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Literature summary for 3.1.6.13 extracted from

  • Demydchuk, M.; Hill, C.; Zhou, A.; Bunkoczi, G.; Stein, P.; Marchesan, D.; Deane, J.; Read, R.
    Insights into Hunter syndrome from the structure of iduronate-2-sulfatase (2017), Nat. Commun., 8, 15786 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.6.13

Cloned(Commentary)

Cloned (Comment) Organism
expression in HT-1080 human fibroblasts Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure with a covalently bound sulfate ion in the active site, to 2.3 A resolution Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P22304
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein deglycosylation with PNGase leads to a decrease in molecular mass from 76000 Da to 58000 Da Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.6
-
 20°C, pH 5.0 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl-alpha-L-iduronate 2-sulfate + H2O
-
 Homo sapiens 4-methylumbelliferol + L-iduronate 2-sulfate
-
 ?
additional information mechanism follows a SN2 nucleophilic attack of the formylglycine FGH84 on the sulfur atom to generate the covalent formylglycine-S adduct, followed by elimination of bound sulfate and rehydration of the resultant formylglycine aldehyde. Residues H229, H138, D334 and K347 are likely to play active roles in proton transfer or activation of water during the reaction cycle Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
? x * 76000, SDS-PAGE Homo sapiens