Catalytic mechanism and specificity for hydrolysis and transglycosylation reactions of cytosolic β-glucosidase from guinea pig liver

Journal of Biological Chemistry

Volumn 273, Issue 52, 1998, Pages 34941-34948

  Hays, William S ^a   VanderJagt, Dorothy J ^a   Bose, Bidisha ^b   Serianni, Anthony S ^b   Glew, Robert H ^a  

^a UNIVERSITY OF NEW MEXICO HEALTH SCIENCES CENTER   (United States)

^b UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCOSIDASE; MANNOSIDE;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CALCULATION; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; CYTOSOL; ENZYME ASSAY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GLYCOSYLATION; GUINEA PIG; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; STOICHIOMETRY;

ANIMALS; BETA-GLUCOSIDASE; CATALYSIS; CYTOSOL; DISACCHARIDES; FLUORODEOXYGLUCOSE F18; GLYCOSYLATION; GUINEA PIGS; HYDROLYSIS; LIVER; MODELS, CHEMICAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; REFERENCE STANDARDS; RHAMNOSE; STEREOISOMERISM; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ANIMALIA; CAVIA PORCELLUS; MAMMALIA; SUS SCROFA;

EID: 0032567336     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.52.34941     Document Type: Article

References (24)

1. Glew, R. H., Gopalan, V., Forsyth, G. W., and VanderJagt, D. J. (1993) in β-Glucosidases: Biochemistry and Molecular Biology, pp. 83-112, American Chemical Society, Washington, D. C.
2. Gopalan, V., VanderJagt, D. J., Libell, D. P., and Glew, R. H. (1992) J. Biol. Chem. 267, 9629-9638
3. Legler, G., and Bieberich, E. (1988) Arch. Biochem. Biophys. 260, 427-436
4. Koshland, D. E. (1953) Biol. Rev. Cambr. Philos. Soc. 28, 416-436
5. Legler, G. and Bieberich, E. (1988) Arch. Biochem. Biophys. 260, 437-442
6. Bader, D. E., Ring, M., and Huber, R. E. (1988) Biochem. Biophys. Res. Commun. 153, 301-306
7. Grace, M. E., Newman, K. M., Scheinker, V., Berg-Fussman, A., and Grabowski, G. A. (1994) J. Biol. Chem. 269, 2283-2291
8. Gebler, J. C., Aebersold, R., and Withers, S. G. (1992) J. Biol. Chem. 267, 11126-11130
9. Miao, S., McCarter, J. D., Grace, M. E., Grabowski, G. A., Aebersold, R., and Withers, S. G. (1994) J. Biol. Chem. 269, 10975-10978
10. McCarter, J. D., and Withers, S. G. (1994) Curr. Opin. Struct. Biol. 4, 885-892
11. Dinter, A., and Berger, E. G. (1995) Adv. Exp. Med. Biol. 376, 53-82
12. Thompson, J. E., Smith, R. C., and Fry, S. C. (1997) Biochem J. 327, 699-708
13. Jobe, A., and Bourgeois, S. (1972) J. Mol. Biol. 69, 397-408
14. Hays, W. S., Jenison, S. A., Yamada, T., Pastuszyn, A. P., and Glew, R. H. (1996) Biochem. J. 319, 829-837
15. Gopalan, V., Pastuszyn, A., Galey, W. R., and Glew, R. H. (1992) J. Biol. Chem. 267, 14027-14032
16. Segel, I. H. (1975) Enzyme Kinetics, pp.100-136, John Wiley & Sons, New York
17. Bax, A., and Subramanian, S. (1986) J. Magn. Reson. 67, 565-569
18. Bock, K., and Pedersen, C., (1983) Adv. Carbohydr. Chem. Biochem. 41, 27-66
19. Podlasek, C. A., Wu, J., Stripe, W. A., Bondo, P. B., and Serianni, A. S. (1995) J. Am. Chem. Soc. 117, 8635-8644
20. Street, I. P., Kempton, J., and Withers, S. G. (1992) Biochemistry 31, 9970-9978
21. Gopalan, V., Glew, R. H., Libell, D. P., and DePetro, J. J. (1989) J. Biol. Chem. 264, 15418-15422
22. Pocsi, I., and Kiss, L. (1988) Biochem. J. 256, 139-146
23. Walsh, C. T. (1979) Enzymatic Reaction Mechanisms, pp. 267-307, Freeman, San Francisco
24. McCarter, J. D., Adam, M. J., and Withers, S. G. (1992) Biochem. J. 286, 721-727