ArticleACS chemical biology2020
Substrate Promiscuity of a Paralytic Shellfish Toxin Amidinotransferase.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Discovery and Biosynthetic Characterization of Darumycins Expand the Chemical Space of Sesterterpene Antibiotics.JACS Au · 2026Article
- Hemolymph-Mediated Dynamics of Paralytic Shellfish Toxins and Tetrodotoxin in Scallops.Marine drugs · 2026Article
- An Alkaloid Biosynthetic Gene Bundle in Animals.Journal of the American Chemical Society · 2026Article
- Biosynthesis of guanidine-containing natural products in cyanobacteria.Journal of industrial microbiology & biotechnology · 2024Review
- Synthesis of Saxitoxin Biosynthetic Intermediates: Reveal the Mechanism for Formation of its Tricyclic Skeleton in Biosynthesis.Chemistry, an Asian journal · 2024Article
- Developing and enhancing promiscuous activity for NAD(P)H-dependent flavin reductase via elimination of cofactor.Heliyon · 2023Article
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- First Identification of 12β-Deoxygonyautoxin 5 (12α-Gonyautoxinol 5) in the CyanobacteriumMarine drugs · 2022Article
- EHreact: Extended Hasse Diagrams for the Extraction and Scoring of Enzymatic Reaction Templates.Journal of chemical information and modeling · 2021Article
- State-of-the-Art Biocatalysis.ACS central science · 2021Review
- Low Temperature and Cold Stress Significantly Increase Saxitoxins (STXs) and Expression of STX Biosynthesis GenesMarine drugs · 2021Article
- Chemoenzymatic Total Synthesis of Natural Products.Accounts of chemical research · 2021Review
- De novo Transcriptome of the Non-saxitoxin ProducingMarine drugs · 2020Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Secondary metabolites are assembled by enzymes that often perform reactions with high selectivity and specificity. Many of these enzymes also tolerate variations in substrate structure, exhibiting promiscuity that enables various applications of a given biocatalyst. However, initial enzyme characterization studies frequently do not explore beyond the native substrates. This limited assessment of substrate scope contributes to the difficulty of identifying appropriate enzymes for specific synthetic applications. Here, we report the natural function of cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins, and demonstrate its ability to modify a breadth of non-native substrates. In addition, we report the first X-ray crystal structure of SxtG, which provides rationale for this enzyme's substrate scope. Taken together, these data confirm the function of SxtG and exemplify its potential utility in biocatalytic synthesis.
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