Sulfatases are a group of esterase class enzymes that catalyze the hydrolysis of sulfate esters. They can be found in a variety of substrates, such as proteins, carbohydrates, and proteins.
The purpose of sulfatase is to degrade sulfur-containing compounds in the environment, but they have a range of functions, both inside and outside the cell. For instance, sulfatases are involved in the degradation of glycolipids in the lysosome of cells. They also have an essential function in the extra-cellular space through their actions on remodeling sulfated glycosaminoglycans.
Sulfatases are a fundamental building block of biological processes and are found in both higher and lower order organisms, both inside and outside the cell. In mammals, like humans, sulfur-containing compounds are produced in both the gonads and adrenals. These organs require the presence of sulfatase to distribute these compounds around the body. The enzyme binds to the sulfated steroids produced by these organs and then circulates them throughout the circulation system.
Sulfatase is also an essential component of the lysosome - a highly acidic, digestive organelle inside the cell. Cellular lysosomes use sulfatases to cleave sulfated glycolipids and glycosaminoglycans, allowing them to digest cellular material and the nutrients contained within other cells. Sulfatase, therefore, is a vital component of immune cell function and plays a crucial role in the digestion of foreign pathogens.
The field of the study of “sulf” sulfatases began in 2001 with the discovery of QSulf1 in the avian species, quail. Similar enzymes were then found in both rodents and humans, revealing that they are evolutionarily conserved and fundamental to the survival of life like the majority of sulfatases.
While many of the sulfatases found so far are located in the lysosomes of eukaryotic cells and essential in catabolism, the new class of sulfs sit on the cellular surface and interacts with the extra-cellular space. Unique structures anchor them to the cell surface, enabling them to secrete into the gaps between cells. Like regular sulfatases, sulfs remove sulfate groups, specifically those on the C-6 position of glucosamines.
Sulfs are different in other respects too. While the sulfatases that occur in the lysosome require a high level of acidity to operate, those in the extra-cellular space do not, preferring the neutral pH of their surrounding environment for optimal activity levels instead.
There are a variety of genetic disorders, such as multiple sulfatase deficiency, which inhibit the action of sulfatases in the body.
Sulfatases are a class of enzymes with a wide variety of structures. The following forms of the enzyme have similar three-dimensional structures; Steroid sulfatase, Cerebroside-sulfatase, Glucosamine-6-sulfatase and Sea urchin embryo arylsulfatase.
There is a range of arylsulfatase labeled A, B, and C, which have specific effects in the intra- and extra-cellular space.
Arylsulfatase A, for instance, is found in the lysosome and hydrolyzes cerebroside sulfate. The B variety of the enzyme is involved in the hydrolysis of sulfate ester group compounds from N-acetylgalactosamine 4-sulfate residues.
Arylsulfatase C is a form of the enzyme found in the membranes of cells that helps with the hydrolysis of 3-beta-hydroxy steroid sulfates.