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Purification and Properties of an Arylsulfatase from Aspergillus oryzae

From the ¹ From the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802

Arylsulfate sulfohydrolase II (EC 3.1.6.1) has been purified from Aspergillus oryzae. The purified arylsulfatase appears to be homogeneous on the basis of disc gel electrophoresis, sucrose density gradient centrifugation, and equilibrium ultracentrifugation. Physical properties and amino acid composition have been determined indicating the enzyme to have a molecular weight of 65,000 ± 2,000 with a high content of aspartic and glutamic acid.

Kinetic constants for the hydrolysis of a series of substituted phenyl sulfate esters at pH 4.0 and 7.5 have been determined. Plots of log V_max/K_m and log V_max against pK_a show that, as the electron-withdrawing ability of the substituent increases, log V_max/K_m increases with decreasing pK_a, while log V_max is independent of pK_a. These results are interpreted in terms of a covalent sulfuryl enzyme intermediate or a rate-determining conformational change.

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