sulfatase

Iduronate 2-Sulfatase, also known as IDS, is a member of the highly conserved sulfatase family of enzymes that catalyze the hydrolysis of O- and N-sulfate esters from a variety of substrates. The human Iduronate 2-Sulfatase IDS consists of a signal peptide, a propeptide, and a mature chain that may be further processed into two chains. Among the identified 18 human sulfatases, Iduronate 2-Sulfatase IDS is required for the lysosomal degradation of the glycosaminoglycans (GAG), heparan sulfate, and dermatan sulfate. Multiple mutations in this X-chromosome localized gene result in Iduronate 2-Sulfatase IDS enzymatic deficiency and lead to the sex-linked Mucopolysaccharidosis Type II (MPS II ), also known as Hunter Syndrome characterized by the lysosomal accumulation of the GAG and their excretion in urine. MPS II has a wide spectrum of clinical manifestations ranging from mild to severe due to the level of Iduronate 2-Sulfatase IDS enzyme. Retroviral-mediated Iduronate 2-Sulfatase IDS gene transfer into lymphoid cells would be a promising gene therapeutic strategy.

Human Sulfatase Modifying Factor 1 (SUMF1) is a 42kDa protein. SUMF1 is a Ca2+-binging member of the sulfatase-modifying factor family. SUMF1 is a soluble ER lumenal glycoprotein, it converts inactive sulfatases into an active form by transforming a catalytic site cysteine into a formylglycine residue. In the ER, SUMF1 can exist as either a monomer, or a disulfide-linked homodimer or a heterodimer with SUMF2. Three splice isoforms are known.

GALNS Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 82.4 kDa and the accession number is P34059.

N-Acetylglucosamine-6-Sulfatase is a member of the Sulfatase family. N-Acetylglucosamine-6-Sulfatase is required for the lysosomal degradation of the Glycosaminoglycans (GAG) Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase hydrolyzes the 6-Sulfate groups of the N-Acetyl-D-Glucosamine 6-Sulfate units of Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase binds 1 Calcium ion per subunit. N-Acetylglucosamine-6-Sulfatase deficiency are the cause of Mucopolysaccharidosis Type 3D (MPS3D), an inborn error leading to lysosomal accumulation of heparan sulfate. MPS3D has profound mental deterioration, hyperactivity, and relatively mild somatic manifestations.

Sialidase-1 belongs to the N-acetyl-a neuraminidase family. Sialidase-1 is expressed in many tissues; it is highly expressed in the pancreas, and weakly expressed in the brain. Sialidase-1 is a lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. Deficiencies in the human enzyme Sialidase-1 leads to sialidosis, a rare lysosomal storage disease. Sialidase-1 has been shown to interact with Cathepsin A (protective protein), β-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex.

N-Sulphoglucosamine Sulphohydrolase (SGSH) is an important member of the sulfatase family which is involved in the degradation of heparin sulfate. SGSH binds one calcium ion per subunit as a cofactor. SGSH catalyzes N-sulfo-D-glucosamine and H2O to D-glucosamine and sulfate. SGSH deficiency is result in mucopolysaccharidosis type 3A (MPS3A), a recessive lysosomal storage disease characterized by neurological dysfunction but relatively mild somatic manifestations.