| Description | S-adenosylmethionine-dependent nucleotide dehydratase RSAD2, also known as viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts [ , , , ].Human viperin is involved in antiviral defense, playing a major role in the cell antiviral state induced by type I and type II interferon [ ]. It catalyses the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism [, [ ]. The resulting ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication []. It displays antiviral effect against a wide range of DNA and RNA viruses, such as HIV-1 virus, hepatitis C virus, human cytomegalovirus, and alphaviruses, but not vesiculovirus [, , , , , ]. | Name | S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 |
| Short Name | RSAD2 | Type | Family |
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