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Cover Feature: Mechanism of Diol Dehydration by a Promiscuous Radical‐SAM Enzyme Homologue of the Antiviral Enzyme Viperin (RSAD2) (ChemBioChem 11/2020)
Author(s) -
Honarmand Ebrahimi Kourosh,
Rowbotham Jack S.,
McCullagh James,
James William S.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000275
Subject(s) - nucleotide , enzyme , stereochemistry , chemistry , residue (chemistry) , biochemistry , tyrosine , diol , gene , organic chemistry
Nucleotide analogues lacking the 3’‐hydroxyl group have antiviral activity. The image illustrates the finding that a thermostable radical‐SAM enzyme catalyses transformation of natural and unnatural nucleotides to their 3’‐deoxy analogues by a mechanism requiring a proton‐coupled electron transfer step from a tyrosine residue. A nucleotide analogue synthesised by the enzyme is known to have broad‐spectrum antiviral activity in humans. The findings suggest a new enzymatic route for green biosynthesis of antiviral nucleotide analogues. More information can be found in the full paper by K. Honarmand Ebrahimi et al.