Human β-glucuronidase: structure, function, and application in enzyme replacement therapy.

Abstract

Lysosomal storage diseases occur due to incomplete metabolic degradation of macromolecules by various hydrolytic enzymes in the lysosome. Despite structural differences, most of the lysosomal enzymes share many common features including a lysosomal targeting motif and phosphotransferase recognition sites. β-Glucuronidase (GUSB) is an important lysosomal enzyme involved in the degradation of glucuronate-containing glycosaminoglycan. The deficiency of GUSB causes mucopolysaccharidosis type VII (MPSVII), leading to lysosomal storage in the brain. GUSB is a well-studied protein for its expression, sequence, structure, and function. The purpose of this review is to summarize our current understanding of sequence, structure, function, and evolution of GUSB and its lysosomal enzyme targeting. Enzyme replacement therapy reported for this protein is also discussed.

• Authors: Huma Naz, Asimul Islam, Abdul Waheed, William S Sly, Faizan Ahmad, Imtaiyaz Hassan
• Journal: Rejuvenation research (Rejuvenation Res) Vol. 16 Issue 5 Pg. 352-63 (Oct 2013) ISSN: 1557-8577 [Electronic] United States
• PMID: 23777470 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Glucuronidase

Topics

• Enzyme Replacement Therapy
• Gene Expression Regulation, Enzymologic
• Glucuronidase (chemistry, genetics, metabolism)
• Humans
• Lysosomal Storage Diseases (enzymology, genetics)
• Lysosomes (metabolism)
• Mutation (genetics)