3.10.1.1: N-sulfoglucosamine sulfohydrolase
This is an abbreviated version!
For detailed information about N-sulfoglucosamine sulfohydrolase, go to the full flat file.
Word Map on EC 3.10.1.1
-
3.10.1.1
-
mucopolysaccharidosis
-
lysosomal
-
sanfilippo
-
mps-iiia
-
naglu
-
n-sulfate
-
sulfate-derived
-
heparinum
-
medicine
-
oestrone
-
hgsnat
-
sumf1
-
iduronate
-
sulfatases
-
ubiquitin-positive
-
drug development
-
pharmacology
-
diagnostics
- 3.10.1.1
- mucopolysaccharidosis
- lysosomal
-
sanfilippo
-
mps-iiia
- naglu
-
n-sulfate
-
sulfate-derived
- heparinum
- medicine
- oestrone
- hgsnat
- sumf1
-
iduronate
-
sulfatases
-
ubiquitin-positive
- drug development
- pharmacology
- diagnostics
Reaction
Synonyms
2-desoxy-2-sulphamido-D-glucose sulphamidase, 2-desoxy-D-glucoside-2-sulphamate sulphohydrolase, heparan N-sulfatase, heparan-N-sulfatase, heparan-N-sulphatase, heparin sulfamidase, N-sulfoglucosamine sulfohydrolase, N-sulphoglucosamine, SGSH, sulfamate sulfohydrolase, sulfamidase, sulfoglucosamine sulfamidase, sulphamate sulphohydrolase, sulphamidase, sulphohydrolase
ECTree
Advanced search results
Reaction
Reaction on EC 3.10.1.1 - N-sulfoglucosamine sulfohydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
N-sulfo-D-glucosamine + H2O = D-glucosamine + sulfate
catalytic reaction mechanism: the active-site formylglycine (FGly70), which is intrinsically reactive, undergoes hydration to form the resting state of the enzyme with a gem-diol group (step 1). Coordination of one of the hydroxyl groups of the gem-diol to a Ca2+ ion facilitates the development of a negative charge on the O atom as its proton is lost to a base. The negatively charged O atom nucleophilically attacks the sulfur centre of the N-linked sulfate group on the glucosamine substrate (step 2), resulting in a covalently bound enzyme-substrate complex with a pentavalent sulfur transition state. An acid (possibly His181) facilitates the cleavage of the S-N bond by protonating the bridging N atom to form an amine leaving group on the N-desulfated substrate, which diffuses away, leaving an O-sulfated enzyme (step 3). Finally, in a step that underlines the importance of the formylglycine residue, another base (His125) deprotonates the second hydroxyl group, resulting in a negatively charged O atom (step 4) that forms a double bond with the C atom as the C-O bond between it and the bridging O atom of the sulfate group breaks, eliminating the sulfate ion and regenerating the formylglycine residue (step 5)