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Volumn 581, Issue 16, 2007, Pages 3033-3038

Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: Implications for ligand binding sites

Author keywords

Allosteric transition; Enzyme engineering; Enzyme regulation; Glycolysis; Phosphofructokinase

Indexed keywords

6 PHOSPHOFRUCTOKINASE; CHIMERIC PROTEIN; FRUCTOSE 1,6 BISPHOSPHATE; FRUCTOSE 2,6 BISPHOSPHATE; ISOENZYME; TETRAMER;

EID: 34250320522     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.059     Document Type: Article
Times cited : (7)

References (31)
  • 2
    • 0019751252 scopus 로고
    • Multimodulation of enzyme activity
    • Sols A. Multimodulation of enzyme activity. Curr. Top. Cell. Regul. 19 (1981) 77-101
    • (1981) Curr. Top. Cell. Regul. , vol.19 , pp. 77-101
    • Sols, A.1
  • 3
    • 85047669951 scopus 로고
    • Allosteric regulatory properties of muscle phosphofructokinase
    • Kemp R.G., and Foe L.G. Allosteric regulatory properties of muscle phosphofructokinase. Mol. Cell Biochem. 57 (1983) 147-154
    • (1983) Mol. Cell Biochem. , vol.57 , pp. 147-154
    • Kemp, R.G.1    Foe, L.G.2
  • 4
    • 0025189804 scopus 로고
    • Structural basis of the allosteric behaviour of phosphofructokinase
    • Schirmer T., and Evans P.R. Structural basis of the allosteric behaviour of phosphofructokinase. Nature (London) 343 (1990) 140-145
    • (1990) Nature (London) , vol.343 , pp. 140-145
    • Schirmer, T.1    Evans, P.R.2
  • 5
    • 0021256418 scopus 로고
    • Evolution of phosphofructokinase: gene duplication and creation of new effector sites
    • Poorman R.A., Randolph A., Kemp R.G., and Heinrikson R.L. Evolution of phosphofructokinase: gene duplication and creation of new effector sites. Nature (London) 309 (1984) 467-469
    • (1984) Nature (London) , vol.309 , pp. 467-469
    • Poorman, R.A.1    Randolph, A.2    Kemp, R.G.3    Heinrikson, R.L.4
  • 6
    • 0030037752 scopus 로고    scopus 로고
    • A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate
    • Heinisch J.J., Boles E., and Timple C. A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. J. Biol. Chem. 271 (1996) 15928-15933
    • (1996) J. Biol. Chem. , vol.271 , pp. 15928-15933
    • Heinisch, J.J.1    Boles, E.2    Timple, C.3
  • 7
    • 0033534164 scopus 로고    scopus 로고
    • Identification of allosteric sites in rabbit phosphofructo-1-kinase
    • Li Y., Rivera D., Ru W., Gunasekera D., and Kemp R.G. Identification of allosteric sites in rabbit phosphofructo-1-kinase. Biochemistry 38 (1999) 16407-16412
    • (1999) Biochemistry , vol.38 , pp. 16407-16412
    • Li, Y.1    Rivera, D.2    Ru, W.3    Gunasekera, D.4    Kemp, R.G.5
  • 8
    • 0036293409 scopus 로고    scopus 로고
    • Role of Ser530, Arg292, and His662 in the allosteric behavior of rabbit muscle phosphofructokinase
    • Chang S.H., and Kemp R.G. Role of Ser530, Arg292, and His662 in the allosteric behavior of rabbit muscle phosphofructokinase. Biochem. Biophys. Res. Commun. 290 (2002) 670-675
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 670-675
    • Chang, S.H.1    Kemp, R.G.2
  • 9
    • 0037199468 scopus 로고    scopus 로고
    • Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase
    • Kemp R.G., and Gunasekera D. Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase. Biochemistry 41 (2002) 9426-9430
    • (2002) Biochemistry , vol.41 , pp. 9426-9430
    • Kemp, R.G.1    Gunasekera, D.2
  • 10
    • 34250305856 scopus 로고    scopus 로고
    • Identification of C-terminal motifs responsible for transmission of inhibition by ATP of mammalian phosphofructokinase, and their contribution to other allosteric effects
    • Martínez-Costa O.H., Hermida C., Sánchez-Martínez C., Santamaría C., and Aragón J.J. Identification of C-terminal motifs responsible for transmission of inhibition by ATP of mammalian phosphofructokinase, and their contribution to other allosteric effects. Biochem. J. 374 (2004) 100-104
    • (2004) Biochem. J. , vol.374 , pp. 100-104
    • Martínez-Costa, O.H.1    Hermida, C.2    Sánchez-Martínez, C.3    Santamaría, C.4    Aragón, J.J.5
  • 12
    • 0023157057 scopus 로고
    • Nature of the subunits of the 6-phosphofructo-1-kinase isoenzymes from rat tissues
    • Dunaway G.A., and Kasten T.P. Nature of the subunits of the 6-phosphofructo-1-kinase isoenzymes from rat tissues. Biochem. J. 242 (1987) 667-671
    • (1987) Biochem. J. , vol.242 , pp. 667-671
    • Dunaway, G.A.1    Kasten, T.P.2
  • 13
    • 0040697067 scopus 로고    scopus 로고
    • Analysis of phosphofructokinase subunits and isozymes in ascites tumour cells and its original tissue, murine mammary gland
    • Sánchez-Martínez C., and Aragón J.J. Analysis of phosphofructokinase subunits and isozymes in ascites tumour cells and its original tissue, murine mammary gland. FEBS Lett. 409 (1997) 86-90
    • (1997) FEBS Lett. , vol.409 , pp. 86-90
    • Sánchez-Martínez, C.1    Aragón, J.J.2
  • 14
    • 0021956861 scopus 로고
    • Isolation and characterization of phosphofructokinase C from rabbit brain
    • Foe L.G., and Kemp R.G. Isolation and characterization of phosphofructokinase C from rabbit brain. J. Biol. Chem. 260 (1985) 726-730
    • (1985) J. Biol. Chem. , vol.260 , pp. 726-730
    • Foe, L.G.1    Kemp, R.G.2
  • 15
    • 0023918653 scopus 로고
    • Analysis of the phosphofructokinase subunits and isozymes in human tissues
    • Dunaway G.A., Kasten T.P., Sebo T., and Trapp R. Analysis of the phosphofructokinase subunits and isozymes in human tissues. Biochem. J. 251 (1988) 677-683
    • (1988) Biochem. J. , vol.251 , pp. 677-683
    • Dunaway, G.A.1    Kasten, T.P.2    Sebo, T.3    Trapp, R.4
  • 16
    • 0342656636 scopus 로고    scopus 로고
    • Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties
    • Sánchez-Martínez C., Estévez A.M., and Aragón J.J. Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties. Biochem. Biophys. Res. Commun. 271 (2000) 635-640
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 635-640
    • Sánchez-Martínez, C.1    Estévez, A.M.2    Aragón, J.J.3
  • 17
    • 0017131087 scopus 로고
    • Control of phosphofructokinase from rat skeletal muscle
    • Tornheim K., and Lowenstein J. Control of phosphofructokinase from rat skeletal muscle. J. Biol. Chem. 251 (1976) 7322-7328
    • (1976) J. Biol. Chem. , vol.251 , pp. 7322-7328
    • Tornheim, K.1    Lowenstein, J.2
  • 18
    • 0342919888 scopus 로고
    • Control of liver 6-phosphofructokinase by fructose 2,6-bisphosphate and other effectors
    • Van Shaftingen E., Jett M.-F., Hue L., and Hers H.-G. Control of liver 6-phosphofructokinase by fructose 2,6-bisphosphate and other effectors. Proc. Natl. Acad. Sci. USA 78 (1981) 3483-3486
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3483-3486
    • Van Shaftingen, E.1    Jett, M.-F.2    Hue, L.3    Hers, H.-G.4
  • 19
    • 0021112132 scopus 로고
    • A binding study of the interaction of β-d-fructose 2,6-bisphosphate with phosphofructokinase and fructose-1,6-bisphosphatase
    • Kitajima S., and Uyeda K. A binding study of the interaction of β-d-fructose 2,6-bisphosphate with phosphofructokinase and fructose-1,6-bisphosphatase. J. Biol. Chem. 258 (1983) 7352-7357
    • (1983) J. Biol. Chem. , vol.258 , pp. 7352-7357
    • Kitajima, S.1    Uyeda, K.2
  • 20
    • 0022363123 scopus 로고
    • Activation of muscle phosphofructokinase by fructose 2,6-bisphosphate and fructose 1,6-bisphosphate is differently affected by other regulatory metabolites
    • Tornheim K. Activation of muscle phosphofructokinase by fructose 2,6-bisphosphate and fructose 1,6-bisphosphate is differently affected by other regulatory metabolites. J. Biol. Chem. 260 (1985) 7985-7989
    • (1985) J. Biol. Chem. , vol.260 , pp. 7985-7989
    • Tornheim, K.1
  • 22
    • 0028793189 scopus 로고
    • Functional complementation of yeast phosphofructokinase mutants by the non-allosteric enzyme from Dictyostelium discoideum
    • Estévez A.M., Heinisch J.J., and Aragón J.J. Functional complementation of yeast phosphofructokinase mutants by the non-allosteric enzyme from Dictyostelium discoideum. FEBS Lett. 377 (1995) 77-84
    • (1995) FEBS Lett. , vol.377 , pp. 77-84
    • Estévez, A.M.1    Heinisch, J.J.2    Aragón, J.J.3
  • 23
    • 0028890670 scopus 로고
    • Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency
    • Raben N., Exelbert R., Spiegel R., Sherman J.B., Nakajima H., Plotz P., and Heinisch J. Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am. J. Hum. Genet. 56 (1995) 131-141
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 131-141
    • Raben, N.1    Exelbert, R.2    Spiegel, R.3    Sherman, J.B.4    Nakajima, H.5    Plotz, P.6    Heinisch, J.7
  • 24
    • 0023668313 scopus 로고
    • Site directed mutagenesis in the effector site of Escherichia coli phosphofructokinase
    • Lau F.T.-K., Fersht A.R., Helling H.W., and Evans P.R. Site directed mutagenesis in the effector site of Escherichia coli phosphofructokinase. Biochemistry 26 (1987) 4143-4148
    • (1987) Biochemistry , vol.26 , pp. 4143-4148
    • Lau, F.T.-K.1    Fersht, A.R.2    Helling, H.W.3    Evans, P.R.4
  • 25
    • 19044397060 scopus 로고    scopus 로고
    • The dimorphic yeast Yarrowia lipolytica possesses an atypical phosphofructokinase: characterization of the enzyme and its encoding gene
    • Flores C.-L., Martínez-Costa O.H., Sánchez V., Gancedo C., and Aragón J.J. The dimorphic yeast Yarrowia lipolytica possesses an atypical phosphofructokinase: characterization of the enzyme and its encoding gene. Microbiology 151 (2005) 1465-1474
    • (2005) Microbiology , vol.151 , pp. 1465-1474
    • Flores, C.-L.1    Martínez-Costa, O.H.2    Sánchez, V.3    Gancedo, C.4    Aragón, J.J.5
  • 26
    • 0031020105 scopus 로고    scopus 로고
    • Cloning, sequencing and developmental expression of phosphofructokinase from Dictyostelium discoideum
    • Estévez A.M., Martínez-Costa O.H., Sánchez V., and Aragón J.J. Cloning, sequencing and developmental expression of phosphofructokinase from Dictyostelium discoideum. Eur. J. Biochem. 243 (1997) 442-451
    • (1997) Eur. J. Biochem. , vol.243 , pp. 442-451
    • Estévez, A.M.1    Martínez-Costa, O.H.2    Sánchez, V.3    Aragón, J.J.4
  • 27
    • 0028606474 scopus 로고
    • Purification and properties of phosphofructokinase from Dictyostelium discoideum
    • Martínez-Costa O.H., Estévez A.M., Sánchez V., and Aragón J.J. Purification and properties of phosphofructokinase from Dictyostelium discoideum. Eur. J. Biochem. 226 (1994) 1007-1017
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1007-1017
    • Martínez-Costa, O.H.1    Estévez, A.M.2    Sánchez, V.3    Aragón, J.J.4
  • 28
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0016725502 scopus 로고
    • Interaction of inhibitors with muscle phosphofructokinase
    • Colombo G., Tate P.W., Girotti A.W., and Kemp R.G. Interaction of inhibitors with muscle phosphofructokinase. J. Biol. Chem. 250 (1975) 9404-9412
    • (1975) J. Biol. Chem. , vol.250 , pp. 9404-9412
    • Colombo, G.1    Tate, P.W.2    Girotti, A.W.3    Kemp, R.G.4
  • 31
    • 0013827487 scopus 로고
    • Regulatory mechanisms in carbohydrate metabolism. VII. Hexokinase and phosphofructokinase
    • Uyeda K., and Racker E. Regulatory mechanisms in carbohydrate metabolism. VII. Hexokinase and phosphofructokinase. J. Biol. Chem. 240 (1965) 4682-4688
    • (1965) J. Biol. Chem. , vol.240 , pp. 4682-4688
    • Uyeda, K.1    Racker, E.2


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