ArticleChembiochem : a European journal of chemical biology2025
Exploring the Substrate Flexibility of GrsB Thioesterase Leads to the Structural Reassignment of a Gramicidin S Variant.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Reprogramming the enduracidin NRPS assembly line via thioesterase domain relocation.Synthetic and systems biotechnology · 2027Article
- Exploring the Substrate Flexibility of GrsB Thioesterase Leads to the Structural Reassignment of a Gramicidin S Variant.Chembiochem : a European journal of chemical biology · 2025Article
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9 authors.
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Abstract
Gramicidin S (GS) is a cyclic decapeptide derived from two pentapeptides. The C-terminal thioesterase (TE) domain of gramicidin S synthetase B (GrsB) dimerizes precursor pentapeptides and cyclizes the resulting linear decapeptide. Recently, a GS variant (GS-SA), in which a single D-Phe is replaced by L-Ser(Allyl), is reported via precursor-directed biosynthesis in a native GS producer. To understand how GrsB-TE processes such modified precursors, its substrate specificity using synthetic linear peptides is investigated. GrsB-TE cyclizes a substrate containing L-Ser(Allyl) at position 6 but not at position 1. However, the enzymatically synthesized GS-SA shows a different high-performance liquid chromatography retention time than that of the reported GS variant. Further structural and functional analyses, including
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