From f6aa97d4360d6f522ea2b19df105aa248871414d Mon Sep 17 00:00:00 2001
From: Remi PLANEL <rplanel@pasteur.fr>
Date: Wed, 20 Dec 2023 18:54:38 +0100
Subject: [PATCH] Update viperin.md
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content/3.defense-systems/viperin.md | 2 +-
1 file changed, 1 insertion(+), 1 deletion(-)
diff --git a/content/3.defense-systems/viperin.md b/content/3.defense-systems/viperin.md
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@@ -25,7 +25,7 @@ Recently, Â Viperin-like enzymes were found in prokaryotes (pVips). Â Strikingly
## Molecular mechanism
-!Figure1](/viperin/human_vip.jpg){max-width=750px}
+{max-width=750px}
Fig.1: Catalytic activity of human Viperin generates ddhCTP :ref{doi=10.1002/1873-3468.13778}
Viperins are members of the radical S-adenosylmethionine (rSAM) superfamily. This group of enzymes use a [4Fe-4S] cluster to cleave S-adenosylmethionine (SAM) reductively, generating a radical which is generally transferred to a substrate. It was demonstrated that through their [4Fe-4S] cluster catalytic activity, eukaryotic viperins convert a ribonucleotide, the cytidine triphosphate (CTP) into a modified ribonucleotide, the 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) :ref{doi=10.1038/s41586-018-0238-4}.Â
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