Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity

Biochemical Journal

Volumn 337, Issue 3, 1999, Pages 503-506

  Batista, Frank R ^a   Hernández, Lázaro ^a   Fernández, Julio R ^a   Arrieta, Juan ^a   Menéndez, Carmen ^a   Gómez, Raúl ^a   Támbara, Yanet ^a   Pons, Tirso ^a  

^a CENTER FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Cuba)

Author keywords

fructofuranosidase; Enzyme activity; Fructosyltransferase; LsdA; Site directed mutagenesis

Indexed keywords

ASPARAGINE; ASPARTIC ACID; BACTERIAL ENZYME; LEVANSUCRASE; SUCROSE;

ACETOBACTER; ACETOBACTER DIAZOTROPHICUS; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME SPECIFICITY; HYDROLYSIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ACETOBACTER; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CONSERVED SEQUENCE; HEXOSYLTRANSFERASES; HYDROLYSIS; MUTAGENESIS, SITE-DIRECTED; SUCROSE;

ACETOBACTER; BACTERIA (MICROORGANISMS); FELIS CATUS; GLUCONACETOBACTER DIAZOTROPHICUS;

EID: 0039848317     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3370503     Document Type: Article

References (20)

1. Hernàndez, L, Arrieta, J., Menéndez, C., Vázquez, R., Coego, A., Suárez, V., Selman, G., Petit-Glatron, M. F. and Chambert, R. (1995) Biochem. J. 309, 113-118
2. Henikoff, S. and Henikoff, J. G. (1991) Nucleic Acids Res. 19, 6565-6572
3. Sprenger, N., Bortlik, K., Brandt, A., Boller, T. and Wiemken, A. (1995) Proc Natl. Acad. Sci. U.S.A. 92, 11652-11656
4. Chávez, F. P., Pons, T., Delgado, J. M. and Rodriguez, L. (1998) Yeast 14, 1223-1232
5. Huynh, T. V., Young, R. A. and Davis, R. W. (1985) in DNA Cloning (Glover, D. M., ed.), vol. 1, pp. 56-110, IRL Press, Oxford
6. Gough, J. and Murray, N. (1983) J. Mol. Biol. 166, 1-19
7. Simon, R., Priefer, U. and Pühler, A. (1983) in Molecular Genetics of the Bacteria - Plant Interaction (Pühler, A., ed.), pp. 98-106, Springer-Verlag, Berlin
8. Coego, A., Ramírez, R., Menéndez, C., Arrieta. J., Hernández, L., Suárez, V., Selman, G. and Pérez, S. (1992) Rev. Latinoam. Microbiol. 34, 189-195
9. Arrieta, J., Hernández, L. Coego, A., Suárez, V., Balmori, E., Menéndez, C., Petit-Glatron, M. F., Chambert, R. and Selman-Housein, G. (1996) Microbiology 142, 1077-1085
10. Ditta, G., Schmidhauser, T., Yakobson, E., Lu, P., Liang, X. W., Finlay, D. R., Guiney, D. and Helinski, D. R. (1985) Plasmid 13, 149-153
11. Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D. J. (1997) Nucleic Acids Res. 25, 3389-3402
12. Gribskov, M., McLachlan, A. D. and Eisenberg, D. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 4355-4358
13. Thompson, J. D., Higgins. D. G. and Gibson, T. J. (1994) Nucleic Acids Res. 22, 4673-4680
14. Sanger, F., Nicklen, S. and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467
15. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254
16. Laemmli, U.K. (1970) Nature (London) 227, 680-685
17. Davies, G. and Henrissat, B. (1995) Structure 15, 853-859
18. Cornish-Bowden, A. (1995) in Analysis of Enzyme Kinetic Data (Cornish-Bowden, A., ed.), pp. 3-192, Oxford University Press, Oxford
19. Reddy, A. and Maley, F. (1990) J. Biol. Chem. 265, 10817-10820
20. Reddy, A. and Maley, F. (1996) J. Biol. Chem. 271, 13953-13958