Perspectives of Bacterial PAPS-Independent Aryl Sulfotransferases for Practical In Vitro Sulfation.

Authors

Katerina Brodsky, Barbora Petránková, Kristýna Slámová, Pavla Bojarová, Kateřina Valentová

Published in

Journal of agricultural and food chemistry. Jul 16, 2026. Epub Jul 16, 2026.

Abstract

PAPS-independent bacterial aryl sulfotransferases (ASTs) do not require the costly and unstable cofactor PAPS like mammalian sulfotransferases. Instead, they use simple aromatic sulfuryl donors. Originally discovered in intestinal bacteria, ASTs display remarkable substrate diversity, catalyzing sulfation of phenols, alcohols, amines, sugars, and polyphenols, including flavonoids and flavonolignans. Among them, AST from Desulfitobacterium hafniense (DhAST) is particularly notable for its stability and broad substrate range. Structural and mechanistic studies reveal that ASTs follow a ping-pong bibi mechanism with transient enzyme sulfation. Recent identification of new ASTs from diverse bacterial species and advances in recombinant expression have broadened the potential of these enzymes for selective and scalable synthesis of sulfated metabolites in vitro. Expanding the available AST library has deepened the understanding of bacterial sulfation pathways and supports their applications in biocatalysis, metabolite synthesis, and production of sulfated bioanalytical standards.

PMID:
42461780
Bibliographic data and abstract were imported from PubMed on 17 Jul 2026.

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