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Publikováno v:
Biochemistry. 37:14937-14942
The post-polyketide synthase (PKS) biosynthetic tailoring of macrolide antibiotics usually involves one or more oxidation reactions catalyzed by cytochrome P450 monooxygenases. As the specificities of members from this class of enzymes vary significa
Autor:
Mary C. Betlach, Arinthip Thamchaipenet, Claes Gustafsson, Gary W. Ashley, Melanie C. Betlach, Robert Mcdaniel, Hong Fu
The structures of complex polyketide natural products, such as erythromycin, are programmed by multifunctional polyketide synthases (PKSs) that contain modular arrangements of functional domains. The colinearity between the activities of modular PKS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc329a3003149be498ed4d8a5a7320c0
https://europepmc.org/articles/PMC26699/
https://europepmc.org/articles/PMC26699/
Publikováno v:
Bioorganicmedicinal chemistry letters. 8(22)
The final step in the biosynthesis of methymycin, neomethymycin, and picromycin is an hydroxylation, shown to be carried out by the cytochrome P-450 monooxygenase, PicK. Direct comparison of the relative k cat K m values for the two substrates, YC-17
Publikováno v:
Chemistry & Biology. (8):553-558
Background A single modular polyketide synthase (PKS) gene cluster is responsible for production of both the 14-membered macrolide antibiotic picromycin and the 12-membered macrolide antibiotic methymycin in Streptomyces Venezuelas . Building on the