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- Title
Reexamination of the cysteine residues in glucocerebrosidase
- Authors
Moharram, Ramy; Maynard, Dawn; Wang, Eric S.; Makusky, Anthony; Murray, Gary J.; Martin, Brian M.
- Abstract
Abstract: Glucocerebrosidase, the deficient enzyme in Gaucher disease, catalyzes the cleavage of the β-glycosidic linkage of glucosylceramide. A previous study on the enzyme identified three disulfide bridges and a single sulfhydryl [Lee, Y., Kinoshita, H., Radke, G., Weiler, S., Barranger, J.A. and Tomich, J.M. (1995) Position of the sulfhydryl group and the disulfide bonds of human glucocerebrosidase. J. Protein Chem. 14(3), 127–137] but recent publication of the X-ray structure identifies only two disulfide bridges with three free sulfhydryls [Dvir, H., Harel, M., McCarthy, A.A., Toker, L., Silman, I., Futerman, A.H. and Sussman, J.L. (2003) X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease. EMBO. 4(7), 704–709]. Using chemical modifications, acid cleavage and enzymatic digestion methods, we report that three free sulfhydryls exist and that the remaining four cysteines form two disulfide bonds located within the first 25 amino-terminal residues, supporting the X-ray structure.
- Subjects
ENZYMES; VIADUCTS; CATALYSTS; PROTEINS
- Publication
FEBS Letters, 2006, Vol 580, Issue 14, p3391
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.04.096