2012
DOI: 10.1016/j.bbapap.2012.07.014
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Radical SAM enzymes involved in the biosynthesis of purine-based natural products

Abstract: The radical S-adenosyl-L-methionine (SAM) superfamily is a widely distributed group of iron-sulfur containing proteins that exploit the reactivity of the high energy intermediate, 5’-deoxyadenosyl radical, which is produced by reductive cleavage of SAM, to carry-out complex radical-mediated transformations. The reactions catalyzed by radical SAM enzymes range from simple group migrations to complex reactions in protein and RNA modification. This review will highlight three radical SAM enzymes that catalyze rea… Show more

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Cited by 23 publications
(15 citation statements)
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References 69 publications
(78 reference statements)
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“…Of particular note is the presence of the radical S-adenosyl-l-methionine (SAM) protein (ID: BC346_05545) in this area. The radical SAM protein is a group of iron-sulfur containing proteins that exploit the reactivity of the high energy intermediate, the 5’-deoxyadenosyl radical, which is produced by reductive cleavage of SAM, to carry-out complex radical-mediated transformations [ 30 ]. In microorganisms, the activity of the radical SAM protein is very important for bacterial adaption to environmental niches and survival [ 31 , 32 ].…”
Section: Resultsmentioning
confidence: 99%
“…Of particular note is the presence of the radical S-adenosyl-l-methionine (SAM) protein (ID: BC346_05545) in this area. The radical SAM protein is a group of iron-sulfur containing proteins that exploit the reactivity of the high energy intermediate, the 5’-deoxyadenosyl radical, which is produced by reductive cleavage of SAM, to carry-out complex radical-mediated transformations [ 30 ]. In microorganisms, the activity of the radical SAM protein is very important for bacterial adaption to environmental niches and survival [ 31 , 32 ].…”
Section: Resultsmentioning
confidence: 99%
“…QueE along with other enzymes required for the initial steps of queuosine biosynthesis (QueC, QueD, QueF) were first identified in Bacillus subtilis by comparative genomics combined with experimental validation in Acinetobacter baylyi 31 . B. subtilis QueE was subsequently studied in detail and shown to be a CDG synthase 22 23 32 33 ( Supplementary Fig. 8 ).…”
Section: Discussionmentioning
confidence: 99%
“…The filamentous cells have a continuous cytoplasm and intact FtsZ rings, suggesting a block downstream of Z-ring formation in the cell division pathway. From a suppressor screen, we determined that filamentation depends on QueE, an enzyme involved in the biosynthesis of a hyper-modified guanosine (queuosine) found in certain tRNAs 22 23 . We further find that PhoP regulates queE transcription, and that increased expression of QueE inhibits cell division.…”
mentioning
confidence: 99%
“…80 In particular, radical SAM enzymes post-translationally modify many RiPPs through epimerization of L-to D-amino acids, 19,81 excision of tyramine to form a-keto moieties, 82 and formation of intramolecular crosslinks including strained cyclophane macrocycles. 83 Radical SAMs also play a role in the biosynthesis of hypermodied tRNA bases 84 and nucleoside-based natural products through C-C bond extension at C5 0 of ribose rings to connect nucleosides to structurally diverse functional groups. 85 A number of other enzyme classes not covered in detail here also were predicted to have remarkable across-EC-class reaction diversity.…”
Section: Hotbeds For Enzyme Discoverymentioning
confidence: 99%