ReviewFrontiers in chemistry2016
Catalytic Promiscuity of the Radical S-adenosyl-L-methionine Enzyme NosL.
Review in Frontiers in chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed.
- Initiation, Propagation, and Termination in the Chemistry of Radical SAM Enzymes.Biochemistry · 2024Review
- Discovery and Biosynthesis of Persiathiacins: Unusual Polyglycosylated Thiopeptides Active Against Multidrug Resistant Tuberculosis.ACS infectious diseases · 2024Article
- Review
- A roadmap for metagenomic enzyme discovery.Natural product reports · 2021Review
- Identification ofMicroorganisms · 2021Article
- Current Advancements in Sactipeptide Natural Products.Frontiers in chemistry · 2021Review
- ICBS 2017 in Shanghai-Illuminating Life with Chemical Innovation.ACS chemical biology · 2018Article
- Mechanistic Studies on Tryptophan Lyase (NosL): Identification of Cyanide as a Reaction Product.Journal of the American Chemical Society · 2018Article
- Biosynthesis of the nosiheptide indole side ring centers on a cryptic carrier protein NosJ.Nature communications · 2017Article
- Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides (RiPPs).Frontiers in chemistry · 2017Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Catalytic promiscuity plays a key role in enzyme evolution and the acquisition of novel biological functions. Because of the high reactivity of radical species, in our view enzymes involving radical-mediated mechanisms could intrinsically be more prone to catalytic promiscuity. This mini-review summarizes the recent advances in the study of NosL, a radical S-adenosyl-L-methionine (SAM)-dependent L-tryptophan (L-Trp) lyase. We demonstrate here the interesting chemistry and remarkable catalytic promiscuity of NosL, and attempt to highlight the high evolvability of radical SAM enzymes and the potential to engineer these enzymes for novel and improved activities.
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Registered trials
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