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Fredilyn Lipata

Researcher at University of Kentucky

Publications -  6
Citations -  427

Fredilyn Lipata is an academic researcher from University of Kentucky. The author has contributed to research in topics: Gene cluster & Gene. The author has an hindex of 6, co-authored 6 publications receiving 405 citations. Previous affiliations of Fredilyn Lipata include Medical University of South Carolina.

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Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus.

TL;DR: MtmOIV, the key oxygenase of the mithramycin biosynthetic pathway in Streptomyces argillaceus, was proven to act initially as Baeyer-Villiger monooxygenase, but may also catalyze various follow-up reaction steps.
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The complete gene cluster of the antitumor agent gilvocarcin V and its implication for the biosynthesis of the gilvocarcins.

TL;DR: This is the first reported gene cluster encoding the biosynthesis of a benzo[d]naphtho[1,2-b]pyran-6-one aryl C-glycoside antibiotic, which lays the foundation for the detailed studies of its intriguing biosynthetic steps and possibly for the generation of gilvocarcin analogues with improved biological activities through combinatorial biosynthesis.
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Rationally designed glycosylated premithramycins: hybrid aromatic polyketides using genes from three different biosynthetic pathways.

TL;DR: The results prove the unique substrate flexibility of the C-glycosyltransferase UrdGT2, which tolerates not only a variety of sugar-donor substrates, but also various acceptor substrate, and represent the first compounds, in which sugars were attached to a position that is normally unglycoslyated.
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The Oxidative Ring Cleavage in Jadomycin Biosynthesis: A Multistep Oxygenation Cascade in a Biosynthetic Black Box

TL;DR: These results demonstrate that both JadF and JadH display secondary dehydratase activities that contrary to their oxygenase activities, appear to be independent of the respective protein-complex binding partners.
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Digitoxosyltetracenomycin C and glucosyltetracenomycin C, two novel elloramycin analogues obtained by exploring the sugar donor substrate specificity of glycosyltransferase ElmGT.

TL;DR: The explorations of glycosyltransferase ElmGT from Streptomyces olivaceus Tü 2353, which shows an interesting flexibility regarding its sugar donor substrate, were extended toward various previously unexplored sugar co-substrates, revealing that ElmGT is able to process an activated non-deoxygenated sugar, NDP-D-glucose, as well as NDP-L-digitoxose.