EC Number |
General Information |
Reference |
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3.1.6.12 | malfunction |
ARSB enzymatic activity is significantly greater in normal than in malignant tissue |
715789 |
3.1.6.12 | malfunction |
ARSB mutations are involved in mucopolysaccharidosis type VI, i.e. MPS VI, Maroteaux-Lamy syndrome |
708591 |
3.1.6.12 | malfunction |
arylsulfatase B is associated with the lysosomal storage disease mucopolysaccharidosis VI |
707573 |
3.1.6.12 | malfunction |
ASB-deficient cells accumulate dermatan sulfate and chondroitin sulfate, which may be partially hydrolyzed by other lysosomal hydrolases |
707109 |
3.1.6.12 | malfunction |
deficiencies of N-acetylgalactosamine-4-sulfatase is associated with the mucopolysaccharidoses |
680928 |
3.1.6.12 | malfunction |
inborn deficiency of ARSB leads to the lysosomal storage disease mucopolysaccharidosis VI, characterized by accumulation of sulfated glycosaminoglycans in vital organs, disruption of normal physiological processes, severe morbidity, and premature death |
715789 |
3.1.6.12 | malfunction |
mucopolysaccharidosis type VI, i.e. MPS VI or Maroteaux-Lamy syndrome, is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase impairs the stepwise degradation of the glycosaminoglycan dermatan sulfate |
709389 |
3.1.6.12 | malfunction |
mucopolysaccharidosis VI, MPS VI or Maroteaux-Lamy syndrome, is an inherited metabolic disease caused by the deficiency of N-acetylgalactosamine 4-sulfatase. In the absence of this enzyme, the stepwise degradation of the glycosaminoglycan dermatan sulfate is blocked, resulting in intracellular accumulation of the substrate into the lysosomes, leading to a progressive disorder with multiple organ and tissue involvement |
709974 |
3.1.6.12 | malfunction |
silencing or overexpression of ASB in normal rat kidney epithelial cells in tissue culture modifies the content of total sulfated glycosaminoglycans, C4S, kininogen, and bradykinin in spent media and cell lysates. Treatment of the cultured cells with chondroitinase ABC also increases the secretion of bradykinin into the spent media and reduces the C4S-associated kininogen. When ASB is overexpressed, the cellular kininogen that associates with C4S declines, suggesting a vital role for chondroitin-4-sulfation in regulating the kininogen-C4S interaction |
707573 |
3.1.6.12 | metabolism |
modification of expression of the enzyme regulates the content of chondroitin sulfate |
680928 |