ArticleChembiochem : a European journal of chemical biology2014
Synergistic actions of tailoring enzymes in pradimicin biosynthesis.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 12 citations in OpenAlex.
- Integrated Metabolomic and Genomic Insights into Amino Acid Incorporation Within the Hybrid Polyketide-Alkaloid Antibiotic TLN-05220.ACS chemical biology · 2026Article
- Integrated metabolomic and genomic insights into amino acid incorporation within the hybrid polyketide-alkaloid antibiotic TLN-05220.bioRxiv : the preprint server for biology · 2025Article
- Chemistry and biology of specialized metabolites produced byNatural product reports · 2024Review
- Three enzymes involved in the N-methylation and incorporation of the pradimicin sugar moieties.Bioorganic & medicinal chemistry letters · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Three key tailoring enzymes in pradimicin biosynthesis: PdmJ, PdmW, and PdmN, were investigated. PdmW was characterized as the C-6 hydroxylase by structural characterization of the corresponding product, 6-hydroxy-G-2A. The efficiencies of the C-5 and C-6 hydroxylations, catalyzed respectively by PdmJ and PdmW, were low when they were expressed individually with the early biosynthetic enzymes that form G-2A. When these two cytochrome P450 enzymes were co-expressed, a dihydroxylated product, 5,6-dihydroxy-G-2A, was efficiently produced, indicating that these two enzymes work synergistically in pradimicin biosynthesis. Heterologously expressed PdmN in Streptomyces coelicolor CH999 converted G-2A to JX137a by ligating a unit of D-alanine to the carboxyl group. PdmN has relaxed substrate specificity toward both amino acid donors and acceptors. Through combinatorial biosynthesis, a series of new pradimicin analogues were produced.
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