Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 523-527 |
| Seitenumfang | 5 |
| Fachzeitschrift | Chemical science |
| Jahrgang | 5 |
| Ausgabenummer | 2 |
| Publikationsstatus | Veröffentlicht - 1 Feb. 2014 |
Abstract
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.
ASJC Scopus Sachgebiete
- Chemie (insg.)
- Allgemeine Chemie
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in: Chemical science, Jahrgang 5, Nr. 2, 01.02.2014, S. 523-527.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Oxidative dearomatisation
T2 - The key step of sorbicillinoid biosynthesis
AU - Al Fahad, Ahmed
AU - Abood, Amira
AU - Fisch, Katja M.
AU - Osipow, Anna
AU - Davison, Jack
AU - Avramović, Marija
AU - Butts, Craig P.
AU - Piel, Jörn
AU - Simpson, Thomas J.
AU - Cox, Russell J.
PY - 2014/2/1
Y1 - 2014/2/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84891399774&partnerID=8YFLogxK
U2 - 10.1039/c3sc52911h
DO - 10.1039/c3sc52911h
M3 - Article
AN - SCOPUS:84891399774
VL - 5
SP - 523
EP - 527
JO - Chemical science
JF - Chemical science
SN - 2041-6520
IS - 2
ER -