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Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus
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Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus
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Journal Article
Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus
2025
Overview
Amide synthases catalyze the formation of macrolactam rings from aniline-containing polyketide-derived seco-acids as found in the important class of ansamycin antibiotics. One of these amide synthases is the geldanamycin amide synthase GdmF, which we recombinantly expressed, purified and studied in detail both functionally as well as structurally. Here we show that purified GdmF catalyzes the amide formation using synthetically derived substrates. The atomic structures of the ligand-free enzyme and in complex with simplified substrates reveal distinct structural features of the substrate binding site and a putative role of the flexible interdomain region for the catalysis reaction.
Amide synthases catalyse the formation of macrolactam rings from aniline-containing polyketide-derived
seco
-acids. In this study, the authors solved the crystal structure of the geldanamycin amide synthase GdmF and demonstrated that it catalyses amide formation using synthetically derived substrates.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 140/131
/ Amide Synthases - metabolism
/ Aniline
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Enzymes
/ Humanities and Social Sciences
/ Lactams, Macrocyclic - chemistry
/ Lactams, Macrocyclic - metabolism
/ Ligands
/ Proteins
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Science
