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Title of Journal: Chem Nat Compd

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Abbravation: Chemistry of Natural Compounds

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Springer US

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DOI

10.1007/s12194-013-0207-4

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ISSN

1573-8388

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A new arylsulfatase from the marine mollusk Empha

Authors: M S Pesentseva V V Sova Al S Sil′chenko A A Kicha Ar S Sil′chenko T Haertle T N Zvyagintseva
Publish Date: 2012/11/17
Volume: 48, Issue: 5, Pages: 853-859
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Abstract

A new arylsulfatase EC 3161 was isolated from the liver of the marine mollusk Turbo chrysostomus The enzyme catalyzed hydrolysis of potassium pnitrophenylsulfate did not affect natural fucoidan and catalyzed cleavage of sulphate in the C4 position of xylose included in carbohydrate chains of holothurian triterpene glycosides Halistanol sulphate and glycosides from starfish that contained sulfates in the aglycon part of the molecule inhibited the activity of the arylsulfatase Several holothurian glycosides in small concentrations 35–8 × 10–10 M increased the enzyme activity The arylsulfatase activity was maximal at pH 7 Its molecular weight was 35 kDa according to gelfiltration The Michaelis constant KM for hydrolysis of pnitrophenylsulfate was 10 mM The inactivation halflife of the enzyme was 15 min at 55°C

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