期刊
BIOCHEMICAL JOURNAL
卷 415, 期 -, 页码 317-324出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20080369
关键词
4'-phosphopantetheinyl transferase (PPTase); lysine; beta-lactam antibiotics; post-translational modification; roquefortine; secondary metabolism
资金
- European Union (Eurofung II)
- DSM (Delft, Holland)
- Torres Quevedo Program [PTQ04-3-0411]
NRPSs (non-ribosomal peptide synthetases) and PKSs (polyketide synthases) require post-translational phosphopantetheinylation to become active. This reaction is catalysed by a PPTase (4'-phosphopantetheinyl transferase). The ppt gene of Penicillium chrysogenum, encoding a protein that shares 50 % similarity with the stand-alone large PPTases, has been cloned. This gene is present its a single copy in the genome of the wild-type and high-penicillin-producing strains (containing Multiple copies of the penicillin gene cluster). Amplification of the ppt gene produced increases in isopenicillin N and benzylpenicillin biosynthesis. A PPTase-defective mutant (Wis54-PPT-) was obtained. It required lysine and lacked pigment and penicillin production, but it still synthesized normal levels of roquefortine. The biosynthesis of roquefortine does not appear to involve PPTase-mediated modification of the synthesizing enzymes. The PPT- mutant did not require fatty acids, which indicates that activation of the fatty acid synthase is performed by it different PPTase. Complementation of Wis54-PPT- with the ppt gene restored lysine biosynthesis, pigmentation and penicillin production, which demonstrates the wide range of processes controlled by this gene.
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