Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis

Autor:	Al-Fahad, Ahmed, Abood, Amira, Fisch, Katja M., Osipow, Anna, Davison, Jack, Avramovic, Marija, Butts, Craig, Piel, Joern, Simpson, Thomas J., Cox, Russell J.
Jazyk:	angličtina
Rok vydání:	2014
Předmět:	Dewey Decimal Classification::500 | Naturwissenschaften::540 | Chemie fungal polyketide pathway sorbicillactone polyketide synthase genes ddc:540 penicillium-chrysogenum gibberella-zeae verticillium-intertextum cluster trichoderma sp usf-2690 aspergillus-nidulans
Zdroj:	Chemical Science, 5 (2) Chemical Science 5 (2014), Nr. 2
ISSN:	2041-6520 2041-6539
Popis:	An FAD-dependent monooxygenase encoding gene (SorbC) was cloned from Penicillium chrysogenum E01-10/3 and expressed as a soluble protein in Escherichia coli. The enzyme efficiently performed the oxidative dearomatisation of sorbicillin and dihydrosorbicillin to give sorbicillinol and dihydrosorbicillinol respectively. Bioinformatic examination of the gene cluster surrounding SorbC indicated the presence of two polyketide synthase (PKS) encoding genes designated sorbA and sorbB. The gene sorbA-encodes a highly reducing iterative PKS while SorbB encodes a non-reducing iterative PKS which features a reductive release domain usually involved in the production of polyketide aldehydes. Using these observations and previously reported results from isotopic feeding experiments a new and simpler biosynthetic route to the sorbicillin class of secondary metabolites is proposed which is consistent with all reported experimental results. Chemical Science, 5 (2) ISSN:2041-6520 ISSN:2041-6539
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ed88313a1ead229dc2bf593eb35d11d https://hdl.handle.net/20.500.11850/78290 Zobrazit plný text záznamu