Sulfatase

Identifiers
Symbol Sulfatase
Pfam PF00884
InterPro IPR000917
PROSITE PDOC00117
SCOP 1auk
SUPERFAMILY 1auk
OPM superfamily 24
OPM protein 1p49

Sulfatases EC 3.1.6.- are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates.

Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfate esters.

Occurrence and importance

Sulfatases are found in lower and higher organisms. In higher organisms they are found in intracellular and extracellular spaces. Steroid sulfatase is distributed in a wide range of tissues throughout the body, enabling sulfated steroids synthesized in the adrenals and gonads to be desulfated following distribution through the circulation system. A large number of sulfatases are localized in the lysosome, an acidic digestive organelle found within the cell. Lysosomal sulfatases cleave a range of sulfated carbohydrates including sulfated glycosaminoglycans and glycolipids. Genetic defects in sulfatase activity can arise through mutations in individual sulfatases and result in certain lysosomal storage disorders with a spectrum of phenotypes ranging from defects in physical and intellectual development.

Three-dimensional structure

The following sulfatases have been shown to be structurally related based on their sequence homology:[1][2][3]

Human proteins containing this domain

ARSA; ARSB; ARSD; ARSE; ARSF; ARSG; ARSH; ARSI; ARSJ; ARSK; GALNS; GNS; IDS; PIGG; SGSH; STS; SULF1; SULF2;

References

  1. von Figura K, Vingron M, Schmidt B, Meyer HE, Peters C, Rommerskirch W, Rupp K, Pohlmann R, Zuhlsdorf M (1990). "Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B". J. Biol. Chem. 265 (6): 3374–3381. PMID 2303452.
  2. Wilson PJ, Morris CP, Anson DS, Occhiodoro T, Bielicki J, Clements PR, Hopwood JJ (1990). "Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA". Proc. Natl. Acad. Sci. U.S.A. 87 (21): 8531–8535. doi:10.1073/pnas.87.21.8531. PMC 54990Freely accessible. PMID 2122463.
  3. Grossman AR, de Hostos EL, Schilling J (1989). "Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii". Mol. Gen. Genet. 218 (2): 229–239. doi:10.1007/BF00331273. PMID 2476654.

This article incorporates text from the public domain Pfam and InterPro IPR000917

This article is issued from Wikipedia - version of the 6/6/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.