메뉴 건너뛰기




Volumn 46, Issue 33, 2007, Pages 9533-9540

Carboxy-terminus recruitment induced by substrate binding in eukaryotic fructose bis-phosphate aldolases

Author keywords

[No Author keywords available]

Indexed keywords

CONFIGURATIONAL ENTROPY; ENAMINE; PHOSPHATE BINDING RESIDUES;

EID: 34548088156     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700615r     Document Type: Article
Times cited : (9)

References (37)
  • 3
    • 0002162125 scopus 로고
    • The mechanism of action of aldolase and the asymmetric labeling of hexose
    • Rose, I. A., and Rieder, S. V. (1958) The mechanism of action of aldolase and the asymmetric labeling of hexose, J. Biol. Chem. 231, 315-329.
    • (1958) J. Biol. Chem , vol.231 , pp. 315-329
    • Rose, I.A.1    Rieder, S.V.2
  • 4
    • 0023446039 scopus 로고
    • Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution
    • Sygusch, J., Beaudry, D., and Allaire, M. (1987) Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution, Proc. Natl. Acad. Sci. U.S.A. 84, 7846-7850.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 7846-7850
    • Sygusch, J.1    Beaudry, D.2    Allaire, M.3
  • 7
    • 9344241404 scopus 로고    scopus 로고
    • Structure of human brain fructose 1,6-(bis)phosphate aldolase: Linking isozyme structure with function
    • Arakaki, T. L., Pezza, J. A., Cronin, M. A., Hopkins, C. E., Zimmer, D. B., Tolan, D. R., and Allen, K. N. (2004) Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function, Protein Sci. 13, 3077-3084.
    • (2004) Protein Sci , vol.13 , pp. 3077-3084
    • Arakaki, T.L.1    Pezza, J.A.2    Cronin, M.A.3    Hopkins, C.E.4    Zimmer, D.B.5    Tolan, D.R.6    Allen, K.N.7
  • 8
    • 0034697983 scopus 로고    scopus 로고
    • Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases
    • Chudzik, D. M., Michels, P. A., de Walque, S., and Hol, W. G. (2000) Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases, J. Mol. Biol. 300, 697-707.
    • (2000) J. Mol. Biol , vol.300 , pp. 697-707
    • Chudzik, D.M.1    Michels, P.A.2    de Walque, S.3    Hol, W.G.4
  • 9
    • 0032584256 scopus 로고    scopus 로고
    • Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum
    • Kim, H., Certa, U., Dobeli, H., Jakob, P., and Hoi, W. G. (1998) Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum, Biochemistry 37, 4388-4396.
    • (1998) Biochemistry , vol.37 , pp. 4388-4396
    • Kim, H.1    Certa, U.2    Dobeli, H.3    Jakob, P.4    Hoi, W.G.5
  • 10
  • 12
    • 22844439573 scopus 로고    scopus 로고
    • High resolution reaction intermediates of rabbit muscle fructose-1,6- bisphosphate aldolase: Substrate cleavage and induced fit
    • St-Jean, M., Lafrance-Vanasse, J., Liotard, B., and Sygusch, J. (2005) High resolution reaction intermediates of rabbit muscle fructose-1,6- bisphosphate aldolase: substrate cleavage and induced fit, J. Biol. Chem. 280, 27262-27270.
    • (2005) J. Biol. Chem , vol.280 , pp. 27262-27270
    • St-Jean, M.1    Lafrance-Vanasse, J.2    Liotard, B.3    Sygusch, J.4
  • 13
    • 0037088583 scopus 로고    scopus 로고
    • A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases
    • Maurady, A., Zdanov, A., de Moissac, D., Beaudry, D., and Sygusch, J. (2002) A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases, J. Biol. Chem. 277, 9474-9483.
    • (2002) J. Biol. Chem , vol.277 , pp. 9474-9483
    • Maurady, A.1    Zdanov, A.2    de Moissac, D.3    Beaudry, D.4    Sygusch, J.5
  • 14
    • 0031024620 scopus 로고    scopus 로고
    • Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase
    • Blom, N., and Sygusch, J. (1997) Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase, Nat. Struct. Biol. 4, 36-39.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 36-39
    • Blom, N.1    Sygusch, J.2
  • 15
    • 0000851814 scopus 로고
    • The catalytic activity of carboxypeptidase-degraded aldolase
    • Drechsler, E. R., Boyer, P. D., and Kowalsky, A. G. (1959) The catalytic activity of carboxypeptidase-degraded aldolase, J. Biol. Chem. 234, 2627-2634.
    • (1959) J. Biol. Chem , vol.234 , pp. 2627-2634
    • Drechsler, E.R.1    Boyer, P.D.2    Kowalsky, A.G.3
  • 16
    • 0000940105 scopus 로고
    • Mechanism of the aldolase reaction
    • Rose, I. A., O'Connell, E. L., and Mehler, A. H. (1965) Mechanism of the aldolase reaction, J. Biol. Chem. 240, 1758-1765.
    • (1965) J. Biol. Chem , vol.240 , pp. 1758-1765
    • Rose, I.A.1    O'Connell, E.L.2    Mehler, A.H.3
  • 17
    • 0027311253 scopus 로고
    • Differential usage of the carboxyl-terminal region among aldolase isozymes
    • Berthiaume, L., Tolan, D. R., and Sygusch, J. (1993) Differential usage of the carboxyl-terminal region among aldolase isozymes, J. Biol. Chem. 268, 10826-10835.
    • (1993) J. Biol. Chem , vol.268 , pp. 10826-10835
    • Berthiaume, L.1    Tolan, D.R.2    Sygusch, J.3
  • 18
    • 0025994844 scopus 로고
    • Carboxyl terminus region modulates catalytic activity of recombinant maize aldolase
    • Berthiaume, L., Loisel, T. P., and Sygusch, J. (1991) Carboxyl terminus region modulates catalytic activity of recombinant maize aldolase, J. Biol. Chem. 266, 17099-17105.
    • (1991) J. Biol. Chem , vol.266 , pp. 17099-17105
    • Berthiaume, L.1    Loisel, T.P.2    Sygusch, J.3
  • 19
    • 0032887162 scopus 로고    scopus 로고
    • Cloning and characterization of Leishmania mexicana fructose-1,6-bisphosphate aldolase
    • de Walque, S., Opperdoes, F. R., and Michels, P. A. (1999) Cloning and characterization of Leishmania mexicana fructose-1,6-bisphosphate aldolase, Mol. Biochem. Parasitol. 103, 279-283.
    • (1999) Mol. Biochem. Parasitol , vol.103 , pp. 279-283
    • de Walque, S.1    Opperdoes, F.R.2    Michels, P.A.3
  • 22
    • 0032125880 scopus 로고    scopus 로고
    • Differences in energy metabolism between trypanosomatidae
    • Tielens, A. G., and Van Hellemond, J. J. (1998) Differences in energy metabolism between trypanosomatidae, Parasitol. Today 14, 265-272.
    • (1998) Parasitol. Today , vol.14 , pp. 265-272
    • Tielens, A.G.1    Van Hellemond, J.J.2
  • 24
    • 0013936228 scopus 로고
    • Specific anion binding to fructose diphosphate aldolase from rabbit muscle
    • Ginsburg, A., and Mehler, A. H. (1966) Specific anion binding to fructose diphosphate aldolase from rabbit muscle, Biochemistry 5, 2623-2634.
    • (1966) Biochemistry , vol.5 , pp. 2623-2634
    • Ginsburg, A.1    Mehler, A.H.2
  • 25
    • 34548061865 scopus 로고    scopus 로고
    • on World Wide Web
    • DeLano, W. L. (2002) The PyMOL Molecular Graphics System on World Wide Web, http://www.pymol.org.
    • (2002)
    • DeLano, W.L.1
  • 26
  • 27
    • 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
  • 29
    • 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., Sect. A 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 0000243829 scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model, 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
  • 32
    • 0023927904 scopus 로고
    • Identification of structural motifs from protein coordinate data: Secondary structure and first-level supersecondary structure
    • Richards, F. M., and Kundrot, C. E. (1988) Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure, Proteins 3, 71-84.
    • (1988) Proteins , vol.3 , pp. 71-84
    • Richards, F.M.1    Kundrot, C.E.2
  • 33
    • 0027053207 scopus 로고
    • On the multiple simultaneous superposition of molecular structures by rigid body transformations
    • Diamond, R. (1992) On the multiple simultaneous superposition of molecular structures by rigid body transformations, Protein Sci. 1, 1279-1287.
    • (1992) Protein Sci , vol.1 , pp. 1279-1287
    • Diamond, R.1
  • 34
    • 0026416668 scopus 로고
    • Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects
    • Sharp, K. A., Nicholls, A., Fine, R. F., and Honig, B. (1991) Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects, Science 252, 106-109.
    • (1991) Science , vol.252 , pp. 106-109
    • Sharp, K.A.1    Nicholls, A.2    Fine, R.F.3    Honig, B.4
  • 35
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page, M. I., and Jencks, W. P. (1971) Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect, Proc. Natl. Acad. Sci. U.S.A. 68, 1678-1683.
    • (1971) Proc. Natl. Acad. Sci. U.S.A , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 36
    • 0030972797 scopus 로고    scopus 로고
    • From chemistry to biochemistry to catalysis to movement
    • Jenks, W. P. (1997) From chemistry to biochemistry to catalysis to movement, Annu. Rev. Biochem. 66, 1-18.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 1-18
    • Jenks, W.P.1
  • 37
    • 33846822002 scopus 로고    scopus 로고
    • Ligand configurational entropy and protein binding
    • Chang, C. A., Chen, W., and Gilson, M. K. (2007) Ligand configurational entropy and protein binding, Proc. Natl. Acad. Sci. U.S.A. 104, 1534-1539.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 1534-1539
    • Chang, C.A.1    Chen, W.2    Gilson, M.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.