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Editorial
. 2022 Dec 5;2(6):538-547.
doi: 10.1021/acsbiomedchemau.2c00078. eCollection 2022 Dec 21.

Twenty Years of Radical SAM! The Genesis of the Superfamily

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Editorial

Twenty Years of Radical SAM! The Genesis of the Superfamily

Squire J Booker et al. ACS Bio Med Chem Au. .
No abstract available

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Figures

Figure 1
Figure 1
Formation of the 5′-deoxyadenosyl 5′-radical via intermediate omega.
Figure 2
Figure 2
Representative transformations catalyzed by RS enzymes.
Figure 3
Figure 3
Formation of 3′-deoxy-3′,4′-didehydro-CTP (ddhCTP) by viperin.
Figure 4
Figure 4
A full SSN of the RS Superfamily highlighting five megagroups (1–5) composed of multiple subgroups and five single subgroups. See radicalSAM.org and ref (6) for details on generating the SSN.
Figure 5
Figure 5
Reaction catalyzed by Mg-protoporphyrin IX monomethylester cyclase (BchE). Only the Mg-PME substrate and protochlorophyllide products are shown.
Figure 6
Figure 6
Structure of polytheonamide A, a RiPP natural product consisting of up to 18 methylations and 21 epimerizations catalyzed by just three RS enzymes (PoyB, PoyC, and PoyD). RS-dependent methylations are highlighted in orange (both bonds and one-letter codes), and epimerizations, to generate the D-configured residue, are shown in red (both bonds and one-letter codes).
Figure 7
Figure 7
Two pathways for the biosynthesis of the lipoyl cofactor. The classical pathway involves a protein composed of a single polypeptide (LIAS or LipA), which attaches sulfur at C6 first and then C8. The alternative pathway involves two proteins. LipS2 installs sulfur first at C8, while LipS1 subsequently installs sulfur at C6. In both pathways, octanoyllysyl-H-protein serves as the starting substrate.
Figure 8
Figure 8
Structures of the [MoFe]-nitrogenase (PDB: 6N59) (A) and the [FeFe]-hydrogenase (PDB: 1M1N) (B). Insets depict the metallocofactor that requires the participation of one or more RS enzymes (NifB for the MoFe cofactor and HydG/HydE for the H-cluster) for its assembly.
Figure 9
Figure 9
Reactions catalyzed by GDGT-MAS, GrsA, and GrsB, three RS enzymes that form bonds between two aliphatic sp3-hybridized carbon centers on hydrocarbons.

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References

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