Arylsulfohydrolase physicochemical properties

Phosphoadenosine 5 -phosphosulfate (PAPS) is the well-known sulfate donor that occupies a central position in sulfate biochemistry (Balasubrama-nian and Bachhawat, 1970 DeMeoi, 1975 Farooqui, 1980b). It is hydrolyzed into PAP and sulfate by PAPS sulfohydrolase (Balasubramanian and Bachhawat, 1962). Nothing has been reported on the purification of this enzyme, but the crude enzyme preparation shows optimal activity at pH 6.0. It is activated by Co " " and Mn " " and inhibited by ADP, fluoride, and sulfhydryl compounds (Balasubramanian and Bachhawat, 1962). The desulfation of PAPS is a specific reaction. Arylsulfohydrolase A from chicken brain and rabbit kidney cortex does not hydrolyze PAPS to PAP (Farooqui and Bachhawat, 1972 Farooqui and Helwig, unpublished). Because PAPS sulfohydrolase has never been purified from any source, nothing is known about its physicochemical properties. 

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