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Plant ribosome-inactivating proteins specifically cleave an  N -glycosidic bond of a unique adenosine in the largest ribosomal RNA, releasing an adenine from ribosomes of different sources. Here,  1 H-nuclear magnetic resonance is used to analyze the enzymatic products of the A-chain of cinnamomin, a type-II ribosome-inactivating protein (RIP) acting on the nucleotides  in situ . The enzymatic activities of the RIP on nine nucleotides are compared. Cinnamomin A-chain can cleave the  N -glycosidic bond and release an adenine base from adenine nucleotides except 5′-ATP; however, it cannot act on 5′-GMP, 5′-CMP, and 5′-UMP. The A-chain in the mixture of cinnamomin A- and B-chain exhibits higher activity toward adenine nucleotides than the A-chain alone does, suggesting that the B-chain can conformationally stabilize the A-chain. Intact cinnamomin also exhibits lower activity toward adenine nucleotides. However, cinnamomin B-chain and heat-denatured intact cinnamomin cannot hydrolyze all the tested nucleotides. We conclude that hydrolysis of the  N -C glycosidic bond of nucleotide compounds by cinnamomin A-chain has a base preference, and the negatively charged phosphate group(s) reduces the recognition ability of the A-chain to adenine nucleotide.

Adenine Nucleotide N-Glycosidase Activity of the A-Chain of Cinnamomin Characterized by 1H-Nuclear Magnetic Resonance