Thermal adaptation of dihydrofolate reductase from the moderate thermophile geobacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; STABILITY;

EID: 84899803746     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500238q     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 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
  • 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
    • 0023959257 scopus 로고
    • Temperature adaptation of lactate dehydrogenase structure, functional and genetic aspects
    • Zuber, H. (1988) Temperature adaptation of lactate dehydrogenase structure, functional and genetic aspects Biophys. Chem. 29, 171-179
    • (1988) Biophys. Chem. , vol.29 , pp. 171-179
    • Zuber, H.1
  • 4
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an antarctic bacterium
    • Russell, R. J. M., Gerike, U., Danson, M. J., Hough, D. W., and Taylor, G. L. (1998) Structural adaptations of the cold-active citrate synthase from an antarctic bacterium Structure 6, 351-361
    • (1998) Structure , vol.6 , pp. 351-361
    • Russell, R.J.M.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0029896617 scopus 로고    scopus 로고
    • An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases
    • 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 pyrophosphatases 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
    • 0032528267 scopus 로고    scopus 로고
    • Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family
    • Yip, K. S. P., Britton, K. L., Stillman, T. J., Lebbink, J., De Vos, W. M., Robb, F. T., Vetriani, C., Maeder, D., and Rice, D. W. (1998) Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family Eur. J. Biochem. 255, 336-346
    • (1998) Eur. J. Biochem. , vol.255 , pp. 336-346
    • Yip, K.S.P.1    Britton, K.L.2    Stillman, T.J.3    Lebbink, J.4    De Vos, W.M.5    Robb, F.T.6    Vetriani, C.7    Maeder, D.8    Rice, D.W.9
  • 10
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock, A. H. (1998) The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins J. Mol. Biol. 284, 489-502
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 11
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hyperthermophilic proteins
    • Xiao, L. and Honig, B. (1999) Electrostatic contributions to the stability of hyperthermophilic proteins J. Mol. Biol. 289, 1435-1444
    • (1999) J. Mol. Biol. , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 12
    • 0033994586 scopus 로고    scopus 로고
    • Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers
    • Kumar, S., Ma, B. Y., Tsai, C. J., and Nussinov, R. (2000) Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers Proteins 38, 368-383
    • (2000) Proteins , vol.38 , pp. 368-383
    • Kumar, S.1    Ma, B.Y.2    Tsai, C.J.3    Nussinov, R.4
  • 13
    • 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
  • 14
    • 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
  • 17
    • 0242699963 scopus 로고
    • A highly resistant thermophilic organism
    • Donk, P. J. (1920) A highly resistant thermophilic organism J. Bacteriol. 5, 373-374
    • (1920) J. Bacteriol. , vol.5 , pp. 373-374
    • Donk, P.J.1
  • 18
    • 0035064602 scopus 로고    scopus 로고
    • Taxonomic study of aerobic thermophilic Bacilli: Descriptions of Geobacillus subterraneus gen nov, sp nov and Geobacillus
    • Uzenensis sp nov from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermoglucosidasius and Bacillus thermodenitrificans to Geobacillus as the new combinations G stearothermophilus, G thermocatenulatus, G thermoleovorans, G kaustophilus, G thermoglucosidasius and G thermodenitrificans
    • Nazina, T. N., Tourova, T. P., Poltaraus, A. B., Novikova, E. V., Grigoryan, A. A., Ivanova, A. E., Lysenko, A. M., Petrunyaka, V. V., Osipov, G. A., Belyaev, S. S., and Ivanov, M. V. (2001) Taxonomic study of aerobic thermophilic Bacilli: Descriptions of Geobacillus subterraneus gen. nov., sp. nov and Geobacillus uzenensis sp. nov from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermoglucosidasius and Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. thermocatenulatus, G. thermoleovorans, G. kaustophilus, G. thermoglucosidasius and G. thermodenitrificans Int. J. Syst. Evol. Microbiol. 51, 433-446
    • (2001) Int J. Syst. Evol. Microbiol. , vol.51 , pp. 433-446
    • Nazina, T.N.1    Tourova, T.P.2    Poltaraus, A.B.3    Novikova, E.V.4    Grigoryan, A.A.5    Ivanova, A.E.6    Lysenko, A.M.7    Petrunyaka, V.V.8    Osipov, G.A.9    Belyaev, S.S.10    Ivanov, M.V.11
  • 19
    • 23944518876 scopus 로고    scopus 로고
    • Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues
    • Kim, H. S., Damo, S. M., Lee, S. Y., Wemmer, D., and Klinman, J. P. (2005) Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues Biochemistry 44, 11428-11439
    • (2005) Biochemistry , vol.44 , pp. 11428-11439
    • Kim, H.S.1    Damo, S.M.2    Lee, S.Y.3    Wemmer, D.4    Klinman, J.P.5
  • 20
    • 45849083521 scopus 로고    scopus 로고
    • Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering
    • Meinhold, L., Clement, D., Tehei, M., Daniel, R., Finney, J. L., and Smith, J. C. (2008) Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering Biochem. J. 94, 4812-4818
    • (2008) Biochem. J. , vol.94 , pp. 4812-4818
    • Meinhold, L.1    Clement, D.2    Tehei, M.3    Daniel, R.4    Finney, J.L.5    Smith, J.C.6
  • 21
    • 77953386194 scopus 로고    scopus 로고
    • Temperature dependence 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 dependence 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
  • 22
    • 80053000013 scopus 로고    scopus 로고
    • Comparative hydrogen-deuterium exchange for a mesophilic vs thermophilic dihydrofolate reductase at 25 °c: Identification of a single active site region with enhanced flexibility in the mesophilic protein
    • Oyeyemi, O. A., Sours, K. M., Lee, T., Kohen, A., Resing, K. A., Ahn, N. G., and Klinman, J. P. (2011) Comparative hydrogen-deuterium exchange for a mesophilic vs thermophilic dihydrofolate reductase at 25 °C: Identification of a single active site region with enhanced flexibility in the mesophilic protein Biochemistry 50, 8251-8260
    • (2011) Biochemistry , vol.50 , pp. 8251-8260
    • Oyeyemi, O.A.1    Sours, K.M.2    Lee, T.3    Kohen, A.4    Resing, K.A.5    Ahn, N.G.6    Klinman, J.P.7
  • 23
    • 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
  • 24
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand induced conformational changes and cooperativity in binding
    • Bystroff, C. and Kraut, J. (1991) Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand induced conformational changes and cooperativity in binding Biochemistry 30, 2227-2239
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 25
    • 77957194843 scopus 로고    scopus 로고
    • Catalysis by dihydrofolate reductase from the psychropiezophile Moritella profunda
    • Evans, R. M., Behiry, E. M., Tey, L.-H., Guo, J., Loveridge, E. J., and Allemann, R. K. (2010) Catalysis by dihydrofolate reductase from the psychropiezophile Moritella profunda ChemBioChem 11, 2010-2017
    • (2010) ChemBioChem , vol.11 , pp. 2010-2017
    • Evans, R.M.1    Behiry, E.M.2    Tey, L.-H.3    Guo, J.4    Loveridge, E.J.5    Allemann, R.K.6
  • 26
    • 0017183894 scopus 로고
    • Effect of temperature on viability of Bacillus stearothermophilus
    • Hashizume, S., Sekiguchi, T., and Nosoh, Y. (1976) Effect of temperature on viability of Bacillus stearothermophilus Arch. Microbiol. 107, 75-80
    • (1976) Arch. Microbiol. , vol.107 , pp. 75-80
    • Hashizume, S.1    Sekiguchi, T.2    Nosoh, Y.3
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 32
    • 56749083652 scopus 로고    scopus 로고
    • Solvent effects on environmentally coupled hydrogen tunnelling during catalysis by dihydrofolate reductase from Thermotoga maritima
    • Loveridge, E. J., Evans, R. M., and Allemann, R. K. (2008) Solvent effects on environmentally coupled hydrogen tunnelling during catalysis by dihydrofolate reductase from Thermotoga maritima Chem. - Eur. J. 14, 10782-10788
    • (2008) Chem. - Eur. J. , vol.14 , pp. 10782-10788
    • Loveridge, E.J.1    Evans, R.M.2    Allemann, R.K.3
  • 33
    • 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
  • 35
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., Tsai, C. J., and Nussinov, R. (2000) Factors enhancing protein thermostability Protein Eng. 13, 179-191
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 36
    • 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
  • 37
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back, J. F., Oakenfull, D., and Smith, M. B. (1979) Increased thermal stability of proteins in the presence of sugars and polyols Biochemistry 18, 5191-5196
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 38
    • 33751220492 scopus 로고    scopus 로고
    • Analysis of sugar biopretective mechanisms on the thermal denaturation of lysozyme from Raman scattering and differential scanning calorimetry investigations
    • Hédoux, A., Willart, J. F., Ionov, R., Affouard, F., Guinet, Y., Paccou, L., Lerbret, A., and Descamps, M. (2006) Analysis of sugar biopretective mechanisms on the thermal denaturation of lysozyme from Raman scattering and differential scanning calorimetry investigations J. Phys. Chem. B 110, 22886-22893
    • (2006) J. Phys. Chem. B , vol.110 , pp. 22886-22893
    • Hédoux, A.1    Willart, J.F.2    Ionov, R.3    Affouard, F.4    Guinet, Y.5    Paccou, L.6    Lerbret, A.7    Descamps, M.8
  • 39
    • 73449104308 scopus 로고    scopus 로고
    • Thermal stability of α-amylase in aqueous cosolvent systems
    • Yadav, J. K. and Prakash, V. (2009) Thermal stability of α-amylase in aqueous cosolvent systems J. Biosci. 34, 377-387
    • (2009) J. Biosci. , vol.34 , pp. 377-387
    • Yadav, J.K.1    Prakash, V.2
  • 40
    • 0032441482 scopus 로고    scopus 로고
    • Stabilization against thermal inactivation pronoted by sugars on enzyme structure and function: Why is the trehalose more effective than other sugars?
    • Sola-Penna, M. and Meyer-Fernandes, J. R. (1998) Stabilization against thermal inactivation pronoted by sugars on enzyme structure and function: Why is the trehalose more effective than other sugars? Arch. Biochem. Biophys. 360, 10-14
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 10-14
    • Sola-Penna, M.1    Meyer-Fernandes, J.R.2
  • 41
    • 0343990040 scopus 로고    scopus 로고
    • Mathematical models for the effects of pH, temperature, and sodium chloride on the growth of Bacillus stearothermophilus in salty carrots
    • Ng, T. M. and Schaffner, D. W. (1997) Mathematical models for the effects of pH, temperature, and sodium chloride on the growth of Bacillus stearothermophilus in salty carrots Appl. Environ. Microbiol. 63, 1237-1243
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1237-1243
    • Ng, T.M.1    Schaffner, D.W.2
  • 42
    • 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
  • 43
    • 0020713914 scopus 로고
    • A soluble NADH dehydrogenase (NADH:ferricyanide oxidoreductase) from Thermus aquaticus strain T351
    • Walsh, K. A. J., Daniel, R. M., and Morgan, H. W. (1983) A soluble NADH dehydrogenase (NADH:ferricyanide oxidoreductase) from Thermus aquaticus strain T351 Biochem. J. 209, 427-433
    • (1983) Biochem. J. , vol.209 , pp. 427-433
    • Walsh, K.A.J.1    Daniel, R.M.2    Morgan, H.W.3
  • 44
    • 0031027749 scopus 로고    scopus 로고
    • Purification and properties of a thermostable pullulanase from a newly isolated thermophilic anaerobic bacterium, Fervidobacterium pennavorans Ven5
    • Koch, R., Canganella, F., Hippe, H., Jahnke, K. D., and Antranikian, G. (1997) Purification and properties of a thermostable pullulanase from a newly isolated thermophilic anaerobic bacterium, Fervidobacterium pennavorans Ven5 Appl. Environ. Microbiol. 63, 1088-1094
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1088-1094
    • Koch, R.1    Canganella, F.2    Hippe, H.3    Jahnke, K.D.4    Antranikian, G.5
  • 45
    • 0029154183 scopus 로고
    • Purification and properties of a highly thermostable, sodium dodecyl sulfate-resistant and stereospecific proteinase from the extremely thermophilic archaeon Thermococcus stetteri
    • Klingeberg, M., Galunsky, B., Sjoholm, C., Kasche, V., and Antranikian, G. (1995) Purification and properties of a highly thermostable, sodium dodecyl sulfate-resistant and stereospecific proteinase from the extremely thermophilic archaeon Thermococcus stetteri Appl. Environ. Microbiol. 61, 3098-3104
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3098-3104
    • Klingeberg, M.1    Galunsky, B.2    Sjoholm, C.3    Kasche, V.4    Antranikian, G.5
  • 46
    • 0028936257 scopus 로고
    • An extremly thermostable aromatic aminotransferase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Andreotti, G., Cubellis, M. V., Nitti, G., Sannia, G., Mai, X. H., Adams, M. W. W., and Marino, G. (1995) An extremly thermostable aromatic aminotransferase from the hyperthermophilic archaeon Pyrococcus furiosus Biochim. Biophys. Acta 1247, 90-96
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 90-96
    • Andreotti, G.1    Cubellis, M.V.2    Nitti, G.3    Sannia, G.4    Mai, X.H.5    Adams, M.W.W.6    Marino, G.7
  • 47
    • 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
  • 48
    • 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
  • 49
    • 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
  • 50
    • 84878660583 scopus 로고    scopus 로고
    • Effect of Dimerization on Dihydrofolate Reductase Catalysis
    • Guo, J., Loveridge, E. J., Luk, L. Y. P., and Allemann, R. K. (2013) Effect of Dimerization on Dihydrofolate Reductase Catalysis Biochemistry 52, 3881-3887
    • (2013) Biochemistry , vol.52 , pp. 3881-3887
    • Guo, J.1    Loveridge, E.J.2    Luk, L.Y.P.3    Allemann, R.K.4
  • 51
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.