Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 333-335 |
| Seitenumfang | 3 |
| Fachzeitschrift | Chemical communications |
| Jahrgang | 46 |
| Ausgabenummer | 2 |
| Publikationsstatus | Veröffentlicht - 2010 |
| Extern publiziert | Ja |
Abstract
The structure of zeamine, a novel polyamino-amide antibiotic metabolite of Dickeya zeae has been established by NMR and detailed MS analyses; labelling studies with 13C-labelled acetates suggest that the repeating secondary amine containing motif may be biosynthesised via a modular PKS containing aminotransferase domains.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Werkstoffwissenschaften (insg.)
- Elektronische, optische und magnetische Materialien
- Werkstoffwissenschaften (insg.)
- Keramische und Verbundwerkstoffe
- Chemie (insg.)
- Allgemeine Chemie
- Werkstoffwissenschaften (insg.)
- Oberflächen, Beschichtungen und Folien
- Werkstoffwissenschaften (insg.)
- Metalle und Legierungen
- Werkstoffwissenschaften (insg.)
- Werkstoffchemie
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in: Chemical communications, Jahrgang 46, Nr. 2, 2010, S. 333-335.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - 13C Labeling reveals multiple amination reactions in the biosynthesis of a novel polyketide polyamine antibiotic zeamine from Dickeya zeae
AU - Wu, Jien
AU - Zhang, Hai Bao
AU - Xu, Jin Ling
AU - Cox, Russell J.
AU - Simpson, Thomas J.
AU - Zhang, Lian Hui
PY - 2010
Y1 - 2010
N2 - The structure of zeamine, a novel polyamino-amide antibiotic metabolite of Dickeya zeae has been established by NMR and detailed MS analyses; labelling studies with 13C-labelled acetates suggest that the repeating secondary amine containing motif may be biosynthesised via a modular PKS containing aminotransferase domains.
AB - The structure of zeamine, a novel polyamino-amide antibiotic metabolite of Dickeya zeae has been established by NMR and detailed MS analyses; labelling studies with 13C-labelled acetates suggest that the repeating secondary amine containing motif may be biosynthesised via a modular PKS containing aminotransferase domains.
UR - http://www.scopus.com/inward/record.url?scp=75649147683&partnerID=8YFLogxK
U2 - 10.1039/b916307g
DO - 10.1039/b916307g
M3 - Article
C2 - 20024369
AN - SCOPUS:75649147683
VL - 46
SP - 333
EP - 335
JO - Chemical communications
JF - Chemical communications
SN - 1359-7345
IS - 2
ER -