Aryl Sulfatase of Unusual Specificity from the Liver of Marine Mollusk Littorina kurila
M. I. Kusaikin,# M. S. Pesentseva, A. S. Sil’chenko, S. A. Avilov, V. V. Sova, T. N. Zvyagintseva, and V. A. Stonik
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Pacific Institute of Bioorganic Chemistry, Far East Division, Russian Academy of Sciences, pr. 100-letiya Vladivostoka 159, Vladivostok, 690022 Russia
An aryl sulfatase of unusual specificity has been isolated from the liver of marine mollusk Littorina kurila. It hydrolyzes p-nitrophenyl sulfate, does not affect the natural fucoidan, and catalyzes splitting off of the sulfate group in position C4 of xylose residues within the carbohydrate chains of holostane triterpene glycosides from sea cucumbers. The properties of the enzyme were studied at pH 5.4. The protein is homogeneous according to electrophoresis and has Μ 45 ± 1 kDa. The semiinactivation time of the enzyme at 60ºC is 20 min, and its K m value for the hydrolysis of p-nitrophenyl sulfate is 8.7 ± 1 mM. It was shown that natural sulfated polyhydroxysteroids inhibit activity of the sulfatase; their I 50 values depend on their structures and are within the range from10–3 to 10–5 M.
Key words: aryl sulfatase , specificity, inhibition; marine mollusk Littorina kurila ; sulfated polyhydroxysteroids ; triterpene glycosides
Received April 18, 2005; in final form, July 1, 2005
Russian Journal of Bioorganic Chemistry 2006, 32 (1):63-70