Functional characterization of the sulfotransferase TotS in totopotensamide biosynthesis

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 th...

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Bibliographic Details
Published in:Tetrahedron 2022-11, Vol.127, p.133103, Article 133103
Main Authors: Tan, Bin, Zhang, Qingbo, Zhang, Liping, Zhu, Yiguang, Zhang, Changsheng
Format: Article
Language:English
Subjects:
Biosynthesis
PAPS
Sulfotransferase
Totopotensamides
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Summary: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. [Display omitted]
ISSN:0040-4020
1464-5416
DOI:10.1016/j.tet.2022.133103