EC Number   |
General Information |
Reference |
|---|
   3.1.6.1 | malfunction |
metachromatic leukodystrophy, MLD, is a lethal neurodegenerative disease caused by a deficiency in the lysosomal arylsulfatase A enzyme leading to the accumulation of sulfatides in glial and neuronal cells |
708658 |
| 3.1.6.1 | malfunction |
metachromatic leukodystrophy, MLD, is an autosomal recessive, lysosomal storage disease caused by a deficiency of the enzyme arylsulfatase A, ARSA |
709618 |
| 3.1.6.1 | metabolism |
in southwest China, soil arylsulfatase activity increases from cropland through to forest following post-agriculture succession, and is significantly lower in clasolite than in dolomite or limestone. Among 14 studied soil variables, soil pH, exchangeable calcium, organic carbon, clay and silt showed significant non-linear relationships with arylsulfatase activity. The activity of soil arylsulfatase is most controlled by soil pH and soil texture, but soil calcium and organic carbon only have indirect or spurious effects on arylsulfatase activity |
750481 |
| 3.1.6.1 | physiological function |
a one-time injection of human arylsufatase B into injured mouse spinal cord eliminates immunoreactivity for chondroitin sulfates within five days, and up to 9 weeks after injury. After a moderate spinal cord injury, locomotor recovery assessed by the Basso Mouse Scale in arylsulfatase B treated mice improves, compared to the buffer-treated control group, at 6 weeks after injection. After a severe spinal cord injury, mice injected with equivalent units of arylsulfatase B or bacterial chondroitinase ABC improve similarly and both groups achieve significantly more locomotor recovery than the buffer-treated control mice. Serotonin and tyrosine hydroxylase immunoreactive axons are more extensively present in mouse spinal cords treated with arylsulfatase B and chondroitinase ABC, and the immunoreactive axons penetrate further beyond the injury site than in control mice |
730725 |
| 3.1.6.1 | physiological function |
arylsulphatase A is a lysosomal enzyme that catabolizes sulphatides, it is likely to be under hormonal control, in particular, by estradiol and progesterone |
709667 |
| 3.1.6.1 | physiological function |
strain Kluyveromyces lactis DSM 70799 has no arylsulfatase activity, whereas the strain GG799 does. The only difference is a base substitution at position 415 resulting in an amino acid exchange from R139 in strain DSM 70799 to S139 in strain GG799. Amino acid position 139 is far away from the catalytic site of the arylsulfatase. The posttranslational modification of C56 to formylglycine is not found in the R139 variant. By contrast, the C56 residue of the S139 variant is modified. The inactive R139 variant exhibits a different structure regarding folding and packing compared to the active S139 variant |
749699 |
