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Radical-Mediated Enzymatic Carbon Chain Fragmentation-Recombination
NosL catalyzed an unprecedented carbon chain reconstitution of L-Trp to give MIA, showing removal of the Cα-N unit and shift of the carboxylate to the indole ring, unveiling a key step in radical S-AdoMet enzyme-catalyzed structural rearrangements during complex biotransformations. Expand
An enzymatic [4+2] cyclization cascade creates the pentacyclic core of pyrroindomycins.
An unprecedented enzymatic [4+2] cyclization cascade that has a central role in the biosynthesis of pyrroindomycins, which are pentacyclic spirotetramate natural products is reported and it is confirmed that homologs are functionally exchangeable. Expand
Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis
Combined with the mutational analysis, these studies provide new insights into the function of the [4Fe-4S] cluster of radical AdoMet enzymes as well as the mechanism of the radical-mediated complex carbon chain rearrangement catalyzed by MIA synthase. Expand
An α/β-hydrolase fold protein in the biosynthesis of thiostrepton exhibits a dual activity for endopeptidyl hydrolysis and epoxide ring opening/macrocyclization
This study characterized a distinct α/β-hydrolase fold protein, TsrI, which exhibits the unprecedented dual activity for endopeptidyl hydrolysis and epoxide ring opening/macrocyclization and uncovered an unusual indirect mechanism of TSR-type thiopeptides, which are able to act against intracellular pathogens through host autophagy induction in addition to direct targeting of bacterial ribosome. Expand
FK506 Maturation Involves a Cytochrome P450 Protein-Catalyzed Four-Electron C-9 Oxidation in Parallel with a C-31 O-Methylation
It is clear that the modifications catalyzed by FkbD and FkbM are of importance to reach the full biological activity of FK506 by forming a key structure motif that is necessary for interaction of the molecule with the receptor and, subsequently, the downstream intracellular responses. Expand
Structural Insights into a Flavin-Dependent [4 + 2] Cyclase that Catalyzes trans-Decalin Formation in Pyrroindomycin Biosynthesis.
Structural insights are provided into PyrE3, a flavin-dependent [4 + 2] cyclase that catalyzes trans-decalin formation in the biosynthesis of pyrroindomycins and appears to selectively accommodate a tetramate-containing, linear polyene intermediate in a highly positively charged pocket. Expand
Concurrent modifications of the C-terminus and side ring of thiostrepton and their synergistic effects with respect to improving antibacterial activities
The double-mutant strain Streptomyces laurentii ΔtsrB/T was designed and constructed based on a recent understanding regarding the structure–activity relationship of thiostrepton (TSR) againstExpand
Identification and Characterization of a New Erythromycin Biosynthetic Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-Producing Halophilic Actinomycete Isolated from Salt
Erythromycins (Ers) are clinically potent macrolide antibiotics in treating pathogenic bacterial infections. Microorganisms capable of producing Ers, represented by Saccharopolyspora erythraea, areExpand
A linear hydroxymethyl tetramate undergoes an acetylation-elimination process for exocyclic methylene formation in the biosynthetic pathway of pyrroindomycins.
The isolation and characterization of a key linear intermediate in the biosynthetic pathway of pyrroindomycins, the potent spirotetramate natural products produced by Streptomyces rugosporus, are reported, indicating that a serine residue serves as the three-carbon unit for tetramate formation and chain-elongation termination. Expand
Insights into the thioamidation of thiopeptins to enhance the understanding of the biosynthetic logic of thioamide-containing thiopeptides.
It is illustrated through a series of in vivo experiments that the thioamide moiety of thiopeptins is generated posttranslationally by a TfuA-YcaO pair, encoded in theThiopeptin biosynthetic gene cluster, before the maturation of the th iopeptide bicyclic scaffold, enhancing the understanding of the biosynthetics logic of thIOamide-containing thiOPEptides. Expand