A study of the relationships of interactions between Asp-201, Na + or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of β-galactosidase

Biochemistry and Cell Biology

Volumn 82, Issue 2, 2004, Pages 275-284

  Xu, Julia ^a   McRae, Mary A A ^a   Harron, Scott ^a   Rob, Beatrice ^a   Huber, Reuben E ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

galactosidase; Aspartic acid; Binding; Potassium; Sodium

Indexed keywords

CATALYSIS; CHEMICAL ACTIVATION; ENZYMES; HYDROPHOBICITY; POTASSIUM; SODIUM;

INHIBITORS; REACTIVITY; TRANSITION STATES;

BIOCHEMISTRY;

ASPARTIC ACID; BETA GALACTOSIDASE; GALACTOSE; HYDROXYL GROUP; POTASSIUM ION; SODIUM ION;

ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL MODIFICATION; ENTHALPY; HYDROPHOBICITY; NONHUMAN; PHYSICAL CHEMISTRY; PROTEIN BINDING; PROTEIN INTERACTION; SUBSTITUTION REACTION;

ASPARTIC ACID; BETA-GALACTOSIDASE; BINDING SITES; ESCHERICHIA COLI; KINETICS; MUTAGENESIS; PLASMIDS; POTASSIUM; PROTEIN BINDING; SODIUM; THERMODYNAMICS;

ARRHENIUS;

EID: 2542505756     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o04-004     Document Type: Article

References (28)

1. Ayala, Y.M., and Di Cera, E. 2000. A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases. Prot. Sci. 9: 1589-1593.
2. Buvinger, W.E., and Riley, M. 1985. Nucleotide sequence of Klebsiella pneumoniae lac genes. J. Bacteriol. 163: 850-857.
3. Case, G.S., and Sinnott, M.L. 1972. The role of magnesium ions in β-galactosidase-catalysed hydrolyses. Biochem. Biophys. Acta, 35: 122-29.
4. David, S., Steves, H., van Riel, M., Simons, G., and ve Vos, W. 1992. Leuconostoc lactis β-galactosidase is encoded by overlapping genes. J. Bacteriol. 174: 4475-4481.
5. Davies, G., and Henrissat, B. 1995. Structures and mechanisms of glycosyl hydrolases. Structure, 3: 853-859.
6. Deschavanne, P.J., Viratelle, O.M., and Yon, J.M. 1978. Conformational adaptability of the active site of β-galactosidase. J. Biol. Chem. 253: 833-37.
7. Edwards, R.A., and Huber, R.E. 1991. Surface denaturation of proteins: the thermal inactivation of β-galactosidase (Escherichia coli) on wall-liquid surfaces. Biochem. Cell Biol. 70: 63-69.
8. Fowler, A.V., and Zabin, I. 1978. Amino acid sequence of β-galactosidase. J. Biol. Chem. 253: 5505-09.
9. Glusker, J.P. 1991. Structural aspects of metal binding to functional groups in proteins. In Advances in protein chemistry. Vol. 42. Edited by C.B. Anfinson, J.T. Edsall, F.M. Richards, and D.S. Eisenberg. Academic Press, New York, N.Y. pp. 1-76.
10. Hancock, K.R., Rockman, E., Yong, C.A., Pearce, L., Maddox, I.S., and Scott, D.B. 1991. Expression and nucleotide sequence of the Clostridium acetobtylicum β-galactosidase gene cloned in Escherichia coli. J. Bacteriol. 173: 3084-3095.
11. Hanzlik, R.P. 1976. Inorganic chemistry of group Ia and IIa metals. In Inorganic aspects of biological and organic chemistry. Academic Press, New York, N.Y. pp. 14-44.
12. Huber, R.E., and Gaunt, M.T. 1983. Importance of hydroxyls at positions 3, 4, and 6 for binding to the "galactose" site of β-galactosidase (Escherichia coli). Arch. Biochem. Biophys. 220: 263-271.
13. Huber, R.E., Gaunt, M.T., and Hurlburt, K.L. 1984. Binding and reactivity at the "glucose" subsite of galactosyl-β-galactosidase (Escherichia coli). Arch. Biochem. Biophys. 234: 151-160.
14. Jacobson, R.H., Zhang, X.-J., DuBose, R.F., and Matthews, B.W. 1994. Three-dimensional structure of β-galactosidase from E. coli. Nature (London), 369: 761-766.
15. Juers, D.H., Jacobson, R.H., Wigley, D., Zhang, X.-J., Huber, R.E., Tronrud, D.E., and Matthews, B.W. 2000. High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for ∂-complementation. Prot. Sci. 9: 1685-1699.
16. Juers, D.H., Heightman, T.D., Vasella, A., McCarter, J.D., Mackenzie, L., Withers, S.G., and Matthews, B.W. 2001. A structural view of the action of Escherichia coli (lacZ) β-galactosidase. Biochemistry, 40: 14 781-14 794.
17. Kalnins, A., Otto, K., Ruther, U., and Muller-Hill, B. 1983. Sequence of the lacZ gene of E. coli. EMBO J. 2: 593-597.
18. McCarter, J.D., Adam, M.J., and Withers, S.G. 1992. Binding energy and catalysis. Biochem. J. 286: 721-727.
19. Mesecar, A.D., Stoddard, B.L., and Koshland, D.E. Jr. 1997. Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences. Science (Washington, D.C.), 277: 202-206.
20. Nagano, H., Kawaguchi, T., Omori, M., Shoji, Z., and Arai, M. 1994. Molecular cloning and nucleotide sequence of the beta-galactosidase gene from Enterobacter cloacae GAO. Biosci. Biotechnol. Biochem. 58: 1866-1899.
21. +. Arch. Biochem. Biophys. 118: 596-610.
22. Obst, M., Meding, E.R., Vogel, R.F., and Hammes, W.P. 1995. Two genes encoding the beta-galactosidase of Lactobacillus sake. Microbiology (Reading, U.K.), 141: 3059-3066.
23. Poch, O., L'Hote, H., Dallery, V., Debeaux, F., Fleer, R., and Sodoyer, R. 1992. Sequence of the Kluyveromyces lactis β-galactosidase: comparison with prokaryotic enzymes and secondary structure analysis. Gene, 118: 55-63.
24. Sambrook, J., Fritsch, E.F., and Maniatis, T. 1988. Molecular Cloning. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
25. Schmidt, B.F., Adams, R.M., Requadt, C., Power, S., and Mainzer, S.E. 1989. Expression and nucleotide sequence of the Lactobacillus bulgaris β-galactosidase gene cloned in Escherichia coli. J. Bacteriol. 171: 625-635.
26. Schroeder, C.J., Robert, C., Lenzen, G., McKay, L.L., and Mercenier, A. 1991. Analysis of the Lac Z sequences from two Streptococcus thermophilus strains: omparisons with the Escherichia coli and Lactobacillus bulgaricus β-galactosidase sequences. J. Gen. Microbiol. 137: 369-380.
27. Vallee, B.L., and Wacker, W.E.C. 1970. Properties of metal-ligand complexes. In The proteins. Vol. 5. Edited by H. Neurath. Academic Press, New York, N.Y. pp. 5-24.
28. Wallenfels, K., and Weil, R. 1972. β-Galactosidase. In The enzymes. Vol. VII. Edited by P.D. Boyer. Academic Press, New York, N.Y. pp. 617-663.