The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides
详细信息 查看全文
- 作者：Laura Vieweg ; Julian Kretz ; Alexander Pesic ; Dennis Kerwat ; Stefan Gr盲tz ; Monique Royer ; St茅phane Cociancich ; Andi Mainz ; Roderich D. S眉ssmuth
- 刊名：Journal of the American Chemical Society
- 出版年：2015
- 出版时间：June 24, 2015
- 年：2015
- 卷：137
- 期：24
- 页码：7608-7611
- 全文大小：265K
- ISSN：1520-5126
文摘
The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria. The bacterium Pantoea dispersa expresses the hydrolase AlbD, conferring natural resistance against albicidin. We show that AlbD is a novel type of endopeptidase that catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimicrobial activity. Additionally, we determined the minimal cleavage motif of AlbD with substrates derived by chemical synthesis. Our results clearly identify AlbD as a unique endopeptidase that is the first member of a new subfamily of peptidases. Our findings provide the molecular basis for a natural detoxification mechanism, potentially rendering a new tool in biological chemistry approaches.