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

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

Volume: 10 Issue: 5

Author(s): Hong Xu and Wang-Yi Liu

Affiliation:

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

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.

Cite this article as:

Xu Hong and Liu Wang-Yi, The Role Of Tyrosine Residues In The Rna N-Glycosidase Activity Of Cinnamomin A-Chain, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478771

DOI https://dx.doi.org/10.2174/0929866033478771	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305