| Modification Notes |
Sulfatases are enzymes that remove sulfate residues from a variety of substrates via the hydrolysis of sulfate esters. In order to function properly, sulfatases require the presence of Cå-formylglycine (FGly), a unique amino acid, in their active site. This amino acid is synthesized by enzymes that use a cysteine to posttranslationally generate FGly. SUMF1 (sulfatase modifying factor 1), also known as FGE, is a 374 amino acid alternatively spliced protein that localizes to the lumen of the endoplasmic reticulum and belongs to the sulfatase-modifying factor family. Expressed ubiquitously with highest expression in liver, kidney and pancreas, SUMF1 exists as either a monomer, a homodimer or a heterodimer (with SUMF2) and functions to oxidize sulfatase cysteine residues to an active FGIy residue, thereby playing an important role in sulfatase activity. Defects in the gene encoding SUMF1 are the cause of multiple sulfatase deficiency (MSD), a heterogeneous disorder characterized by metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. |
