Purification and properties of adenosine 5'-phophosulfate deaminating enzyme from marine macroalga Gloiopeltis furcata

An enzyme which catalyzed the hydrolytic removal of the 6-amino group of adenosine 5'-phosphosulfate (APS) into inosine 5'-phosphosulfate was purified from the marine red macroalga Gloioeltis furcata by means of salt fractionation, affinity, anion-exchange, and hydrophobic interaction chromatographies. The native enzyme had a M(r) of about 285000. Dissociation yielded a form with a M(r) of about 70000. The enzyme catalyzed the irreversible deamination of adenosine and its 5'-substituted compounds in addition to APS. Thus the enzyme seemed to be a nonspecific adenine nucleotide deaminase. Some properties were determined and compared with those of other nonspecific adenine nucleotide deaminases.