EC Number   |
Subunits |
Reference |
|---|
   3.1.6.8 | monomer |
1 * 140000, each monomer consists of 2 equivalent polypeptide chains |
135684, 135695 |
| 3.1.6.8 | monomer |
1 * 66000, SDS-PAGE |
681035 |
| 3.1.6.8 | monomer |
at pH 5.6 monomer, at pH 4.8 tetramer |
135554, 135679, 135695 |
| 3.1.6.8 | More |
mature lysosomal arylsulfatase A forms dimers at neutral pH, while in the early biosynthetic pathway, arylsulfatase A forms oligomers with more than two subunits. Within a heteromer, the misfolded subunit exerts a dominant negative effect on the wild-type subunit |
714958 |
| 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 |
650583 |
| 3.1.6.8 | More |
the polypeptide complexes, rather than the monomers, are subject to endoplasmic reticulum quality control and, within a heteromer, the misfolded subunit exerts a dominant negative effect on the wild-type subunit |
714779 |
| 3.1.6.8 | octamer |
ar pH 5.0-5.4, the enzyme exists in solution as a dimer or as an octamer |
649125 |
| 3.1.6.8 | octamer |
at pH below 6, the enzyme exists in solution as octamer |
650583 |
| 3.1.6.8 | octamer |
tetramer of dimers |
135692 |
| 3.1.6.8 | oligomer |
early enzyme |
714958 |
