Ring Contraction Catalyzed by the Metal-Dependent Radical SAM Enzyme: 7-Carboxy-7-deazaguanine Synthase from B. multivorans. Theoretical Insights into the Reaction Mechanism and the Influence of Metal Ions

ACS Catalysis ◽  
2015 ◽  
Vol 5 (7) ◽  
pp. 3953-3965 ◽  
Author(s):  
Wenyou Zhu ◽  
Yongjun Liu
Keyword(s):  
Reaction Mechanism ◽  
Metal Ions ◽  
Radical Sam ◽  
Ring Contraction ◽  
Radical Sam Enzyme

Characterization and Mechanistic Study of the Radical SAM Enzyme ArsS Involved in Arsenosugar Biosynthesis

2021 ◽  
Author(s):  
Jinduo Cheng ◽  
Wenjuan Ji ◽  
Suze Ma ◽  
Xinjian Ji ◽  
Zixin Deng ◽  
...  
Keyword(s):  
Mechanistic Study ◽  
Radical Sam ◽  
Radical Sam Enzyme

Characterization of the DNA repair spore photoproduct lyase enzyme from Clostridium acetobutylicum: A radical-SAM enzyme

2007 ◽  
Vol 10 (8) ◽  
pp. 756-765 ◽  
Author(s):  
Alexia Chandor ◽  
Thierry Douki ◽  
Didier Gasparutto ◽  
Serge Gambarelli ◽  
Yannis Sanakis ◽  
...  
Keyword(s):  
Dna Repair ◽  
Clostridium Acetobutylicum ◽  
Radical Sam ◽  
Spore Photoproduct Lyase ◽  
Radical Sam Enzyme ◽  
Spore Photoproduct

Evidence for the synthesis of an unusual high spin (S = 7/2) [Cu–3Fe–4S] cluster in the radical-SAM enzyme RSAD2 (viperin)

2018 ◽  
Vol 54 (62) ◽  
pp. 8614-8617 ◽  
Author(s):  
K. Honarmand Ebrahimi ◽  
C. Silveira ◽  
S. Todorovic
Keyword(s):  
High Spin ◽  
Radical Sam ◽  
Radical Sam Enzyme

We demonstrate the synthesis of an unusual high spin [Cu–3Fe–4S] cluster in the radical S-adenosylmethionine enzyme RSAD2 (also known as viperin).

Aerobic Enzymes and Their Radical SAM Enzyme Counterparts in Tetrapyrrole Pathways

Biochemistry ◽  
2018 ◽  
Vol 58 (2) ◽  
pp. 85-93 ◽  
Author(s):  
Bin Li ◽  
Jennifer Bridwell-Rabb
Keyword(s):  
Radical Sam ◽  
Radical Sam Enzyme ◽  
Aerobic Enzymes

scholarly journals Viperin: An ancient radical SAM enzyme finds its place in modern cellular metabolism and innate immunity

2020 ◽  
Vol 295 (33) ◽  
pp. 11513-11528 ◽  
Author(s):  
Soumi Ghosh ◽  
E. Neil G. Marsh
Keyword(s):  
Catalytic Activity ◽  
Antiviral Activity ◽  
Defense Mechanism ◽  
Viral Infections ◽  
Viral Proteins ◽  
Innate Immune ◽  
Radical Sam ◽  
Biochemical Processes ◽  
Cellular Processes ◽  
Radical Sam Enzyme

Viperin plays an important and multifaceted role in the innate immune response to viral infection. Viperin is also notable as one of very few radical SAM–dependent enzymes present in higher animals; however, the enzyme appears broadly conserved across all kingdoms of life, which suggests that it represents an ancient defense mechanism against viral infections. Although viperin was discovered some 20 years ago, only recently was the enzyme's structure determined and its catalytic activity elucidated. The enzyme converts CTP to 3′-deoxy-3′,4′-didehydro-CTP, which functions as novel chain-terminating antiviral nucleotide when misincorporated by viral RNA-dependent RNA polymerases. Moreover, in higher animals, viperin interacts with numerous other host and viral proteins, and it is apparent that this complex network of interactions constitutes another important aspect of the protein's antiviral activity. An emerging theme is that viperin appears to facilitate ubiquitin-dependent proteasomal degradation of some of the proteins it interacts with. Viperin-targeted protein degradation contributes to the antiviral response either by down-regulating various metabolic pathways important for viral replication or by directly targeting viral proteins for degradation. Here, we review recent advances in our understanding of the structure and catalytic activity of viperin, together with studies investigating the interactions between viperin and its target proteins. These studies have provided detailed insights into the biochemical processes underpinning this unusual enzyme's wide-ranging antiviral activity. We also highlight recent intriguing reports that implicate a broader role for viperin in regulating nonpathological cellular processes, including thermogenesis and protein secretion.

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