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Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93

Zugehörigkeit
Institute of Microbiology, Microbial Phytopathology, University of Jena, Germany
Braun, S. D.;
Zugehörigkeit
Institute of Microbiology, Microbial Phytopathology, University of Jena, Germany
Hofmann, J.;
GND
1059102854
Zugehörigkeit
Julius Kühn-Institute (JKI), Institute for Plant Protection in Fruit Crops and Viticulture, Germany; Jacobs University Bremen, School of Engineering and Science, Bremen, Germany
Wensing, Annette;
Zugehörigkeit
Jacobs University Bremen, School of Engineering and Science, Bremen, Germany
Ullrich, M. S.;
Zugehörigkeit
Jacobs University Bremen, School of Engineering and Science, Bremen, Germany
Weingart, H.;
Zugehörigkeit
Institute of Microbiology, Microbial Phytopathology, University of Jena, Germany
Völksch, B.;
Zugehörigkeit
Max Planck Institute for Chemical Ecology, Bioorganic Chemistry, Jena, Germany
Spiteller, D.

The epiphyte Pseudomonas syringae pv. syringae 22d/93 (Pss22d) produces the rare amino acid 3-methylarginine (MeArg), which is highly active against the closely related soybean pathogen Pseudomonas syringae pv. glycinea. Since these pathogens compete for the same habitat, Pss22d is a promising candidate for biocontrol of P. syringae pv. glycinea. The MeArg biosynthesis gene cluster codes for the S-adenosylmethionine (SAM)-dependent methyltransferase MrsA, the putative aminotransferase MrsB, and the amino acid exporter MrsC. Transfer of the whole gene cluster into Escherichia coli resulted in heterologous production of MeArg. The methyltransferase MrsA was overexpressed in E. coli as a His-tagged protein and functionally characterized (K(m), 7 mM; k(cat), 85 min(-1)). The highly selective methyltransferase MrsA transfers the methyl group from SAM into 5-guanidino-2-oxo-pentanoic acid to yield 5-guanidino-3-methyl-2-oxo-pentanoic acid, which then only needs to be transaminated to result in the antibiotic MeArg

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