메뉴 건너뛰기




Volumn 1784, Issue 7-8, 2008, Pages 1115-1121

Effects of pressure on enzyme function of Escherichia coli dihydrofolate reductase

Author keywords

Dihydrofolate reductase; Enzyme activity; High pressure; Volume change

Indexed keywords

DEUTERIUM; DIHYDROFOLATE REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAHYDROFOLIC ACID;

EID: 52449135534     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.005     Document Type: Article
Times cited : (26)

References (28)
  • 2
    • 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. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36 (1997) 586-603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 3
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
    • Kitahara R., Sareth S., Yamada H., Ohmae E., Gekko K., and Akasaka K. High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry 39 (2000) 12789-12795
    • (2000) Biochemistry , vol.39 , pp. 12789-12795
    • Kitahara, R.1    Sareth, S.2    Yamada, H.3    Ohmae, E.4    Gekko, K.5    Akasaka, K.6
  • 4
    • 0027998347 scopus 로고
    • Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function
    • Gekko K., Kunori Y., Takeuchi H., Ichihara S., and Kodama M. Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: important roles of a flexible loop in the stability and function. J. Biochem. (Tokyo) 116 (1994) 34-41
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 34-41
    • Gekko, K.1    Kunori, Y.2    Takeuchi, H.3    Ichihara, S.4    Kodama, M.5
  • 5
    • 0029939820 scopus 로고    scopus 로고
    • Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function
    • Ohmae E., Iriyama K., Ichihara S., and Gekko K. Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. (Tokyo) 119 (1996) 703-710
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 703-710
    • Ohmae, E.1    Iriyama, K.2    Ichihara, S.3    Gekko, K.4
  • 6
    • 0031981532 scopus 로고    scopus 로고
    • Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and function
    • Ohmae E., Ishimura K., Iwakura M., and Gekko K. Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. (Tokyo) 123 (1998) 839-846
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 839-846
    • Ohmae, E.1    Ishimura, K.2    Iwakura, M.3    Gekko, K.4
  • 8
    • 0034836475 scopus 로고    scopus 로고
    • Effects of pressure on the activity and spectroscopic properties of carboxyl proteinases. Apparent correlation of pepstatin-insensitivity and pressure response
    • Fujiwara S., Kunugi S., Oyama H., and Oda K. Effects of pressure on the activity and spectroscopic properties of carboxyl proteinases. Apparent correlation of pepstatin-insensitivity and pressure response. Eur. J. Biochem. 268 (2001) 645-655
    • (2001) Eur. J. Biochem. , vol.268 , pp. 645-655
    • Fujiwara, S.1    Kunugi, S.2    Oyama, H.3    Oda, K.4
  • 9
    • 0037171123 scopus 로고    scopus 로고
    • Effects of high pressure on enzymatic activity
    • Northrop D.B. Effects of high pressure on enzymatic activity. Biochem. Biophys. Acta 1595 (2002) 71-79
    • (2002) Biochem. Biophys. Acta , vol.1595 , pp. 71-79
    • Northrop, D.B.1
  • 10
    • 23144459878 scopus 로고    scopus 로고
    • Linear and non-linear pressure dependence of enzyme catalytic parameters
    • Masson P., and Balny C. Linear and non-linear pressure dependence of enzyme catalytic parameters. Biochem. Biophys. Acta 1724 (2005) 440-450
    • (2005) Biochem. Biophys. Acta , vol.1724 , pp. 440-450
    • Masson, P.1    Balny, C.2
  • 11
    • 33645973697 scopus 로고    scopus 로고
    • What lies in the future of high-pressure bioscience?
    • Balny C. What lies in the future of high-pressure bioscience?. Biochem. Biophys. Acta 1764 (2006) 632-639
    • (2006) Biochem. Biophys. Acta , vol.1764 , pp. 632-639
    • Balny, C.1
  • 12
    • 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. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26 (1987) 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 13
    • 0034704984 scopus 로고    scopus 로고
    • Effect of ligand binding on the flexibility of dihydrofolate reductase as revealed by compressibility
    • Kamiyama T., and Gekko K. Effect of ligand binding on the flexibility of dihydrofolate reductase as revealed by compressibility. Biochim. Biophys. Acta 1478 (2000) 257-266
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 257-266
    • Kamiyama, T.1    Gekko, K.2
  • 14
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr D.D., McElheny D., Dyson H.J., and Wright P.E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313 (2006) 1638-1642
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 15
    • 4644368825 scopus 로고    scopus 로고
    • Pressure-dependent activity of dihydrofolate reductase from a deep-sea bacterium Shewanella violacea strain DSS12
    • Ohmae E., Kubota K., Nakasone K., Kato C., and Gekko K. Pressure-dependent activity of dihydrofolate reductase from a deep-sea bacterium Shewanella violacea strain DSS12. Chem. Lett. 33 (2004) 798-799
    • (2004) Chem. Lett. , vol.33 , pp. 798-799
    • Ohmae, E.1    Kubota, K.2    Nakasone, K.3    Kato, C.4    Gekko, K.5
  • 16
    • 0028952263 scopus 로고
    • A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase gene from Escherichia coli
    • Iwakura M., Jones B.E., Luo J., and Matthews C.R. A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase gene from Escherichia coli. J. Biochem. (Tokyo) 117 (1995) 480-488
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 480-488
    • Iwakura, M.1    Jones, B.E.2    Luo, J.3    Matthews, C.R.4
  • 18
    • 0018759051 scopus 로고
    • Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase
    • Williams J.W., Morrison J.F., and Duggleby R.G. Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase. Biochemistry 18 (1979) 2567-2573
    • (1979) Biochemistry , vol.18 , pp. 2567-2573
    • Williams, J.W.1    Morrison, J.F.2    Duggleby, R.G.3
  • 19
    • 0020466628 scopus 로고
    • Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli
    • Stone S.R., and Morrison J.F. Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli. Biochemistry 21 (1982) 3757-3765
    • (1982) Biochemistry , vol.21 , pp. 3757-3765
    • Stone, S.R.1    Morrison, J.F.2
  • 20
    • 0021872251 scopus 로고
    • Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase
    • Penner M.H., and Frieden C. Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase. J. Biol. Chem. 260 (1985) 5366-5369
    • (1985) J. Biol. Chem. , vol.260 , pp. 5366-5369
    • Penner, M.H.1    Frieden, C.2
  • 21
    • 0015752362 scopus 로고
    • The reliability of Michaelis constants and maximum velocities estimated by using the integrated Michaelis-Menten equation
    • Atkins G.L., and Nimmo I.A. The reliability of Michaelis constants and maximum velocities estimated by using the integrated Michaelis-Menten equation. Biochem. J. 135 (1973) 779-784
    • (1973) Biochem. J. , vol.135 , pp. 779-784
    • Atkins, G.L.1    Nimmo, I.A.2
  • 22
    • 5644245248 scopus 로고    scopus 로고
    • Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function
    • Goudar C.T., Harris S.K., McInerney M.J., and Suflita J.M. Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function. J. Microbiol. Methods 59 (2004) 317-326
    • (2004) J. Microbiol. Methods , vol.59 , pp. 317-326
    • Goudar, C.T.1    Harris, S.K.2    McInerney, M.J.3    Suflita, J.M.4
  • 24
    • 0034097153 scopus 로고    scopus 로고
    • Effects of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis
    • Northrop D.B., and Cho Y.K. Effects of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis. Biochemistry 39 (2000) 2406-2412
    • (2000) Biochemistry , vol.39 , pp. 2406-2412
    • Northrop, D.B.1    Cho, Y.K.2
  • 25
    • 0035936574 scopus 로고    scopus 로고
    • Effect of pressure on deuterium isotope effects of formate dehydrogenase
    • Quirk D.J., and Northrop D.B. Effect of pressure on deuterium isotope effects of formate dehydrogenase. Biochemistry 40 (2001) 847-851
    • (2001) Biochemistry , vol.40 , pp. 847-851
    • Quirk, D.J.1    Northrop, D.B.2
  • 26
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
    • Cameron C.E., and Benkovic S.J. Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry 36 (1997) 15792-15800
    • (1997) Biochemistry , vol.36 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 27
    • 0025270551 scopus 로고
    • + ternary complex. Substrate binding and a model for the transition state
    • + ternary complex. Substrate binding and a model for the transition state. Biochemistry 29 (1990) 3263-3277
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.