Tailoring the P450 Monooxygenase Gene for FR-008/Candicidin Biosynthesis

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Tailoring the P450 monooxygenase gene for FR-008/candicidin biosynthesis.

Tailoring steps are often important for the activity of mature antibiotics. Here, we report that novel decarboxylated FR-008/candicidin derivatives were obtained from the P450 monooxygenase gene fscP mutant of Streptomyces sp. strain FR-008. The toxicity of decarboxylated FR-008/candicidin derivatives has been shown to be greatly reduced compared to that of wild-type FR-008/candicidin.

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Biosynthesis, Encodes a Putative Cytochrome P450 Monooxygenase

Phytoalexins are low molecular weight antimicrobial compounds that are synthesized in response to pathogen attack. The phytoalexin camalexin, an indole derivative, is produced by Arabidopsis in response to infection with the bacterial pathogen Pseudomonas syringae. The phytoalexin deficient 3 ( pad3 ) mutation, which causes a defect in camalexin production, has no effect on resistance to P. syr...

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Arabidopsis PAD3, a gene required for camalexin biosynthesis, encodes a putative cytochrome P450 monooxygenase.

Phytoalexins are low molecular weight antimicrobial compounds that are synthesized in response to pathogen attack. The phytoalexin camalexin, an indole derivative, is produced by Arabidopsis in response to infection with the bacterial pathogen Pseudomonas syringae. The phytoalexin deficient 3 (pad3) mutation, which causes a defect in camalexin production, has no effect on resistance to P. syrin...

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The P450 monooxygenase BcABA1 is essential for abscisic acid biosynthesis in Botrytis cinerea.

The phytopathogenic ascomycete Botrytis cinerea is known to produce abscisic acid (ABA), which is thought to be involved in host-pathogen interaction. Biochemical analyses had previously shown that, in contrast to higher plants, the fungal ABA biosynthesis probably does not proceed via carotenoids but involves direct cyclization of farnesyl diphosphate and subsequent oxidation steps. We present...

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Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity.

A ferredoxin associated with biological Fe-S cluster assembly has been remodelled to transfer electrons to a P450 enzyme and support substrate oxidation at 80% of the physiological ferredoxin activity, opening up the possibility of tailoring ferredoxins to reconstitute the activity of P450 enzymes for which the electron transfer partner proteins are not known.

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ژورنال

عنوان ژورنال: Applied and Environmental Microbiology

سال: 2009

ISSN: 0099-2240,1098-5336

DOI: 10.1128/aem.00859-08