메뉴 건너뛰기




Volumn 579, Issue 11, 2005, Pages 2313-2318

Role of Cys-295 on subunit interactions and allosteric regulation of phosphofructokinase-2 from Escherichia coli

Author keywords

Allosteric regulation; Escherichia coli; Phosphofructokinase; SH group; Subunit interaction

Indexed keywords

6 PHOSPHOFRUCTO 2 KINASE; ADENOSINE TRIPHOSPHATE MAGNESIUM; ALANINE; CYSTEINE; OLIGOMER; PHENYLALANINE; TETRAMER;

EID: 17644363680     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.02.078     Document Type: Article
Times cited : (9)

References (18)
  • 1
    • 0024215739 scopus 로고
    • Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
    • Y. Shirakihara, and P. Evans Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products J. Mol. Biol. 204 1988 973 994
    • (1988) J. Mol. Biol. , vol.204 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.2
  • 2
    • 0014413329 scopus 로고
    • Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli
    • D. Blangy, H. Buc, and J. Monod Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli J. Mol. Biol. 31 1968 13 35
    • (1968) J. Mol. Biol. , vol.31 , pp. 13-35
    • Blangy, D.1    Buc, H.2    Monod, J.3
  • 3
    • 0024974796 scopus 로고
    • Crystal structure of unliganded phosphofructokinase from Escherichia coli
    • W.R. Rypniewski, and P.R. Evans Crystal structure of unliganded phosphofructokinase from Escherichia coli J. Mol. Biol. 207 1989 805 821
    • (1989) J. Mol. Biol. , vol.207 , pp. 805-821
    • Rypniewski, W.R.1    Evans, P.R.2
  • 4
    • 0018185175 scopus 로고
    • Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme
    • J. Babul Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme J. Biol. Chem. 253 1978 4350 4355
    • (1978) J. Biol. Chem. , vol.253 , pp. 4350-4355
    • Babul, J.1
  • 5
    • 0025189804 scopus 로고
    • Structural basis of the allosteric behaviour of phosphofructokinase
    • T. Schirmer, and P.R. Evans Structural basis of the allosteric behaviour of phosphofructokinase Nature 343 1990 140 145
    • (1990) Nature , vol.343 , pp. 140-145
    • Schirmer, T.1    Evans, P.R.2
  • 6
    • 0028787961 scopus 로고
    • Tetramer-dimer equilibrium of phosphofructokinase and formation of hybrid tetramers
    • G. Le Bras, I. Auzat, and J.R. Garel Tetramer-dimer equilibrium of phosphofructokinase and formation of hybrid tetramers Biochemistry 34 1995 13203 13210
    • (1995) Biochemistry , vol.34 , pp. 13203-13210
    • Le Bras, G.1    Auzat, I.2    Garel, J.R.3
  • 7
    • 0028956133 scopus 로고
    • Hypercooperativity induced by interface mutations in the phosphofructokinase from Escherichia coli
    • I. Auzat, G. Le Bras, and J.R. Garel Hypercooperativity induced by interface mutations in the phosphofructokinase from Escherichia coli J. Mol. Biol. 246 1995 248 253
    • (1995) J. Mol. Biol. , vol.246 , pp. 248-253
    • Auzat, I.1    Le Bras, G.2    Garel, J.R.3
  • 8
    • 0022226641 scopus 로고
    • Effect of ATP on phosphofructokinase-2 from Escherichia coli. A mutant enzyme altered in the allosteric site for MgATP
    • V. Guixé, and J. Babul Effect of ATP on phosphofructokinase-2 from Escherichia coli. A mutant enzyme altered in the allosteric site for MgATP J. Biol. Chem. 260 1985 11001 11005
    • (1985) J. Biol. Chem. , vol.260 , pp. 11001-11005
    • Guixé, V.1    Babul, J.2
  • 10
    • 0023742763 scopus 로고
    • Influence of ligands on the aggregation of the normal and mutant forms of phosphofructokinase 2 of Escherichia coli
    • V. Guixé, and J. Babul Influence of ligands on the aggregation of the normal and mutant forms of phosphofructokinase 2 of Escherichia coli Arch. Biochem. Biophys. 264 1988 519 524
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 519-524
    • Guixé, V.1    Babul, J.2
  • 11
    • 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
    • V. Guixé 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 2000 313 319
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 313-319
    • Guixé, V.1
  • 12
    • 0344825224 scopus 로고    scopus 로고
    • Structural and functional roles of cysteines 238 and 295 in Escherichia coli phosphofructokinase-2
    • M. Báez, P.H. Rodríguez, J. Babul, and V. Guixé Structural and functional roles of cysteines 238 and 295 in Escherichia coli phosphofructokinase-2 Biochem. J. 376 2003 277 283
    • (2003) Biochem. J. , vol.376 , pp. 277-283
    • Báez, M.1    Rodríguez, P.H.2    Babul, J.3    Guixé, V.4
  • 13
    • 0020964799 scopus 로고
    • Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme
    • F. Daldal Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme J. Mol. Biol. 168 1983 285 305
    • (1983) J. Mol. Biol. , vol.168 , pp. 285-305
    • Daldal, F.1
  • 14
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • S. Tabor, and C.C. Richardson A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes Proc. Nat. Acad. Sci. USA 82 1985 1074 1078
    • (1985) Proc. Nat. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 15
    • 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 modelling
    • R. Cabrera, H. Fischer, S. Trapani, A.F. Craievich, R.C. Garrat, V. Guixé, and J. Babul Domain motions and quaternary packing of phosphofructokinase-2 from Escherichia coli studied by Small Angle X-ray Scattering and homology modelling J. Biol. Chem. 278 2003 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
  • 16
    • 0037177207 scopus 로고    scopus 로고
    • Mutational analysis of the subunit interface of Vibrio harveyi bacterial luciferase
    • J.K. Inlow, and T.O. Baldwin Mutational analysis of the subunit interface of Vibrio harveyi bacterial luciferase Biochemistry 41 2002 3906 3915
    • (2002) Biochemistry , vol.41 , pp. 3906-3915
    • Inlow, J.K.1    Baldwin, T.O.2
  • 17
    • 0030690267 scopus 로고    scopus 로고
    • A mutant phosphofructokinase produces a futile cycle during gluconeogenesis in Escherichia coli
    • J.C. Torres, V. Guixé, and J. Babul A mutant phosphofructokinase produces a futile cycle during gluconeogenesis in Escherichia coli Biochem. J. 327 1997 675 684
    • (1997) Biochem. J. , vol.327 , pp. 675-684
    • Torres, J.C.1    Guixé, V.2    Babul, J.3
  • 18
    • 1642286478 scopus 로고    scopus 로고
    • Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium
    • M.A. Vargo, L. Nguyen, and R. Colman Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium Biochemistry 43 2004 3327 3335
    • (2004) Biochemistry , vol.43 , pp. 3327-3335
    • Vargo, M.A.1    Nguyen, L.2    Colman, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.