N-acetylglucosamine 6-sulfatase (GNS) hydrolyses 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of keratan sulfate

Stable Identifier
R-HSA-1638032
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

N-acetylglucosamine 6-sulfatase (GNS) is a lysosomal enzyme which degrades glycosaminoglycans such as heparan sulfate and keratan sulfate. GNS shows strong sequence similarity to other sulphatases such as the family of arylsulfatases and the conversion to 3-oxo-alanine (formylglycine, FGly) of a cysteine residue is critical for catalytic activity, based on this similarity (Robertson et al. 1992, Robertson et al. 1988). Defects in GNS are the cause of mucopolysaccharidosis type IIID (MPSIIID, MIM:252940), also called Sanfilippo D syndrome (Valstar et al. 2010).

Literature References
PubMed ID Title Journal Year
20232353 Mucopolysaccharidosis type IIID: 12 new patients and 15 novel mutations

Kariminejad, R, Willems, PJ, Eckert, D, Czartoryska, B, Omran, H, Tokatli, A, Wessels, MW, Bertoli-Avella, AM, Elfferich, P, Olmer, R, Bürger, F, van Diggelen, OP, Valstar, MJ, Niermeijer, MF, van den Bos-Terpstra, F, Ruijter, GJ, Neijs, S, Suheyl Ezgü, F, Bosschaart, AN, Filocamo, M, Poorthuis, BJ, Simeonov, E, Halley, DJ, Puissant, H, Wevers, RA, de Graaf, B

Hum Mutat 2010
1463457 A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases

Hopwood, JJ, Morris, CP, Freeman, C, Robertson, DA

Biochem J 1992
3196333 Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase

Hopwood, JJ, Morris, CP, Freeman, C, Nelson, PV, Robertson, DA

Biochem Biophys Res Commun 1988
Participants
Participates
Catalyst Activity

N-acetylglucosamine-6-sulfatase activity of OxA-GNS [lysosomal lumen]

Orthologous Events
Authored
Reviewed
Created
Cite Us!