DISTRIBUTION OF ADENOSINE (PHOSPHATE) DEAMINASES WITH UNUSUAL SUBSTRATE-SPECIFICITY IN MARINE MOLLUSKS

Crude preparations of nine species of marine molluscs converted adenos ine 3'-phenylphosphonate to inosine 3'-phenylphosphate . An enzyme hig hly purified from Batillus cornutus, a gastropod, and an enzyme partly purified from Meretrix lusoria, a bivalve, had activities toward aden osine and 3'-phosphorylated adenosines, but little or none for 5'-phos phorylated adenosines. These results, considering together with the pr evious results for the adenosine (phosphate) deaminase from Todarodes pacificus, a cephalopod, reported elsewhere, suggest that a class of a denosine (phosphate) deaminases with this substrate specificity might be widely distributed in marine molluscs. (C) 1998 Elsevier Science In c.