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Biological Chemistry

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Volume 381, Issue 5-6 (Jun 2000)


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

Y.-Z. Xu / Y.-J. Li / H.-Y. Hu / R.-g. Hu / H. Wu / W.-Y. Liu
Published Online: 2005-07-05 | DOI: https://doi.org/10.1515/BC.2000.058


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, 1H-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.

About the article

Published Online: 2005-07-05

Published in Print: 2000-06-21

Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.058. Export Citation

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