Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine

Journal of Biological Chemistry

Volumn 273, Issue 11, 1998, Pages 6096-6103

  Recksiek, Michael ^a   Selmer, Thorsten ^a   Dierks, Thomas ^a   Schmidt, Bernhard ^a   Von Figura, Kurt ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; ARYLSULFATASE; PHOSPHOSERINE; SULFATASE;

ALKALINITY; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HYDROLYSIS; PH; PRIORITY JOURNAL; PROTEIN PROCESSING;

ALKALINE PHOSPHATASE; BINDING SITES; CATECHOLS; CEREBROSIDE-SULFATASE; CHONDRO-4-SULFATASE; GALACTOSE; GLYCINE; HUMANS; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; SERINE; SULFURIC ACID ESTERS;

EID: 0032513051     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.11.6096     Document Type: Article

References (29)

1. Franco, B., Meroni, G., Parenti, G., Levilliers, J., Bernard, L., Gebbia, M., Cox, L., Maroteaux, P., Sheffield, L., Rappold, G. A., Andria, G., Petit, C., and Ballabio, A. (1995) Cell 81, 15-25
2. Parenti, G., Meroni, G., and Ballabio, A. (1997) Curr. Opin. Gen. Dev. 7, 386-391
3. Schmidt, B., Selmer, T., Ingendoh, A., and von Figura, K. (1995) Cell 82, 271-278
4. Selmer, T., Hallmann, A., Schmidt, B., Sumper, M., and von Figura, K. (1996) Eur. J. Biochem. 238, 341-345
5. Bond, C. S., Clements, P. R., Ashby, S. J., Collyer, C. A., Harrop, S. J., Hopwood, J. J., and Guss, J. M. (1997) Structure 5, 277-289
6. Lukatela, G., Krauß, N., Theis, K., Selmer, T., Gieselmann, V., von Figura, K., and Saenger, W. (1998) Biochemistry, in press
7. Dierks, T., Schmidt, B., and von Figura, K. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 11963-11968
8. Sowadski, J. M., Handschumacher, M. D., Murthy, H. M. K., Foster, B. A., and Wyckoff, H. W. (1985) J. Mol. Biol. 186, 417-433
9. Kim, E. E., and Wyckoff, H. W. (1991) J. Mol. Biol. 218, 449-464
10. Coleman, J. E. (1992) Annu. Rev. Biophys. Biomol. Struct. 21, 441-483
11. Prosser, C. I., and Roy, A. B. (1980) Biochim. Biophys. Acta 613, 130-139
12. Stein, C., Gieselmann V., Kreysing, J., Schmidt, B., Pohlmann, R., Waheed, A., Meyer, H. E., O'Brien, J. S., and von Figura, K. (1989) J. Biol. Chem. 264, 1252-1259
13. Peters, C., Schmidt, B., Rommerskirch, W., Rupp, K., Zühlsdorf, M., Vingron, M., Meyer H., Pohlmann, R., and von Figura, K. (1990) J. Biol. Chem. 265, 3374-3381
14. Artelt, P., Morelle, C., Ausmeier, M., Fitzek, M., and Hauser, H. (1988) Gene (Amst.) 68, 213-219
15. Kasper, D., Dittmer, F., von Figura, K., and Pohlmann, R. (1996) J. Cell. Biol. 134, 615-623
16. Sommerlade, H. J., Selmer, T., Ingendoh, A., Gieselmann, V., von Figura, K., Neifer, K., and Schmidt, B. (1994) J. Biol. Chem. 269, 20977-20981
17. Gibson, G. J., Saccone, G. T. P., Brooks, A., Clements, P. R., and Hopwood, J. J. (1987) Biochem. J. 248, 755-764
18. Laemmli, U. K. (1970) Nature 227, 680-685
19. Dierks, T., Volkmer, J., Schlenstedt, G., Jung, C., Sandholzer, U., Zachmann, K., Schlotterhose, F., Neifer, K., Schmidt, B., and Zimmermann, R. (1996) EMBO J. 15, 6931-6942
20. Partrigde, S. M. (1949) Nature 164, 433
21. Seiler, H., and Erlenmeyer, H. (1964) Helv. Clin. Acta 47, 264
22. Roy, A. B. (1953) Biochem. J. 55, 653-661
23. Lee, G. D., and van Etten, R. L. (1975) Arch. Biochem. Biophys. 166, 280-294
24. Jerfy, A., and Roy, A. B. (1973) Biochim. Biophys. Acta 293, 178-190
25. Brooks, D. A., Robertson, D. A., Bindloss, C., Litjens, T., Anson, D. S., Peters, C., Morris, C. P., and Hopwood, J. J. (1995) Biochem. J. 307, 457-463
26. Gettins, P., Metzler, M., and Coleman, J. E. (1985) J. Biol. Chem. 260, 2875-2883
27. Ried, T. W., and Wilson, I. B. (1971) Enzymes 4, 373-415
28. Mehl, E., and Jatzkewitz, H. (1968) Biochim. Biophys. Acta 151, 619-627
29. Hopwood, J. J., Elliott, H., Muller, V. J., and Saccone, G. T. P. (1986) Biochem. J. 234, 507-514