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Titolo:
Alternative modular polyketide synthase expression controls macrolactone structure
Autore:
Xue, YQ; Sherman, DH;
Indirizzi:
Univ Minnesota, Dept Microbiol, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 robiol, Minneapolis, MN 55455 USA Univ Minnesota, Biol Proc Technol Inst, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 l Inst, Minneapolis, MN 55455 USA
Titolo Testata:
NATURE
fascicolo: 6769, volume: 403, anno: 2000,
pagine: 571 - 575
SICI:
0028-0836(20000203)403:6769<571:AMPSEC>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
STREPTOMYCES-VENEZUELAE; BIOSYNTHESIS; ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Sherman, DH Univ Minnesota, Dept Microbiol, Box 196,1460 Mayo Mem Bldg, Minneapolis, MN 55455 USA Univ Minnesota Box 196,1460 Mayo Mem Bldg Minneapolis MN USA 55455
Citazione:
Y.Q. Xue e D.H. Sherman, "Alternative modular polyketide synthase expression controls macrolactone structure", NATURE, 403(6769), 2000, pp. 571-575

Abstract

Modular polyketide synthases are giant multifunctional enzymes that catalyse the condensation of small carboxylic acids such as acetate and propionate into structurally diverse polyketides that possess a spectrum of biological activities(1,2). In a modular polyketide synthase, an enzymatic domain catalyses a specific reaction, and three to six enzymatic domains involved in a condensation-processing cycle are organized into a module(3). A fundamental aspect of a modular polyketide synthase is that its module arrangementlinearly specifies the structure of its polyketide product(3). Here we report a natural example in which alternative expression of the pikromycin polyketide synthase results in the generation of two macrolactone structures. Expression of the full-length modular polyketide synthase PikAIV in Streptomyces venezuelae generates the 11-membered ring macrolactone narbonolide, whereas expression of the amino-terminal truncated form of PikAIV leads to 'skipping' of the final condensation cycle in polyketide biosynthesis to generate the 12-membered ring macrolactone 10-deoxymethynolide. Our findings provide insight into the structure and function of modular polyketide synthases, as well as a new set of tools to generate structural diversity in polyketide natural products.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 01:58:02