Enzymes for Research, Diagnostic and Industrial Use
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| Catalog | Product Name | EC No. | CAS No. | Source | Price |
|---|---|---|---|---|---|
| NATE-0002 | Native Flavobacterium heparinum 2-O-Sulfatase | Flavobacterium ... | Inquiry |
2-O-sulfatase is an enzyme that plays a key role in biological processes through its ability to catalyze the removal of sulfate from molecules. Sulfation is a post-translational modification that is involved in many biological processes such as cell signaling, extracellular matrix formation and xenobiotic metabolism. The sulfate group is derived from ATP and is transferred to the receptor molecule via a thiotransferase to generate the sulfation product. Sulfate groups can also be removed by sulfatases to generate desulfation products.
2-O-sulfatase consists of a polypeptide chain that contains the catalytic site and is divided into several structural domains. The catalytic site consists of a sulfate ion, a calcium ion and a water molecule. This catalytic site is surrounded by a characteristic fold that is similar to the conserved fold of the sulfatase family. 2-O-sulfatase is also capable of forming dimers, although their functional relevance is not known.
2-O-sulfatase catalyzes the hydrolysis reaction of the 2-O-sulfate group in GAGs, including heparan sulfate (HS), dermatan sulfate (DS), and chondroitin sulfate (CS). After hydrolysis, these GAGs can be further processed by other enzymes, leading to the production of smaller GAG metabolites that are ultimately excreted. 2-O-sulfate esterase hydrolysis of the 2-O-sulfate moiety is essential for the catabolism and recycling of GAGs, and disruption of its activity can lead to the accumulation of undigested GAGs, resulting in lysosomal storage disease.
Mutations in the gene encoding sulfatase modifier 1 (SUMF1) or sulfatase can lead to reduced 2-O-sulfatase activity, resulting in a series of lysosomal storage diseases collectively known as sulfatase deficiency syndromes. These disorders include Maroteaux-Lamy syndrome, Sanfilippo syndrome and other mucopolysaccharidoses characterized by the accumulation of undigested GAGs in the lysosomes of cells.
The potential application of 2-O-sulfatase has been explored in an animal model of Sanfilippo syndrome. In an animal model of Sanfilippo syndrome, intracerebral injection of recombinant 2-O-sulfatase produced impressive effects by reducing the storage of sulfated GAGs in lysosomes, delaying the progression of the disease. Recombinant technology has enabled the production of 2-O-sulfatase and offers potential efficacy for enzyme replacement therapy in patients with Sanfilippo and other sulfate deficiency syndromes. Replacement of this deficient enzyme by gene therapy or treatment with recombinant preparations of 2-O-sulfate lyase could help treat lysosomal storage diseases.
2-O-sulfatase is a key enzyme that plays a fundamental role in the degradation of sulfated glycosaminoglycans. The enzyme is expressed in a variety of tissues, but primarily in the liver, where it plays a role in the metabolism of GAGs. 2-O-sulfatase deficiency can lead to a range of lysosomal storage diseases, and the development of new therapies may involve the use of recombinant 2-O-sulfatase and sulfatase-activating probes. Understanding the function and regulation of 2-O-sulfatase has the potential to lead to the development of new diagnostic tools and therapeutic options for the treatment of sulfatase deficiency.
