The slow kinetic transients of arylsulphatase A.
A simple model is described to account for the anomalous time course of arylsulphatase A. In the case of the ox liver and human placental enzymes the enzyme-nitrocatechol sulphate complex can, in addition to forming products, slowly break down to form an inactive species which can turn in slowly regenerate active enzyme. When the inactive form binds sulphate the rate of reactivation is enhanced, 218-fold in the case of the ox enzyme. Rat liver arylsulphatase A is refractory to reactivation by sulphate.
D000818:Animals; D002396:Catechols / Q000378:metabolism; D002417:Cattle; D002553:Cerebroside-Sulfatase / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008954:Models, Biological; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D051381:Rats; D013429:Sulfatases / Q000378:metabolism*; D013431:Sulfates / Q000494:pharmacology
D002396:Catechols; D013431:Sulfates; C012036:sodium sulfate; D013429:Sulfatases; D002553:Cerebroside-Sulfatase; C021228:4-nitrocatechol sulfate