Aspects of the biosynthesis of non-aromatic fungal polyketides by iterative polyketide synthases.
In: Antonie van Leeuwenhoek, Jg. 78 (2000-12-01), Heft 3/4, S. 287-295
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Zugriff:
Lovastatin biosynthesis in Aspergillus terreus involves two unusual type I multifunctional polyketide syntheses (PKSs). Lovastatin nonaketide synthase (LNKS), the product of the lovB gene, is an iterative PKS that interacts with LovC, a putative enoyl reductase, to catalyze the 35 separate reactions in the biosynthesis of dihydromonacolin L, a lovastatin precursor. LNKS also displays Diels-Alderase activity in vitro. Lovastatin diketide synthase (LDKS) made by lovF, in contrast, acts non-iteratively like the bacterial modular PKSs to make (2 R)-2–methylbutyric acid. Then, like LNKS, LDKS interacts closely with another protein, the LovD transesterase enzyme that catalyzes attachment of the 2–methylbutyric acid to monacolin J in the final step of the lovastatin pathway. Key features of the genes for these four enzymes and others, plus the regulatory and self-resistance factors involved in lovastatin production, are also described. [ABSTRACT FROM AUTHOR]
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Titel: |
Aspects of the biosynthesis of non-aromatic fungal polyketides by iterative polyketide synthases.
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Autor/in / Beteiligte Person: | Hutchinson, C. ; Kennedy, Jonathan ; Park, Cheonseok ; Kendrew, Steven ; Auclair, Karine ; Vederas, John |
Link: | |
Zeitschrift: | Antonie van Leeuwenhoek, Jg. 78 (2000-12-01), Heft 3/4, S. 287-295 |
Veröffentlichung: | 2000 |
Medientyp: | academicJournal |
ISSN: | 0003-6072 (print) |
DOI: | 10.1023/A:1010294330190 |
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