The studies on substrate, product and inhibitor binding to a wild-type and neuronopathic form of human acid-β-glucosidase

Journal of Molecular Modeling

Volumn 13, Issue 11, 2007, Pages 1133-1139

  Zubrzycki, Igor Z ^a   Borcz, Agnieszka ^a   Wiacek, Magdalena ^a   Hagner, Wojciech ^b  

^a UNIVERSITY OF RZESZÓW   (Poland)

^b NICOLAUS COPERNICUS UNIVERSITY   (Poland)

Author keywords

Human acid glucosidase; Molecular docking; Molecular dynamics; Mutations; S binding place

Indexed keywords

ARGININE; GLUCOSYLCERAMIDASE; LEUCINE; PROLINE; RECOMBINANT PROTEIN;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INHIBITOR INTERACTION; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GAUCHER DISEASE; MOLECULAR DOCKING; MOLECULAR DYNAMICS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FUNCTION; WILD TYPE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHEMISTRY; ENZYMOLOGY; HUMAN; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; GAUCHER DISEASE; GLUCOSYLCERAMIDASE; HUMANS; POINT MUTATION; RECOMBINANT PROTEINS; X-RAY DIFFRACTION;

EID: 34848920371     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-007-0232-5     Document Type: Article

References (29)

1. Erickson AH, Ginns EI, Barranger JA (1985) J Biol Chem 260:14319-14324
2. Coutinho PM, Henrissat B (1999) Carbohydrate-active enzymes: An integrated database approach. The Royal Society of Chemistry, Cambridge, pp 3-12
3. Bergmann JE, Grabowski GA (1989) Am J Hum Genet 44:741-750
4. Grace ME, Newman KM, Scheinker V, Berg-Fussman A, Grabowski GA (1994) J Biol Chem 269:2283-2291
5. Sawkar AR, Cheng WC, Beutler E, Wong CH, Balch WE, Kelly JW (2002) Proc Natl Acad Sci (USA) 99:15428-15433
6. Barranger JA, Ginns EI (1989) Glucosylceramide Lipidoses: Gaucher Disease, 6th ed. McGraw Hill Inc., New York
7. Takasaki S, Murray GJ, Furbisch FS, Brady RO, Baranger JA, Kobata A (1984) J Biol Chem 259:10112-10117
8. Berg-Fussman A, Grace ME, Grabowski GA (1993) J Biol Chem 268:14861-14866
9. Horowitz M, Zimran A (1994) Hum Mutat 3:1-11
10. Fabrega S, Durand P, Mornon J-P, Lehn P (2002) J Soc Biol 196:151-160
11. Miao S, McCarter JD, Grace ME, Grabowski GA, Aebersold R, Withers SG (1994) J Biol Chem 269:10975-10978
12. Fabrega S, Durand P, Codogno P, Bauvy C, Delomenie C, Henrissat B, Martin BM, McKinney C, Ginns EI, Mornon JP, Lehn P (2000) Glycobiology 10:1217-1224
13. Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, Sussman JL (2003) EMBO Rep 4:704-709
14. Premkumar L, Sawkar AR, Boldin-Adamsky S, Toker L, Silman I, Kelly JW, Futerman AH, Sussman JL (2005) J Biol Chem 280:23815-23819
15. Morel N, Bon S, Greenblatt H, Wodak S, Sussman JL, Massoulie J, Silman I (1999) Mol Parmacol 55:982-992
16. Guex N, Peitsch MC (1997) Electrophoresis 18:2714-2723
17. Berendsen HJ, Postma JP, van Gunsteren WF, Hermans J (1981) Intramolecular Forces, D. Reidel Publishing Company, Dordrecht
18. Zubrzycki IZ (2002) Biophys J 82:2906-2915
19. Ryckaert JP, Ciccotti G, Berendsen HJC (1977) Journal of Computational Physics 23:327
20. Berendsen HJC, Postma JPM, Vangunsteren WF, Dinola A, Haak JR (1984) J Chem Phys 81:3684
21. Van Der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJ (2005) J Comput Chem 26:1701-1718
22. Jorgensen WL, Maxwell DS, Tirado-Rives J (1996) J Am Chem Soc 118:11225-11236
23. Humphrey W, Dalke A, Schulten K (1996) J Mol Graph 14:33-38, 27-38
24. DeLano W, The PyMOL Molecular Graphics System. 2002, DeLano Scientific, San Carlos
25. Hetenyi C, van der Spoel D (2006) FEBS Lett 580:1447-1450
26. Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, Belew RK, Olson AJ (1998) J Comput Chem 19:1639
27. Sanner MF (1999) J Mol Graph Model 17:57-61
28. Kabsch W, Sander C (1983) Biopolymers 22:2577-2637
29. Uchiyama A, Tomatsu S, Kondo N, Suzuki Y, Shimozawa N, Fukuda S, Sukegawa K, Taki N, Inamori H, Orii T (1994) Hum Mol Genet 3:1183-1184