Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage.
Science
; 268(5216): 1487-9, 1995 Jun 09.
Article
em En
| MEDLINE
| ID: mdl-7770773
ABSTRACT
Macrocyclic polyketides exhibit an impressive range of medically useful activities, and there is great interest in manipulating the genes that govern their synthesis. The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain extension. The resulting mutant markedly accelerates formation of the predicted triketide lactone, compared to a control in which the repositioned domain is inactive. Repositioning of the cyclase should be generally useful for redirecting polyketide synthesis to obtain polyketides of specified chain lengths.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Engenharia de Proteínas
/
Saccharopolyspora
/
Complexos Multienzimáticos
Idioma:
En
Revista:
Science
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Reino Unido