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Literature summary for 3.1.6.8 extracted from

  • Vagedes, P.; Saenger, W.; Knapp, E.W.
    Driving forces of protein association: the dimer-octamer equilibrium in arylsulfatase A (2002), Biophys. J., 83, 3066-3078.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cerebroside 3-sulfate + H2O Homo sapiens
-
cerebroside + sulfate galactosyl ceramid ?
cerebroside 3-sulfate + H2O Homo sapiens
-
cerebroside + sulfate galactosyl ceramide ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P15289
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cerebroside 3-sulfate + H2O
-
Homo sapiens cerebroside + sulfate galactosyl ceramid ?
cerebroside 3-sulfate + H2O
-
Homo sapiens cerebroside + sulfate galactosyl ceramide ?

Subunits

Subunits Comment Organism
dimer at pH above 6, the enzyme exists in solution as a dimer Homo sapiens
More The dimer-octamer equilibrium is regulated by the pH and may be explained by a switch function of Glu424. Glu424 in the conformation suitable for the intramolecular hydrogen bonds to Gln460. Glu424 in the conformation suitable for the intermolecular hydrogen bonds to Phe398 Homo sapiens
octamer at pH below 6, the enzyme exists in solution as octamer Homo sapiens