PMID: 6111349Feb 13, 1981Paper

3',5'-Cyclic nucleotide phosphodiesterase activity of the sulphatase A of ox liver

Biochimica Et Biophysica Acta
T UchidaA B Roy

Abstract

The sulphatase A (aryl-sulphate sulphohydrolase, EC 3.1.6.1) of ox liver hydrolyses adenosine 3',5'-monophosphate (cyclic AMP) to adenosine 5'-phosphate at an optimum pH of approx. 4.3, close that for the hydrolysis of cerebroside sulphate, a physiological substrate for sulphatase A. The Km is 11.6 mM for cyclic AMP. On polyacrylamide gel electrophoresis sulphatase A migrates as a single protein band which coincides with both the arylsulphatase and phosphodiesterase activities, suggesting that these are due to a single protein. Cyclic AMP competitively inhibits the arylsulphatase activity of sulphatase A, showing that both activities are associated with a single active site on the enzyme. sulphatase A also hydrolyses guanosine 3',5'-monophosphate, but not uridine 3',5'-monophosphate nor adenosine 2',3'-monophosphate.

References

Feb 19, 1975·Biochimica Et Biophysica Acta·A B Roy
Nov 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·G Lancelot, C Hélène
Jun 1, 1977·The Australian Journal of Experimental Biology and Medical Science·H J Jeffrey, A B Roy
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Jun 8, 2000·International Journal of Systematic and Evolutionary Microbiology·H XinT Nakase
Jun 1, 1964·Journal of Biochemistry·L W NICHOL, A B ROY

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Citations

Jan 1, 1984·Neurochemical Pathology·A A Farooqui, L A Horrocks
Mar 1, 1990·Molecular and Chemical Neuropathology·S N Shah
Apr 1, 1999·Chemistry & Biology·P J O'Brien, D Herschlag
Apr 18, 2009·Angewandte Chemie·Ann C BabtieFlorian Hollfelder

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