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Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the formation of the covalent enzyme–m 7 GMP intermediate
Author(s) -
Lin Hua-Yang,
Yu Chiao-Yuan,
Hsu Yau-Heiu,
Meng Menghsiao
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.05.024
Subject(s) - covalent bond , enzyme , gtp' , histidine , biochemistry , stereochemistry , residue (chemistry) , moiety , chemistry , nucleotide , biology , gene , organic chemistry
The alphavirus‐like mRNA capping enzyme of Bamboo mosaic virus (BaMV) exhibits an AdoMet‐dependent guanylyltransferase activity by which the methyl group of AdoMet is transferred to GTP, leading to the formation of m 7 GTP, and the m 7 GMP moiety is next transferred to the 5′ end of ppRNA via a covalent enzyme–m 7 GMP intermediate. The function of the conserved H68 of the BaMV capping enzyme in the intermediate formation was analyzed by mutagenesis in this study. The nature of the bond linking the enzyme and m 7 GMP was changed in the H68C mutant protein, strongly suggesting that H68 covalently binds to m 7 GMP in the intermediate.