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The Role Of Tyrosine Residues In The Rna N-Glycosidase Activity Of Cinnamomin A-Chain

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Abstract:

Cinnamomin is a type II ribosome-inactivating protein (RIP) and its A-chain (CTA) is a RNA Nglycosidase. It is observed that modification of tyrosine residues by N-acetylimidazole (N-AI) causes almost complete loss of CTA activity. Adenine partially protects tyrosine residues from modification by NAI. It is proposed that tyrosine residues are involved in the active site of CTA and they are crucial in recognition and binding of ribosomal RNA. Tryptophan residues of CTA are also studied by NBS modification.

Keywords: chemical modification; cinnamomin; ribosome-inactivating protein; rna n-glycosidase; tryptophan residue; tyrosine residue

Document Type: Review Article

DOI: https://doi.org/10.2174/0929866033478771

Affiliations: State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Science. 320 Yue-yang Road, Shanghai 200031, China.

Publication date: 2003-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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