Title : Structural comparison of differently glycosylated forms of
acid-beta-glucosidase , the defective
enzyme in Gaucher disease
Abstract :
- Gaucher disease is caused by mutations in the gene encoding acid-beta-glucosidase
- A recombinant form of this enzyme , Cerezyme, is used to treat Gaucher disease patients by ; enzyme-replacement therapy'
- Crystals of Cerezyme after its partial deglycosylation were obtained earlier and the structure was solved to 2.0 A resolution [Dvir et al. (2003), EMBO Rep. 4, 704-709]
- The crystal structure of unmodified Cerezyme is now reported, in which a substantial number of sugar residues bound to three asparagines via N-glycosylation could be visualized
- The structure of intact fully glycosylated Cerezyme is virtually identical to that of the partially deglycosylated enzyme
- However, the three loops at the entrance to the active site , which were previously observed in alternative conformations, display additional variability in their structures
- Comparison of the structure of acid-beta-glucosidase with that of xylanase , a bacterial enzyme from a closely related protein family, demonstrates a close correspondence between the active-site residues of the two enzymes
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. glycosylated, , acid-beta-glucosidase, -, -
- 0. glycosylated, , enzyme, -, -
- 5. deglycosylated, , enzyme, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):