Substrate specific sulfatase activity from hair follicles in recessive X-linked ichthyosis.
Recessive X-linked ichthyosis (RXLI) has its biochemical basis in a defect of the enzyme steroid sulfatase. Since several studies have reported a simultaneous deficiency of arylsulfatase C and steroid sulfatase it has been hypothesized that both enzymes are identical. In human hair follicles, however, hydrolytic activity for 4-methylumbelliferone sulfate, the substrate for arylsulfatase C, is found, while dehydroepiandrosterone sulfate is not hydrolyzed at all. These findings suggested the possible existence of two different enzymes. In the present paper structure-activity studies and molecular energy calculations are used for the demonstration that the remaining sulfatase activity in hair follicles of RXLI patients can be explained on the basis of the assumption that the enzyme has not lost its total function but has become less efficient.
D000293:Adolescent; D000328:Adult; D003687:Dehydroepiandrosterone / Q000031:analogs & derivatives / Q000378:metabolism; D019314:Dehydroepiandrosterone Sulfate; D004855:Equilenin / Q000378:metabolism; D004970:Estrone / Q000031:analogs & derivatives / Q000378:metabolism; D005260:Female; D008040:Genetic Linkage; D006197:Hair / Q000201:enzymology*; D006801:Humans; D006923:Hymecromone / Q000031:analogs & derivatives / Q000378:metabolism; D007057:Ichthyosis / Q000201:enzymology* / Q000235:genetics; D008297:Male; D008875:Middle Aged; D013379:Substrate Specificity; D013429:Sulfatases / Q000378:metabolism*; D014960:X Chromosome
C019492:4-methylumbelliferyl sulfate; D004970:Estrone; D006923:Hymecromone; D003687:Dehydroepiandrosterone; D019314:Dehydroepiandrosterone Sulfate; D013429:Sulfatases; C017296:estrone sulfate; D004855:Equilenin