Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis

Biochemistry

Volumn 37, Issue 11, 1998, Pages 3654-3664

  Lukatela, G ^a,b   Krauss, N ^a   Theis, K ^a   Selmer, T ^b   Gieseimann, V ^b,c   Von Figura, K ^b   Saenger, W ^a  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c UNIVERSITY OF KIEL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE; ALKALINE PHOSPHATASE; CEREBROSIDE SULFATASE; HYDROLASE; LYSOSOME ENZYME; METAL ION; SULFATE;

ANIMAL CELL; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME MODIFICATION; ESTERIFICATION; HAMSTER; HUMAN; HYDROLYSIS; MULTIPLE SULFATASE DEFICIENCY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING;

ALDEHYDES; ALKALINE PHOSPHATASE; BINDING SITES; CEREBROSIDE-SULFATASE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MAGNESIUM; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SULFURIC ACID ESTERS;

ANIMALIA; CRICETINAE;

EID: 0032539976     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9714924     Document Type: Article

References (45)

1. Baker, A. D., & Engel, R. (1992) Organic Chemistry, p 81, West Publishing Co., St. Paul, MM.
2. Ballabio, A., & Shapiro, L. J. (1995) Steroid sulfatase deficiency and X-linked ichthyosis, in The metabolic and molecular bases of inherited disease (Scriver, C. R., Beaudet, A. L., and Sly, W. S., Eds.) pp 2999-3022, McGraw-Hill, New York.
3. Bell, R. P., & Onwood, D. N. (1962) Trans. Faraday Soc: 58, 1557-1561.
4. Bond, C. S., Clements, P. R., & Ashby, S. R. (1997) Structure 5, 277-289.
5. Brünger, A. T. (1992) X-PLOR Version 3.1, Yale University Press, New Haven and London.
6. CCP4 (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D50, 760-763.
7. Chao, H. H. J., Waheed, A., & Pohlmann, R (1990) EMBO J. 9, 3507-3513.
8. Coleman, J. E. (1992) Structure 21, 441-483.
9. Evans, S. V. (1993) SETOR: Hardware lighted three-dimensional solid model representation of macromolecules, J. Mol. Graphics 11, 134-138.
10. Franco, B., Meroni, G., & Parenti, G. (1995) Cell 81, 15-25.
11. Fujii, T., Kobayashi, T., & Honke, K (1992) Biochim. Biophys. Acta 1122, 93-98.
12. Holm, L., & Sander, L. (1993) DALI version 2.0, J. Mol. Biol. 233, 123-138.
13. Jeffrey, G. A., & Saenger, W. (1991) Hydrogen Bonding in Biological Structures, Springer Verlag, Heidelberg and New York.
14. Jones, T. A., Zou, J.-Y., & Cowan, S. W. (1991) Acta Crystallogr. A47, 110-119.
15. Kim, E. E., & Wyckoff, H. W. (1991) J. Mol. Biol. 218, 449-464.
16. Kolodny, E. H., & Fluharty, A. L. (1995) Metachromatic leukodystrophy and multiple sulfatase deficiency: sulfatide lipidosis, in The metabolic and molecular bases of inherited disease (Senver, C. R., Beaudet, A. L., & Sly, W. S., Eds.) pp 2693-2741, McGraw-Hill, New York.
17. Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
18. Lee, G. D., & van Etten, R. L. (1975) Arch. Biochem. Biophys. 166, 280-294.
19. Marker, A., & Roy, A. B. (1983) Biochim. Biophys. Acta 742, 446-451.
20. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497
21. McEwen, W. K. (1936) J. Am. Chem. Soc. 58, 1124-1129.
22. McPherson, A., Koszelak, S., & Axelrod, H (1986) J. Crystal Growth 76, 547-553.
23. Messerschmidt, A., & Pflugrath, J. W. (1987) J. Appl. Crystallogr. 20, 306-315.
24. Neufeld, E. F., & Muenzer, J. (1995) The mucopolysaccharidoses, in The metabolic and molecular bases of interited disease (Scriver, C. R., Beaudet, A. L., Sly, W. S., & Valle, D. Eds.) pp 2645-2694, McGraw-Hill, New York.
25. Nichol, L. W., & Roy, A. B. (1966) Biochemistry 5, 1379-1388.
26. Nicholls, A. (1992) GRASP, Columbia University, 630 Westth St New York, NY 10032.
27. Nicholls, R. C., & Roy, A. B. (1971) Arylsulfatases, in The Enzymes, 3rd Ed., Vol. 5, pp 21-41, Academic Press, New York.
28. Nicolaides, A., & Radom, L. (1995) J. Chem. Soc., Chem. Commun., 701-702.
29. Otwinowski, Z. (1993) Oscillation Data Reduction Program, in Proceedings of the CCP4 Study Weekend: "Data Collection and Proceeding" (Sawyer, L., Isaacs, N., & Bailey, S., Eds.) pp 56-62, SERC Laboratory, Daresbury.
30. Presser, C. I., & Roy, A. B. (1980) Biochim. Biophys. Acta 613 130-139.
31. Roy, A. B. (1976) J. Exp. Biol. Med. Sci. 54, 111-135.
32. Schmidt, B., Seimer, T., & Ingendoh, A.(1995) Cell 82, 271-278.
33. Seimer, T., Hallmann, A., & Schmidt, B. (1996) Eur. J. Biochem. 238, 341-345.
34. Sommerlade, H.-J., Seimer, T., & Ingendoh, A. (1994) J. Biol Chem. 269, 20977-20981.
35. Sowadski, J. M., Handschumacher, M. D., & Krishna Murthy, H. M. (1985) J. Mol. Biol. 186, 417-433.
36. Spencer, B. (1958) Biochem. J. 69, 155-159.
37. Spencer, B. (1962) Biochem. J. 73, 442-447.
38. Stein, C, Hille, A., & Seidel, J. (1989) J. Biol. Chem. 264, 13865-13872
39. Uchida, T., Egami, F., & Roy, A. B. (1981) Biochim. Biophys. Acta 657, 356-363.
40. Vallee, B. L., & Auld, D. S. (1993) Biochemistry 32, 6493-6501.
41. Waheed, A., & van Etten, R. L. (1979) Arch. Biochem. Biophys. 195, 248-251.
42. Waheed, A., & van Etten, R. L. (1980a) Arch. Biochem. Biophys. 203, 11-24.
43. Waheed, A., & van Etten, R. L. (1980b) Biochim. Biophys. Acta 614, 92-101.
44. Waheed, A., & van Etten, R. L. (1985) Int. J. Pept. Protein Res. 26, 362-372.
45. Weast, R. C., Selby, S. M., & Hodgman, C. D. (1962) Handbook of Chemistry and Physics, p D90, The Chemical Rubber Co., Cleveland, OH.