Publications by authors named "Sofie Dekimpe"
Article Synopsis
- Bacterial trans-acyltransferase polyketide synthases (trans-AT PKSs) are large enzymes that create various bioactive compounds, including anticancer agents like oximidine.
- Researchers identified the gene cluster for oximidine in the bacterium Pseudomonas baetica and discovered four new variants, highlighting a simpler intermediate with strong anticancer properties.
- The study also detailed the oximidine biosynthesis process, revealing a unique mechanism for forming O-methyloxime involving a specific monooxygenase and methyltransferase, expanding knowledge on trans-AT PKSs and their potential for creating new drug variants.
Covering: up to the end of 2020Nonribosomal peptide synthetases are remarkable molecular machines that produce a wide range of structurally complex peptide natural products with important applications in medicine and agriculture. Condensation domains play a central role in these biosynthetic pathways by catalysing amide bond formation between various aminoacyl substrates. In recent years, however, it has become increasingly clear that the catalytic repertoire of C domains extends far beyond conventional peptide bond formation.
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