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• W2562550142 startingPage "2849" @default.
• W2562550142 abstract "The chemical complexity and biological activity of the glycopeptide antibiotics (GPAs) stems from their unique crosslinked structure, which is generated by the actions of cytochrome P450 (Oxy) enzymes that affect the crosslinking of aromatic side chains of amino acid residues contained within the GPA heptapeptide precursor. Given the crucial role peptide cyclisation plays in GPA activity, the characterisation of this process is of great importance in understanding the biosynthesis of these important antibiotics. Here, we report the cyclisation activity and crystal structure of StaF, the D- O -E ring forming Oxy enzyme from A47934 biosynthesis. Our results show that the specificity of StaF is reduced when compared to Oxy enzymes catalysing C- O -D ring formation and that this activity relies on interactions with the non-ribosomal peptide synthetase via the X-domain. Despite the interaction of StaF with the A47934 X-domain being weaker than for the preceding Oxy enzyme StaH, StaF retains higher levels of in vitro activity: we postulate that this is due to the ability of the StaF/X-domain complex to allow substrate reorganisation after initial complex formation has occurred. These results highlight the importance of testing different peptide/protein carrier constructs for in vitro GPA cyclisation assays and show that different Oxy homologues can display significantly different catalytic propensities despite their overall similarities." @default.
• W2562550142 created "2017-01-06" @default.
• W2562550142 creator A5007731083 @default.
• W2562550142 creator A5083774401 @default.
• W2562550142 creator A5091811974 @default.
• W2562550142 date "2016-12-27" @default.
• W2562550142 modified "2023-10-01" @default.
• W2562550142 title "Biochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934" @default.
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• W2562550142 doi "https://doi.org/10.3762/bjoc.12.284" @default.
• W2562550142 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5238595" @default.
• W2562550142 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28144358" @default.
• W2562550142 hasPublicationYear "2016" @default.
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