Reexamination of the cysteine residues in glucocerebrosidase.
FEBS Lett
; 580(14): 3391-4, 2006 Jun 12.
Article
em En
| MEDLINE
| ID: mdl-16712845
ABSTRACT
Glucocerebrosidase, the deficient enzyme in Gaucher disease, catalyzes the cleavage of the beta-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-beta-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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cisteína
/
Glucosilceramidase
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Estados Unidos