ArticleBiochemistry2014
Structural studies of the spinosyn forosaminyltransferase, SpnP.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Sustainable Biocatalytic Cascades: A Versatile Tool in the Synthesis of Natural Products With Therapeutic Potential.Chembiochem : a European journal of chemical biology · 2026Review
- Enhancement of spinosad production in Saccharopolyspora spinosa by overexpression of the complete 74-kb spinosyn gene cluster.Microbial cell factories · 2025Article
- Developing a robust genome editing tool based on an endogenous type I-B CRISPR-Cas system in Saccharopolyspora spinosa.Science China. Life sciences · 2025Article
- The LysR family transcriptional regulator ORF-L16 regulates spinosad biosynthesis inSynthetic and systems biotechnology · 2024Article
- Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023Review
- Improving spinosad production by tuning expressions of the forosamine methyltransferase and the forosaminyl transferase to reduce undesired less active byproducts in the heterologous host Streptomyces albus J1074.Microbial cell factories · 2023Article
- Increasing the heterologous production of spinosad inSynthetic and systems biotechnology · 2021Article
- Midecamycin Is Inactivated by Several Different Sugar Moieties at Its Inactivation Site.International journal of molecular sciences · 2021Article
- Biochemical characterization of a glycosyltransferase Gtf3 from3 Biotech · 2020Article
- New Sipanmycin Analogues Generated by Combinatorial Biosynthesis and Mutasynthesis Approaches Relying on the Substrate Flexibility of Key Enzymes in the Biosynthetic Pathway.Applied and environmental microbiology · 2020Article
- Cooperative Involvement of Glycosyltransferases in the Transfer of Amino Sugars during the Biosynthesis of the Macrolactam Sipanmycin by Streptomyces sp. Strain CS149.Applied and environmental microbiology · 2018Article
- Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP.Nature chemical biology · 2018Article
- Natural [4 + 2]-Cyclases.Chemical reviews · 2017Review
- Computational study of a model system of enzyme-mediated [4+2] cycloaddition reaction.PloS one · 2015Article
- Chemoenzymatic synthesis of spinosyn A.Angewandte Chemie (International ed. in English) · 2014Article
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Authors and funding
5 authors.
Funding
Abstract
Spinosyns A and D (spinosad) are complex polyketide natural products biosynthesized through the cooperation of a modular polyketide synthase and several tailoring enzymes. SpnP catalyzes the final tailoring step, transferring forosamine from a TDP-D-forosamine donor substrate to a spinosyn pseudoaglycone acceptor substrate. Sequence analysis indicated that SpnP belongs to a small group of glycosyltransferases (GTs) that require an auxiliary protein for activation. However, unlike other GTs in this subgroup, no putative auxiliary protein gene could be located in the biosynthetic gene cluster. To learn more about SpnP, the structures of SpnP and its complex with TDP were determined to 2.50 and 3.15 Å resolution, respectively. Binding of TDP causes the reordering of several residues in the donor substrate pocket. SpnP possesses a structural feature that has only been previously observed in the related glycosyltransferase EryCIII, in which it mediates association with the auxiliary protein EryCII. This motif, H-X-R-X5-D-X5-R-X12-20-D-P-X3-W-L-X12-18-E-X4-G, may be predictive of glycosyltransferases that interact with an auxiliary protein. A reverse glycosyl transfer assay demonstrated that SpnP possesses measurable activity in the absence of an auxiliary protein. Our data suggest that SpnP can bind its donor substrate by itself but that the glycosyl transfer reaction is facilitated by an auxiliary protein that aids in the correct folding of a flexible loop surrounding the pseudoaglycone acceptor substrate-binding pocket.
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