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Volumn 376, Issue 1, 2003, Pages 277-283

Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2

Author keywords

Allosteric regulation; Eosin 5 maleimide; Phospho fructokinase 2; Pyrene N (1 pyrenyl) maleimide; SH group

Indexed keywords

ADENOSINETRIPHOSPHATE; CHEMICAL MODIFICATION; DIMERS; DISSOCIATION; ENZYMES; ESCHERICHIA COLI; MOLECULAR STRUCTURE; MONOMERS;

EID: 0344825224     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030795     Document Type: Article
Times cited : (2)

References (20)
  • 1
    • 0021883206 scopus 로고
    • Nucleotide sequence and high level expression of the major Escherichia coli phosphofructokinase
    • Hellinga, H. W. and Evans, P. R. (1985) Nucleotide sequence and high level expression of the major Escherichia coli phosphofructokinase. Eur. J. Biochem. 149, 363-373
    • (1985) Eur. J. Biochem. , vol.149 , pp. 363-373
    • Hellinga, H.W.1    Evans, P.R.2
  • 2
    • 0018185175 scopus 로고
    • Phosphofructokinases from Escherichia coli: Purification and characterization of the nonallosteric isozyme
    • Babul, J. (1978) Phosphofructokinases from Escherichia coli: purification and characterization of the nonallosteric isozyme. J. Biol. Chem. 253, 4350-4355
    • (1978) J. Biol. Chem. , vol.253 , pp. 4350-4355
    • Babul, J.1
  • 3
    • 0014413329 scopus 로고
    • Kinetics of allosteric interactions of pohosphofructokinase from Escherichia coli
    • Blangy, D., Buc, H. and Monod, J. (1968) Kinetics of allosteric interactions of pohosphofructokinase from Escherichia coli. J. Mol. Biol. 31, 13-35
    • (1968) J. Mol. Biol. , vol.31 , pp. 13-35
    • Blangy, D.1    Buc, H.2    Monod, J.3
  • 4
    • 0021265957 scopus 로고
    • Kinetic mechanism of phosphofructokinase-2 from Escherichia coli
    • Campos, G., Guixé, V. and Babul, J. (1984) Kinetic mechanism of phosphofructokinase-2 from Escherichia coli. J. Biol. Chem. 259, 6147-6152
    • (1984) J. Biol. Chem. , vol.259 , pp. 6147-6152
    • Campos, G.1    Guixé, V.2    Babul, J.3
  • 5
    • 0022226641 scopus 로고
    • Effect of ATP on phosphofructokinase-2 from Escherichia coli. A mutant enzyme altered in the allosteric site for MgATP
    • Guixé, V. and Babul, J. (1985) Effect of ATP on phosphofructokinase-2 from Escherichia coli. A mutant enzyme altered in the allosteric site for MgATP. J. Biol. Chem. 260, 11001-11005
    • (1985) J. Biol. Chem. , vol.260 , pp. 11001-11005
    • Guixé, V.1    Babul, J.2
  • 6
    • 0345647106 scopus 로고    scopus 로고
    • Ligand-induced conformational transitions in Escherichia coli phosphofructokinase-2: Evidence for an allosteric site for MgATP
    • Guixé, V., Rodríguez, P. H. and Babul, J. (1998) Ligand-induced conformational transitions in Escherichia coli phosphofructokinase-2: evidence for an allosteric site for MgATP. Biochemistry 37, 13269-13275
    • (1998) Biochemistry , vol.37 , pp. 13269-13275
    • Guixé, V.1    Rodríguez, P.H.2    Babul, J.3
  • 7
    • 0023742763 scopus 로고
    • Influence of ligands on the aggregation of the normal and mutant forms of phosphofructokinase-2 of Escherichia coli
    • Guixé, V. and Babul, J. (1988) Influence of ligands on the aggregation of the normal and mutant forms of phosphofructokinase-2 of Escherichia coli. Arch. Biochem. Biophys. 264, 519-524
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 519-524
    • Guixé, V.1    Babul, J.2
  • 8
    • 0036399167 scopus 로고    scopus 로고
    • Ligand-dependent structural changes and limited proteolysis of E. coli phosphofructokinase-2
    • Cabrera, C., Guixé, V., Alfaro, J., Rodríguez, P. H. and Babul, J. (2002) Ligand-dependent structural changes and limited proteolysis of E. coli phosphofructokinase-2. Arch. Biochem. Biophys. 406, 289-295
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 289-295
    • Cabrera, C.1    Guixé, V.2    Alfaro, J.3    Rodríguez, P.H.4    Babul, J.5
  • 9
    • 0033907956 scopus 로고    scopus 로고
    • Sequencing, cloning and high level expression of the pfp gene, encoding a PPi-dependent phosphofructokinase from the extremely thermophilic eubacterium Dictyoglomus thermophilum
    • Ding, Y. R., Ronimus, R. S. and Morgan, H. W. (2000) Sequencing, cloning and high level expression of the pfp gene, encoding a PPi-dependent phosphofructokinase from the extremely thermophilic eubacterium Dictyoglomus thermophilum. J. Bacteriol. 182, 4661-4666
    • (2000) J. Bacteriol. , vol.182 , pp. 4661-4666
    • Ding, Y.R.1    Ronimus, R.S.2    Morgan, H.W.3
  • 10
    • 0031596609 scopus 로고    scopus 로고
    • PPi-dependent phosphofructokinase from Thermoproteus tenax, an archeal descendant of an ancient line in phosphofructokinase evolution
    • Siebers, B., Klenk, H. P. and Hensel, R. (1998) PPi-dependent phosphofructokinase from Thermoproteus tenax, an archeal descendant of an ancient line in phosphofructokinase evolution. J. Bacteriol. 180, 2137-2143
    • (1998) J. Bacteriol. , vol.180 , pp. 2137-2143
    • Siebers, B.1    Klenk, H.P.2    Hensel, R.3
  • 11
    • 0035158003 scopus 로고    scopus 로고
    • Thermotoga maritima phosphofructokinases: Expression and characterization of two unique enzymes
    • Ding, Y. R., Ronimus, R. S. and Morgan, H. W. (2001) Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes. J. Bacteriol. 183, 791-794
    • (2001) J. Bacteriol. , vol.183 , pp. 791-794
    • Ding, Y.R.1    Ronimus, R.S.2    Morgan, H.W.3
  • 12
    • 0033571484 scopus 로고    scopus 로고
    • Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1 -kinase of Borrelia burgddoferi
    • Deng, Z., Roberts, D., Wang, X. and Kemp, R. G. (1999) Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1 -kinase of Borrelia burgddoferi. Arch. Biochem. Biophys. 371, 326-331
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 326-331
    • Deng, Z.1    Roberts, D.2    Wang, X.3    Kemp, R.G.4
  • 13
    • 0035799336 scopus 로고    scopus 로고
    • Reaction path of phosphofructo-1-kinase is altered by mutagenesis and alternative substrates
    • Wang, X. and Kemp, R. G. (2001) Reaction path of phosphofructo-1-kinase is altered by mutagenesis and alternative substrates. Biochemistry 40, 3938-3942
    • (2001) Biochemistry , vol.40 , pp. 3938-3942
    • Wang, X.1    Kemp, R.G.2
  • 14
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork, P., Sander, C. and Valencia, A. (1993) Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein. Sci. 2, 31-40
    • (1993) Protein. Sci. , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 16
    • 0037631360 scopus 로고    scopus 로고
    • Domain motions and quaternary packing of phosphofructokinase-2 from Escherichia coli studied by small angle X-ray scattering and homology modeling
    • Cabrera, R., Fischer, H., Trapani, S., Craievich, A. F., Garrat, R. C., Guixé, V. and Babul, J. (2003) Domain motions and quaternary packing of phosphofructokinase-2 from Escherichia coli studied by small angle X-ray scattering and homology modeling. J. Biol. Chem. 278, 12913-12919
    • (2003) J. Biol. Chem. , vol.278 , pp. 12913-12919
    • Cabrera, R.1    Fischer, H.2    Trapani, S.3    Craievich, A.F.4    Garrat, R.C.5    Guixé, V.6    Babul, J.7
  • 17
    • 0034656069 scopus 로고    scopus 로고
    • Chemical modification of SH groups of E. coli phosphofructokinase-2 induces subunit dissociation: Monomers are inactive but preserve ligand binding properties
    • Guixé, V. (2000) Chemical modification of SH groups of E. coli phosphofructokinase-2 induces subunit dissociation: monomers are inactive but preserve ligand binding properties. Arch. Biochem. Biophys. 376, 313-319
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 313-319
    • Guixé, V.1
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0029026779 scopus 로고
    • Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: Revised amino acid sequence, site-directed mutagenesis, and microenviroment characteristics of cysteines 365 and 458
    • Krautwust, H., Encinas, M. V., Marcus, F., Latshaw, S. T., Kemp, R. G., Frey, P. A. and Cardemil, E. (1995) Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenviroment characteristics of cysteines 365 and 458. Biochemistry 34, 6382-6388
    • (1995) Biochemistry , vol.34 , pp. 6382-6388
    • Krautwust, H.1    Encinas, M.V.2    Marcus, F.3    Latshaw, S.T.4    Kemp, R.G.5    Frey, P.A.6    Cardemil, E.7
  • 20
    • 0028241105 scopus 로고
    • Bovine inositol monophosphatase. Ligand binding to pyrene-maleimide- labelled enzyme
    • Greasley, P. J., Hunt, L. G. and Gore, M. G. (1994) Bovine inositol monophosphatase. Ligand binding to pyrene-maleimide-labelled enzyme. Eur. J. Biochem. 222, 453-460
    • (1994) Eur. J. Biochem. , vol.222 , pp. 453-460
    • Greasley, P.J.1    Hunt, L.G.2    Gore, M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.