Abstract
Sulfation plays important roles in various biological systems, however, tailoring modification by sulfation is relatively less common in bacterial natural products. Totopotensamide C (TPM C) was the sulfated derivative of Totopotensamide A (TPM A), a polyketide-peptide glycoside. Herein we report the genetic and biochemical characterization of TotS as a 3′-phosphoadenosine-5′-phosphosulfate (PAPS)-dependent sulfotransferase to append the sulfate to phenolic hydroxyl of TPM A to form TPM C. TotS also acts on TPM B to afford a new sulfated analogue. Key amino acid residues involved in substrate and cofactor binding of TotS were identified by homology modeling and site-directed mutagenesis. This study sets a stage to further expand the structural diversity of TPMs by sulfation.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
