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Volumn 7, Issue 10, 2011, Pages 678-684

Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ALDOSE ERYTHROSE 4 PHOSPHATE; FRUCTOSE 6 PHOSPHATE; KETOSE; LYSINE; PHOSPHATE; SCHIFF BASE; SEDOHEPTULOSE 7 PHOSPHATE; TRANSALDOLASE; UNCLASSIFIED DRUG;

EID: 80052961459     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.633     Document Type: Article
Times cited : (59)

References (31)
  • 1
    • 63049112606 scopus 로고    scopus 로고
    • Transaldolase: From biochemistry to human disease
    • Samland, A. K. & Sprenger, G. A. Transaldolase: from biochemistry to human disease. Int. J. Biochem. Cell Biol. 41, 1482-1494 (2009).
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1482-1494
    • Samland, A.K.1    Sprenger, G.A.2
  • 2
    • 0037073492 scopus 로고    scopus 로고
    • The pentose phosphate pathway
    • Horecker, B. L. The pentose phosphate pathway. J. Biol. Chem. 277, 47965-47971 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47965-47971
    • Horecker, B.L.1
  • 4
    • 0030585419 scopus 로고    scopus 로고
    • Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family
    • Jia, J. et al. Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family. Structure 4, 715-724 (1996). (Pubitemid 126661294)
    • (1996) Structure , vol.4 , Issue.6 , pp. 715-724
    • Jia, J.1    Huang, W.2    Schorken, U.3    Sahm, H.4    Sprenger, G.A.5    Lindqvist, Y.6    Schneider, G.7
  • 6
    • 1842332171 scopus 로고    scopus 로고
    • Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: Mechanistic implications for class I aldolases
    • Jia, J., Schorken, U., Lindqvist, Y., Sprenger, G. A. & Schneider, G. Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases. Protein Sci. 6, 119-124 (1997). (Pubitemid 27045250)
    • (1997) Protein Science , vol.6 , Issue.1 , pp. 119-124
    • Jia, J.1    Schorken, U.2    Lindqvist, Y.3    Sprenger, G.A.4    Schneider, G.5
  • 9
    • 0036304877 scopus 로고    scopus 로고
    • Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family
    • DOI 10.1016/S0022-2836(02)00258-9
    • Thorell, S., Schurmann, M., Sprenger, G. A. & Schneider, G. Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family. J. Mol. Biol. 319, 161-171 (2002). (Pubitemid 34729493)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 161-171
    • Thorell, S.1    Schurmann, M.2    Sprenger, G.A.3    Schneider, G.4
  • 10
    • 57649143109 scopus 로고    scopus 로고
    • Replacement of a phenylalanine by a tyrosine in the active site confers fructose-6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin
    • Schneider, S., Sandalova, T., Schneider, G., Sprenger, G. A. & Samland, A. K. Replacement of a phenylalanine by a tyrosine in the active site confers fructose-6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin. J. Biol. Chem. 283, 30064-30072 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 30064-30072
    • Schneider, S.1    Sandalova, T.2    Schneider, G.3    Sprenger, G.A.4    Samland, A.K.5
  • 11
    • 0000767302 scopus 로고
    • Conformations of acyclic sugar derivatives: Part II. Determination of conformations of alditol acetates in solution by use of 250-Mhz n. m.r. spectra
    • Angyal, S. J., Lefur, R. & Gagnaire, D. Conformations of acyclic sugar derivatives: part II. Determination of conformations of alditol acetates in solution by use of 250-Mhz n. m.r. spectra. Carbohydr. Res. 23, 121-134 (1972).
    • (1972) Carbohydr. Res. , vol.23 , pp. 121-134
    • Angyal, S.J.1    Lefur, R.2    Gagnaire, D.3
  • 12
    • 0002921257 scopus 로고
    • Carbon-13-enriched carbohydrates. Preparation of erythrose, threose, glyceraldehyde, and glycolaldehyde with 13C enrichment in various carbon atoms
    • Serianni, A. S., Clark, E. L. & Barker, R. Carbon-13-enriched carbohydrates. Preparation of erythrose, threose, glyceraldehyde, and glycolaldehyde with 13C enrichment in various carbon atoms. Carbohydr. Res. 72, 79-91 (1979).
    • (1979) Carbohydr. Res. , vol.72 , pp. 79-91
    • Serianni, A.S.1    Clark, E.L.2    Barker, R.3
  • 13
    • 22844439573 scopus 로고    scopus 로고
    • High resolution reaction intermediates of rabbit muscle fructose- 1,6-bisphosphate aldolase: Substrate cleavage and induced fit
    • DOI 10.1074/jbc.M502413200
    • St-Jean, M., Lafrance-Vanasse, J., Liotard, B. & Sygusch, J. High resolution reaction intermediates of rabbit muscle fructose-1, 6-bisphosphate aldolase: substrate cleavage and induced fit. J. Biol. Chem. 280, 27262-27270 (2005). (Pubitemid 41040766)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 27262-27270
    • St.-Jean, M.1    Lafrance-Vanasse, J.2    Liotard, B.3    Sygusch, J.4
  • 15
    • 77949782018 scopus 로고    scopus 로고
    • Redesigning the active site of transaldolase TalB from Escherichia coli: New variants with improved affinity towards nonphosphorylated substrates
    • Schneider, S. et al. Redesigning the active site of transaldolase TalB from Escherichia coli: new variants with improved affinity towards nonphosphorylated substrates. ChemBioChem 11, 681-690 (2010).
    • (2010) ChemBioChem , vol.11 , pp. 681-690
    • Schneider, S.1
  • 16
    • 77954232498 scopus 로고    scopus 로고
    • Structure of a class I tagatose-1, 6-bisphosphate aldolase investigation into an apparent loss of stereospecificity
    • LowKam, C., Liotard, B. & Sygusch, J. Structure of a class I tagatose-1, 6-bisphosphate aldolase investigation into an apparent loss of stereospecificity. J. Biol. Chem. 285, 21143-21152 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 21143-21152
    • LowKam, C.1    Liotard, B.2    Sygusch, J.3
  • 17
  • 19
    • 35648979411 scopus 로고    scopus 로고
    • Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate
    • DOI 10.1021/bi700844m
    • Asztalos, P. et al. Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46, 12037-12052 (2007). (Pubitemid 350022361)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12037-12052
    • Asztalos, P.1    Parthier, C.2    Golbik, R.3    Kleinschmidt, M.4    Hubner, G.5    Weiss, M.S.6    Friedemann, R.7    Wille, G.8    Tittmann, K.9
  • 20
    • 47349102781 scopus 로고    scopus 로고
    • Thiamin diphosphate catalysis: Enzymic and nonenzymic covalent intermediates
    • Kluger, R. & Tittmann, K. Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates. Chem. Rev. 108, 1797-1833 (2008).
    • (2008) Chem. Rev. , vol.108 , pp. 1797-1833
    • Kluger, R.1    Tittmann, K.2
  • 21
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr, D. D., Nussinov, R. & Wright, P. E. The role of dynamic conformational ensembles in biomolecular recognition. Nat. Chem. Biol. 5, 789-796 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 22
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • Hammes, G. G., Chang, Y. C. & Oas, T. G. Conformational selection or induced fit: a flux description of reaction mechanism. Proc. Natl. Acad. Sci. USA 106, 13737-13741 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 23
    • 68649107927 scopus 로고    scopus 로고
    • Preparative scale enzymatic synthesis of D-sedoheptulose-7-phosphate from β-hydroxypyruvate and D-ribose-5-phosphate
    • Charmantray, F., Helaine, V., Legeret, B. & Hecquet, L. Preparative scale enzymatic synthesis of D-sedoheptulose-7-phosphate from β-hydroxypyruvate and D-ribose-5-phosphate. J. Mol. Catal. B Enzym. 57, 6-9 (2009).
    • (2009) J. Mol. Catal. B Enzym. , vol.57 , pp. 6-9
    • Charmantray, F.1    Helaine, V.2    Legeret, B.3    Hecquet, L.4
  • 24
    • 77957818235 scopus 로고    scopus 로고
    • The crystal structure of human transketolase and new insights into its mode of action
    • Mitschke, L. et al. The crystal structure of human transketolase and new insights into its mode of action. J. Biol. Chem. 285, 31559-31570 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 31559-31570
    • Mitschke, L.1
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 30
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new sofware suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography & NMR system: a new sofware suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 31
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J. & Wodak, S. J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205 (1999). (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3


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