Abstract
An adenosine (phosphate) deaminase from the squid liver had much lower activity for 5'-deoxyadenosine than that for adenosine, 2'-, or 3'-deoxyadenosine. 3'-IMP and inosine as well as purine riboside and adenine competitively inhibited the deamination of adenosine 3'-phenylphosphonate by the enzyme, but 5'-AMP and 5'-IMP did not. The enzyme deaminated the 5'-hydroxyl terminal adenosine residue in dinucleotides and trinucleotide, but not the 3'-hydroxyl terminal one in dinucleotides. The 5'-hydroxyl group of the ribose moiety was necessary for the substrate binding and catalytic activity of the squid enzyme. These results indicated that the recognition of ribose moiety in the substrate by the squid enzyme might be intermediate between those by adenosine deaminase and adenosine (phosphate) deaminase from microorganisms.
