메뉴 건너뛰기




Volumn 8, Issue 2, 1999, Pages 291-297

Crystal structure of human muscle aldolase complexed with fructose 1,6- bisphosphate: Mechanistic implications

Author keywords

Fructose 1,6 bisphosphate aldolase; Mechanism; Schiff's base

Indexed keywords

FRUCTOSE 1,6 BISPHOSPHATE; FRUCTOSE BISPHOSPHATE ALDOLASE; MUSCLE ENZYME;

EID: 0032965916     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.2.291     Document Type: Article
Times cited : (96)

References (41)
  • 1
    • 0015797959 scopus 로고
    • Pyridoxal phosphate binding site of rabbit muscle aldolase
    • Anai M, Lai CY, Horecker BL. 1973. Pyridoxal phosphate binding site of rabbit muscle aldolase. Arch Biochem Biophys 156:712-719.
    • (1973) Arch Biochem Biophys , vol.156 , pp. 712-719
    • Anai, M.1    Lai, C.Y.2    Horecker, B.L.3
  • 2
    • 0031024620 scopus 로고    scopus 로고
    • Product binding and role of the C-terminal region in class I D-fructose-1,6-bisphosphate aldolase
    • Blom NS, 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.S.1    Sygusch, J.2
  • 3
    • 0029761259 scopus 로고    scopus 로고
    • Novel active site in escherichia coli fructose-1,6-bisphosphate aldolase
    • Blom NS, Tetreault S, Coulombe R, Sygusch J. 1996. Novel active site in Escherichia coli fructose-1,6-bisphosphate aldolase. Nat Struc Biol 3:856-862.
    • (1996) Nat Struc Biol , vol.3 , pp. 856-862
    • Blom, N.S.1    Tetreault, S.2    Coulombe, R.3    Sygusch, J.4
  • 4
    • 0030949759 scopus 로고    scopus 로고
    • Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds
    • Blonski C, De Moissac DD, Périe J, Sygusch J. 1997. Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds. Biochem J 323:71-77.
    • (1997) Biochem J , vol.323 , pp. 71-77
    • Blonski, C.1    De Moissac, D.D.2    Périe, J.3    Sygusch, J.4
  • 5
    • 0028955737 scopus 로고
    • Divergent evolution of a β/α-barrel subclass: Detection of numerous phosphate-binding sites by motif search
    • Bork P, Gellerich J, Groth H, Hooft R, Martin F. 1995. Divergent evolution of a β/α-barrel subclass: Detection of numerous phosphate-binding sites by motif search. Protein Sci 4:268-274.
    • (1995) Protein Sci , vol.4 , pp. 268-274
    • Bork, P.1    Gellerich, J.2    Groth, H.3    Hooft, R.4    Martin, F.5
  • 7
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • Brünger AT. 1993. Assessment of phase accuracy by cross validation: The free R value. Methods and applications. Acta Crystallogr A42:140-149.
    • (1993) Acta Crystallogr , vol.A42 , pp. 140-149
    • Brünger, A.T.1
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4, The Collaborative Computational Project, No. 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 9
    • 0030589053 scopus 로고    scopus 로고
    • The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold
    • Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar A, Plater A, Berry A, Hunter WH. 1996. The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. Structure 14:1303-1315.
    • (1996) Structure , vol.14 , pp. 1303-1315
    • Cooper, S.J.1    Leonard, G.A.2    McSweeney, S.M.3    Thompson, A.W.4    Naismith, J.H.5    Qamar, A.6    Plater, A.7    Berry, A.8    Hunter, W.H.9
  • 10
    • 0030513295 scopus 로고    scopus 로고
    • The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli
    • Dreyer MK, Schultz GE. 1996. The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. Acta Crystallogr D52:1082-1091.
    • (1996) Acta Crystallogr , vol.D52 , pp. 1082-1091
    • Dreyer, M.K.1    Schultz, G.E.2
  • 12
    • 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
  • 13
    • 0027230033 scopus 로고
    • Paracatalytic inactivation of fructose 1,6-bisphosphate aldolase
    • Gupta S, Hollenstein R, Kochbar S, Christen P. 1993. Paracatalytic inactivation of fructose 1,6-bisphosphate aldolase. Eur J Biochem 214:515-519.
    • (1993) Eur J Biochem , vol.214 , pp. 515-519
    • Gupta, S.1    Hollenstein, R.2    Kochbar, S.3    Christen, P.4
  • 14
    • 0017159311 scopus 로고
    • Affinity labelling of a previously undetected lysyl residue in class I aldolase
    • Hartman FC, Brown JP. 1978. Affinity labelling of a previously undetected lysyl residue in class I aldolase. J Biol Chem 251:3057-3062.
    • (1978) J Biol Chem , vol.251 , pp. 3057-3062
    • Hartman, F.C.1    Brown, J.P.2
  • 17
    • 0030585419 scopus 로고    scopus 로고
    • Crystal structure of transaldolase 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. 1996. Crystal structure of transaldolase 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
  • 18
    • 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, Schörken U, Lindqvist Y, Sprenger GA, Schneider G. 1997. 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) Protein Sci , vol.6 , pp. 119-124
    • Jia, J.1    Schörken, U.2    Lindqvist, Y.3    Sprenger, G.A.4    Schneider, G.5
  • 19
    • 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
  • 20
    • 0026298598 scopus 로고
    • Topography and conformational changes of fructose-1,6-bisphosphate aldolase
    • Kochman M, Dobryszycki P. 1991. Topography and conformational changes of fructose-1,6-bisphosphate aldolase. Acta Biochim Pol 38:407-421.
    • (1991) Acta Biochim Pol , vol.38 , pp. 407-421
    • Kochman, M.1    Dobryszycki, P.2
  • 21
    • 0015951572 scopus 로고
    • Amino acid sequence of rabbit muscle aldolase and the structure of the active site
    • Lai C, Nakai N, Chang D. 1974. Amino acid sequence of rabbit muscle aldolase and the structure of the active site. Science 183:1204-1206.
    • (1974) Science , vol.183 , pp. 1204-1206
    • Lai, C.1    Nakai, N.2    Chang, D.3
  • 22
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin VS, Wilson KS. 1993. Automated refinement of protein models. Acta Crystallogr D49:129-147.
    • (1993) Acta Crystallogr , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 24
    • 0016699271 scopus 로고
    • Arginine as the C-1 phosphate binding site in rabbit muscle aldolase
    • Lobb RR, Stokes AM, Hill HAO, Riordan JF. 1976. Arginine as the C-1 phosphate binding site in rabbit muscle aldolase. FEBS Lett 54:70-72.
    • (1976) FEBS Lett , vol.54 , pp. 70-72
    • Lobb, R.R.1    Stokes, A.M.2    Hill, H.A.O.3    Riordan, J.F.4
  • 25
    • 0026604146 scopus 로고
    • Fructose-bisphosphate aldolases: An evolutionary biology
    • Marsh JJ, Lebherz HG. 1992. Fructose-bisphosphate aldolases: An evolutionary biology. Trends Biosci 17:110-113.
    • (1992) Trends Biosci , vol.17 , pp. 110-113
    • Marsh, J.J.1    Lebherz, H.G.2
  • 27
    • 0027473531 scopus 로고
    • Site directed mutagenesis identifies Asp 33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A
    • Morris AJ, Tolan DR. 1993. Site directed mutagenesis identifies Asp 33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A. J Biol Chem 268:1095-1102.
    • (1993) J Biol Chem , vol.268 , pp. 1095-1102
    • Morris, A.J.1    Tolan, D.R.2
  • 28
    • 33751158425 scopus 로고
    • Lysine 146 of rabbit muscle aldolase is essential for the cleavage and condensation of the C3-C4 bond of fructose 1,6-bisphosphate
    • Morris AJ, Tolan DR. 1994. Lysine 146 of rabbit muscle aldolase is essential for the cleavage and condensation of the C3-C4 bond of fructose 1,6-bisphosphate. Biochemistry 33:12291-12297.
    • (1994) Biochemistry , vol.33 , pp. 12291-12297
    • Morris, A.J.1    Tolan, D.R.2
  • 29
    • 0014369485 scopus 로고
    • The mechanism of action of aldolases
    • Morse DE, Horecker BL. 1968. The mechanism of action of aldolases. Adv Enzymol 31:125-181.
    • (1968) Adv Enzymol , vol.31 , pp. 125-181
    • Morse, D.E.1    Horecker, B.L.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallogr D53:240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, 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
  • 32
    • 0014603237 scopus 로고
    • Molecular and catalytic properties of human aldolase C
    • Penhoet EE, Kochman M, Rutter WJ. 1969. Molecular and catalytic properties of human aldolase C. Biochemistry 8:4396-4402.
    • (1969) Biochemistry , vol.8 , pp. 4396-4402
    • Penhoet, E.E.1    Kochman, M.2    Rutter, W.J.3
  • 34
    • 0017336858 scopus 로고
    • 2 aldolase (muscle) and partition of the enzyme among catalytic intermediates in the steady state
    • 2 aldolase (muscle) and partition of the enzyme among catalytic intermediates in the steady state. J Biol Chem 253:479-482.
    • (1977) J Biol Chem , vol.253 , pp. 479-482
    • Rose, I.A.1    O'Connell, E.L.2
  • 35
    • 0001369687 scopus 로고
    • The evolution of aldolase
    • Rutter WJ. 1964. The evolution of aldolase. Fed Proc 23:1248-1257.
    • (1964) Fed Proc , vol.23 , pp. 1248-1257
    • Rutter, W.J.1
  • 36
    • 0028035218 scopus 로고
    • Cross-linked enzyme crystals of fructose diphosphate aldolase: Development as a catalyst for synthesis
    • Sobolev SB, Bartoszko-Malik A, Oeschger TR, Montelbano MM. 1994. Cross-linked enzyme crystals of fructose diphosphate aldolase: Development as a catalyst for synthesis. Tetrahedron Lett 35:7751-7754.
    • (1994) Tetrahedron Lett , vol.35 , pp. 7751-7754
    • Sobolev, S.B.1    Bartoszko-Malik, A.2    Oeschger, T.R.3    Montelbano, M.M.4
  • 37
    • 0021257326 scopus 로고
    • Catalytic activity of rabbit skeletal muscle aldolase in the crystal state
    • Sygusch J, Beaudry D. 1984. Catalytic activity of rabbit skeletal muscle aldolase in the crystal state. J Biol Chem 259:10222-10227.
    • (1984) J Biol Chem , vol.259 , pp. 10222-10227
    • Sygusch, J.1    Beaudry, D.2
  • 38
    • 0023446039 scopus 로고
    • Molecular architecture of rabbit skeletal muscle aldolase at 2.7 angstrom resolution
    • Sygusch J, Beaudry D, Allaire M. 1987. Molecular architecture of rabbit skeletal muscle aldolase at 2.7 angstrom 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
  • 39
    • 0025634063 scopus 로고
    • Inactivation of mammalian fructose diphosphate aldolases by COOH terminus autophosphorylation
    • Sygusch J, Beaudry D, Allaire M. 1990. Inactivation of mammalian fructose diphosphate aldolases by COOH terminus autophosphorylation. Arch Biochem Biophys 283:227-233.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 227-233
    • Sygusch, J.1    Beaudry, D.2    Allaire, M.3
  • 40
    • 0024520620 scopus 로고
    • Site directed mutagenesis of human aldolase isozymes: The role of cys. 72 and cys. 338 residues of aldolase A and the carboxy-terminal tyr residues of aldolase A and B
    • Takahashi I, Takasaki Y, Hori K. 1989. Site directed mutagenesis of human aldolase isozymes: The role of cys. 72 and cys. 338 residues of aldolase A and the carboxy-terminal tyr residues of aldolase A and B. J Biochem 105:281-286.
    • (1989) J Biochem , vol.105 , pp. 281-286
    • Takahashi, I.1    Takasaki, Y.2    Hori, K.3
  • 41
    • 0026571088 scopus 로고
    • Studies on chimeric fusion proteins of human aldolase isozymes A and B
    • Takahashi I, Hori K. 1992. Studies on chimeric fusion proteins of human aldolase isozymes A and B. Protein Eng 5:101-104.
    • (1992) Protein Eng , vol.5 , pp. 101-104
    • Takahashi, I.1    Hori, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.