메뉴 건너뛰기




Volumn 6, Issue 1, 1997, Pages 119-124

Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: Mechanistic implications for class I aldolases

Author keywords

aldolase; enzyme mechanism; protein crystallography; Schiff base intermediate

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; TRANSALDOLASE;

EID: 1842332171     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060113     Document Type: Article
Times cited : (65)

References (23)
  • 1
    • 0030062533 scopus 로고    scopus 로고
    • Inhibition of the catalytic activity of human transaldolase by antibodies and site-directed mutagenesis
    • Banki K, Perl A. 1996. Inhibition of the catalytic activity of human transaldolase by antibodies and site-directed mutagenesis. FEBS Lett 378:161-165.
    • (1996) FEBS Lett , vol.378 , pp. 161-165
    • Banki, K.1    Perl, A.2
  • 2
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger A. 1989. Crystallographic refinement by simulated annealing: Application to crambin. Acta Crystallogr A45:50-61.
    • (1989) Acta Crystallogr , vol.A45 , pp. 50-61
    • Brünger, A.1
  • 3
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structure
    • Brünger A. 1992. Free R value: A novel statistical quantity for assessing the accuracy of crystal structure. Nature 355:472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.1
  • 4
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A47:392-400.
    • (1991) Acta Crystallogr , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 6
    • 0029444684 scopus 로고
    • Class I aldolases: Substrate specificity, mechanism, inhibitors and structural aspects
    • Gefflaut T, Blonski C, Perie J, Willson M. 1995. Class I aldolases: Substrate specificity, mechanism, inhibitors and structural aspects. Prog Biophys Mol Biol 63:301-340.
    • (1995) Prog Biophys Mol Biol , vol.63 , pp. 301-340
    • Gefflaut, T.1    Blonski, C.2    Perie, J.3    Willson, M.4
  • 8
    • 77956895467 scopus 로고
    • Aldolases
    • Boyer PD, ed. New York: Academic Press
    • Horecker BL, Tsolas O, Lai CY. 1972. Aldolases. In: Boyer PD, ed. The Enzymes. Vol 7. New York: Academic Press. pp 213-258.
    • (1972) The Enzymes , vol.7 , pp. 213-258
    • Horecker, B.L.1    Tsolas, O.2    Lai, C.Y.3
  • 9
    • 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, Huang W, Schörken U, Sahm H, Sprenger GA, Lindqvist Y, Schneider G. 1996a. Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family. Structure 4:715-724.
    • (1996) Structure , vol.4 , pp. 715-724
    • Jia, J.1    Huang, W.2    Schörken, U.3    Sahm, H.4    Sprenger, G.A.5    Lindqvist, Y.6    Schneider, G.7
  • 10
    • 0030065103 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Escherichia coli
    • Jia J, Lindqvist Y, Schneider G, Schörken U, Sahm H, Sprenger GA. 1996b. Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Escherichia coli. Acta crystallogr D52:192-193.
    • (1996) Acta Crystallogr , vol.D52 , pp. 192-193
    • Jia, J.1    Lindqvist, Y.2    Schneider, G.3    Schörken, U.4    Sahm, H.5    Sprenger, G.A.6
  • 11
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones TA, Zou JY, Cowan S, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 12
    • 0015053755 scopus 로고
    • Studies on the structure of rabbit muscle aldolase. 3. Primary structure of the BrCN peptide containing the active site
    • Lai CY, Oshima T. 1971. Studies on the structure of rabbit muscle aldolase. 3. Primary structure of the BrCN peptide containing the active site. Arch Biochem Biophys 144:363-374.
    • (1971) Arch Biochem Biophys , vol.144 , pp. 363-374
    • Lai, C.Y.1    Oshima, T.2
  • 13
    • 0014129401 scopus 로고
    • Isolation and sequence analysis of a peptide from the active site of transaldolase
    • Lai CY, Chen C, Tsolas O. 1967a. Isolation and sequence analysis of a peptide from the active site of transaldolase. Arch Biochem Biophys 121:790-797.
    • (1967) Arch Biochem Biophys , vol.121 , pp. 790-797
    • Lai, C.Y.1    Chen, C.2    Tsolas, O.3
  • 14
    • 1842380996 scopus 로고
    • Preparation of β- Glycerophosphate aldolase and β-glyceryl transaldolase
    • Lai CY, Hoffee P, Horecker BL. 1967b. Preparation of β-glycerophosphate aldolase and β-glyceryl transaldolase. Methods Enzymol 11:667-671.
    • (1967) Methods Enzymol , vol.11 , pp. 667-671
    • Lai, C.Y.1    Hoffee, P.2    Horecker, B.L.3
  • 15
    • 0001513484 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:946-950.
    • (1993) J Appl Crystallogr , vol.26 , pp. 946-950
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, M.4
  • 16
    • 0027285118 scopus 로고
    • A data-based reaction mechanism for type I fructose bisphosphate aldolase
    • Littlechild JA, Watson HC. 1993. A data-based reaction mechanism for type I fructose bisphosphate aldolase. Trends Biosci 18:36-39.
    • (1993) Trends Biosci , vol.18 , pp. 36-39
    • Littlechild, J.A.1    Watson, H.C.2
  • 17
    • 0027332569 scopus 로고
    • Lysine 144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase
    • Miosga T, Schaaff-Gerstenschläger I, Franken E, Zimmermann FK. 1993. Lysine 144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase. Yeast 9:1241-1249.
    • (1993) Yeast , vol.9 , pp. 1241-1249
    • Miosga, T.1    Schaaff-Gerstenschläger, I.2    Franken, E.3    Zimmermann, F.K.4
  • 18
    • 0027473531 scopus 로고
    • Site-directed mutagenesis identifies Aspartate33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A
    • Morris AJ, Tolan DR. 1993. Site-directed mutagenesis identifies Aspartate33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A. J Biol Chem 268:1095-1100.
    • (1993) J Biol Chem , vol.268 , pp. 1095-1100
    • Morris, A.J.1    Tolan, D.R.2
  • 20
    • 0028862915 scopus 로고
    • Transaldolase B of Escherichia coli K-12: Cloning of its gene, talB, and characterization of the enzyme from recombinant strains
    • Sprenger GA, Schörken U, Sprenger G, Sahm H. 1995. Transaldolase B of Escherichia coli K-12: Cloning of its gene, talB, and characterization of the enzyme from recombinant strains. J Bacteriol 177:5930-5936.
    • (1995) J Bacteriol , vol.177 , pp. 5930-5936
    • Sprenger, G.A.1    Schörken, U.2    Sprenger, G.3    Sahm, H.4
  • 21
    • 0023446039 scopus 로고
    • Molecular architecture of rabbit skeletal muscle aldolase at 2.7 Å resolution
    • Sygusch J, Beaudry D, Allaire M. 1987. Molecular architecture of rabbit skeletal muscle aldolase at 2.7 Å resolution. Proc Natl Acad Sci USA 84:7846-7850.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7846-7850
    • Sygusch, J.1    Beaudry, D.2    Allaire, M.3
  • 23
    • 0001389155 scopus 로고
    • Transaldolase
    • Boyer PD, ed. New York: Academic Press
    • Tsolas O, Horecker BL. 1972. Transaldolase. In: Boyer PD, ed. The Enzymes. Vol 7. New York: Academic Press. pp. 259-280.
    • (1972) The Enzymes , vol.7 , pp. 259-280
    • Tsolas, O.1    Horecker, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.