메뉴 건너뛰기




Volumn 10, Issue 7, 1996, Pages 799-801

Functional interaction of hexokinase with ATP requires participation by both small and large lobes of the enzyme: Implications for other proteins using the actin fold as a nucleotide binding motif

Author keywords

ATP binding; binding of ATP; hexokinase

Indexed keywords

ACTIN; ADENINE; ADENOSINE TRIPHOSPHATE; GLUCOSE; HEXOKINASE;

EID: 0029894209     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.7.8635698     Document Type: Article
Times cited : (16)

References (17)
  • 2
    • 0025923850 scopus 로고
    • 18O isotope effects for hexokinase-catalyzed phosphoryl transfer from ATP
    • 18O isotope effects for hexokinase-catalyzed phosphoryl transfer from ATP. Biochemistry 30, 3634-3639
    • (1991) Biochemistry , vol.30 , pp. 3634-3639
    • Jones, J.P.1    Weiss, P.M.2    Cleland, W.W.3
  • 3
    • 0021104723 scopus 로고
    • Solvent isotope effects on the reaction catalyzed by yeast hexokinase
    • Taylor, K. B., Cook, P. F., and Cleland, W. W. (1983) Solvent isotope effects on the reaction catalyzed by yeast hexokinase. Eur. J. Biochem. 134, 571-574
    • (1983) Eur. J. Biochem. , vol.134 , pp. 571-574
    • Taylor, K.B.1    Cook, P.F.2    Cleland, W.W.3
  • 6
    • 0018802524 scopus 로고
    • Space-filling models of kinase clefts and conformation changes
    • Anderson, C. M., Zucker, F. H., and Steitz, T. A. (1979) Space-filling models of kinase clefts and conformation changes. Science 204, 375-380
    • (1979) Science , vol.204 , pp. 375-380
    • Anderson, C.M.1    Zucker, F.H.2    Steitz, T.A.3
  • 7
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A. M., and Chothia, C. (1994) Structural mechanisms for domain movements in proteins. Biochemistry 33, 6739-6749
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 8
    • 0019325449 scopus 로고
    • Crystallographic studies and model building of ATP at the active site of hexokinase
    • Shoham, M., and Steitz, T. A. (1980) Crystallographic studies and model building of ATP at the active site of hexokinase. J. Mol. Biol. 140, 1-14
    • (1980) J. Mol. Biol. , vol.140 , pp. 1-14
    • Shoham, M.1    Steitz, T.A.2
  • 10
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K. M., DeLuca-Flaherty, C., and McKay, D. B. (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature (London) 346, 623-628
    • (1990) Nature (London) , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 11
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty, K. M., McKay, D. B., Kabsch, W., and Holmes, K. C. (1991) Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl. Acad. Sci. USA 88, 5041-5045
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 12
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, A. (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. USA 89, 7290-7294
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 13
    • 0028944687 scopus 로고
    • The actin fold
    • Kabsch, W., and Holmes, K. C. (1995) The actin fold. FASEB J. 9, 167-174
    • (1995) FASEB J. , vol.9 , pp. 167-174
    • Kabsch, W.1    Holmes, K.C.2
  • 14
    • 0021978310 scopus 로고
    • The role of the α-helix dipole in protein function and structure
    • Hol, W. G. J. (1985) The role of the α-helix dipole in protein function and structure. Prog. Biophys. Mol. Biol. 45, 149-195
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.J.1
  • 15
    • 0023854041 scopus 로고
    • The complete amino acid sequence of the catalytic domain of rat brain hexokinase, deduced from the cloned cDNA
    • Schwab, D. A., and Wilson, J. E. (1988) The complete amino acid sequence of the catalytic domain of rat brain hexokinase, deduced from the cloned cDNA. J. Biol. Chem. 263, 3220-3224
    • (1988) J. Biol. Chem. , vol.263 , pp. 3220-3224
    • Schwab, D.A.1    Wilson, J.E.2
  • 16
    • 0024605390 scopus 로고
    • Complete amino acid sequence of rat brain hexokinase, deduced from the cloned cDNA, and proposed structure of a mammalian hexokinase
    • Schwab, D. A., and Wilson, J. E. (1989) Complete amino acid sequence of rat brain hexokinase, deduced from the cloned cDNA, and proposed structure of a mammalian hexokinase. Proc. Natl. Acad. Sci. USA 86, 2563-2567
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2563-2567
    • Schwab, D.A.1    Wilson, J.E.2
  • 17
    • 0025231712 scopus 로고
    • Glucose phosphorylation. Interaction of a 50-amino acid peptide of yeast hexokinase with trinitrophenyl ATP
    • Arora, K. K., Shenbagamurthi, P., Fanciulli, M., and Pedersen, P. L. (1990) Glucose phosphorylation. Interaction of a 50-amino acid peptide of yeast hexokinase with trinitrophenyl ATP. J. Biol. Chem. 265, 5324-5328
    • (1990) J. Biol. Chem. , vol.265 , pp. 5324-5328
    • Arora, K.K.1    Shenbagamurthi, P.2    Fanciulli, M.3    Pedersen, P.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.