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Literature summary 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.6.8 Homo sapiens P15289
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.1.6.8 dimer at pH above 6, the enzyme exists in solution as a dimer Homo sapiens
3.1.6.8 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
3.1.6.8 octamer at pH below 6, the enzyme exists in solution as octamer Homo sapiens