메뉴 건너뛰기




Volumn 328, Issue 6 SPEC. ISS., 2005, Pages 549-556

The structure of E. coli β-galactosidase

Author keywords

Allolactose; Lactose; Tetramer; complementation; galactosidase

Indexed keywords

BETA GALACTOSIDASE;

EID: 20444373710     PISSN: 16310691     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.crvi.2005.03.006     Document Type: Short Survey
Times cited : (144)

References (22)
  • 1
    • 0028178377 scopus 로고
    • Three-dimensional structure of β-galactosidase from E. coli
    • R.H. Jacobson X.-J. Zhang R.F. DuBose B.W. Matthews Three-dimensional structure of β-galactosidase from E. coli Nature 369 1994 761-766
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.-J.2    DuBose, R.F.3    Matthews, B.W.4
  • 2
    • 0033820067 scopus 로고    scopus 로고
    • High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for α-complementation
    • D.H. Juers R.H. Jacobson D. Wigley X.-J. Zhang R.E. Huber D.E. Tronrud B.W. Matthews High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for α-complementation Protein Sci. 9 2000 1685-1699
    • (2000) Protein Sci. , vol.9 , pp. 1685-1699
    • Juers, D.H.1    Jacobson, R.H.2    Wigley, D.3    Zhang, X.-J.4    Huber, R.E.5    Tronrud, D.E.6    Matthews, B.W.7
  • 3
    • 0017875606 scopus 로고
    • Amino acid sequence of β-galactosidase
    • A. Fowler I. Zabin Amino acid sequence of β-galactosidase J. Biol. Chem. 253 1978 5521-5525
    • (1978) J. Biol. Chem. , vol.253 , pp. 5521-5525
    • Fowler, A.1    Zabin, I.2
  • 5
    • 77956902300 scopus 로고
    • β-Galactosidase
    • third ed. Academic Press London
    • K. Wallenfels R. Weil β-Galactosidase third ed. The Enzymes vol. 7 1972 Academic Press London 617-663
    • (1972) The Enzymes , vol.7 , pp. 617-663
    • Wallenfels, K.1    Weil, R.2
  • 6
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • D.E. Koshland Jr. Stereochemistry and the mechanism of enzymatic reactions Biol. Rev. 28 1953 416-436
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland Jr., D.E.1
  • 7
    • 0015505491 scopus 로고
    • A common intermediate in the hydrolysis of β-galactosides by β-galactosidase from Escherichia coli
    • T.M. Stokes I.B. Wilson A common intermediate in the hydrolysis of β-galactosides by β-galactosidase from Escherichia coli Biochemistry 11 1972 1061-1064
    • (1972) Biochemistry , vol.11 , pp. 1061-1064
    • Stokes, T.M.1    Wilson, I.B.2
  • 9
    • 0028178438 scopus 로고
    • Substitutions for Glu-537 of β-galactosidase from Escherichia coli cause large decreases in catalytic activity
    • J. Yuan M. Martinez-Bilbao R.E. Huber Substitutions for Glu-537 of β-galactosidase from Escherichia coli cause large decreases in catalytic activity Biochem. J. 299 1994 527-531
    • (1994) Biochem. J. , vol.299 , pp. 527-531
    • Yuan, J.1    Martinez-Bilbao, M.2    Huber, R.E.3
  • 10
    • 0026666602 scopus 로고
    • Binding energy and catalysis. Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lacZ) β-galactosidase
    • J.D. McCarter M.J. Adam S.G. Withers Binding energy and catalysis. Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lacZ) β-galactosidase Biochem. J. 286 1992 721-727
    • (1992) Biochem. J. , vol.286 , pp. 721-727
    • McCarter, J.D.1    Adam, M.J.2    Withers, S.G.3
  • 11
    • 0023132247 scopus 로고
    • Strong inhibitory effect of furanoses and sugar lactones on β-galactosidase of Escherichia coli
    • R.E. Huber R.L. Brockbank Strong inhibitory effect of furanoses and sugar lactones on β-galactosidase of Escherichia coli Biochemistry 26 1987 1526-1531
    • (1987) Biochemistry , vol.26 , pp. 1526-1531
    • Huber, R.E.1    Brockbank, R.L.2
  • 12
    • 0029095922 scopus 로고
    • Synthesis of galactose- and N-acetylglucosamine-derived tetrazoles and their evaluation as β-glycosidase inhibitors
    • T.D. Heightman P. Ermert D. Klein A. Vasella Synthesis of galactose- and N-acetylglucosamine-derived tetrazoles and their evaluation as β-glycosidase inhibitors Helv. Chim. Acta 78 1995 514-532
    • (1995) Helv. Chim. Acta , vol.78 , pp. 514-532
    • Heightman, T.D.1    Ermert, P.2    Klein, D.3    Vasella, A.4
  • 13
    • 0018137643 scopus 로고
    • Ions, ion-pairs and catalysis by the lacZ β-galactosidase of Escherichia coli
    • M.L. Sinnott Ions, ion-pairs and catalysis by the lacZ β-galactosidase of Escherichia coli FEBS Lett. 94 1978 1-9
    • (1978) FEBS Lett. , vol.94 , pp. 1-9
    • Sinnott, M.L.1
  • 14
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • M.L. Sinnott Catalytic mechanisms of enzymic glycosyl transfer Chem. Rev. 90 1990 1171-1202
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 16
    • 0016332320 scopus 로고
    • Lac repressor can be fused to β-galactosidase
    • B. Müller-Hill J. Kania Lac repressor can be fused to β-galactosidase Nature 249 1974 561-563
    • (1974) Nature , vol.249 , pp. 561-563
    • Müller-Hill, B.1    Kania, J.2
  • 17
    • 0020975429 scopus 로고
    • Chimeric genetics with β-galactosidase
    • T.S. Papas M. Rosenberg C. Chirikjian (Eds.) Elsevier New York
    • G.M. Weinstock M.L. Berman T.J. Silhavy Chimeric genetics with β-galactosidase in: T.S. Papas M. Rosenberg C. Chirikjian (Eds.) Gene Amplification and Analysis vol. 3 1982 Elsevier New York 27-64
    • (1982) Gene Amplification and Analysis , vol.3 , pp. 27-64
    • Weinstock, G.M.1    Berman, M.L.2    Silhavy, T.J.3
  • 18
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat A. Bairoch New families in the classification of glycosyl hydrolases based on amino acid sequence similarities Biochem. J. 293 1993 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 19
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • B. Henrissat G. Davies Structural and sequence-based classification of glycoside hydrolases Curr. Opin. Struct. Biol. 7 1997 637-644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 20
    • 20444416865 scopus 로고    scopus 로고
    • This is a website describing various characteristics of the glycosyl hydrolase families
    • A. Bairoch http://www.expasy.ch/cgi-bin/lists?glycosid.txt This is a website describing various characteristics of the glycosyl hydrolase families (1997)
    • (1997)
    • Bairoch, A.1
  • 21
    • 0032923813 scopus 로고    scopus 로고
    • Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between β-galactosidase and other glycohydrolases
    • D.H. Juers R.E. Huber B.W. Matthews Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between β-galactosidase and other glycohydrolases Protein Sci. 8 1999 122-136
    • (1999) Protein Sci. , vol.8 , pp. 122-136
    • Juers, D.H.1    Huber, R.E.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.