Non-ribosomal peptide synthesis

• Applicant: Professor Dr. Mohamed A. Marahiel
• Subject Area: Biochemistry
• Term: from 2009 to 2014
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 152010838

• Final Report Year: 2015

Final Report Abstract

No abstract available

Publications

• (2009) Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis. FEBS J. 276, 3669-3682
  Helmetag, V., Samel, S.A., Thomas, M.G., Marahiel, M.A. and Essen, L.-O.
  
• (2009) The structural diversity of acidic lipopeptide antibiotics. Chembiochem 10, 607-616
  Strieker, M. and Marahiel, M.A.
  
• (2009) TioS T-TE – a prototypical thioesterase responsible for cyclodimerization of the quinoline- and quinoxaline-type class of chromodepsipeptides. FEBS J. 276, 1641-1653
  Robbel, L., Hoyer, K.M. and Marahiel, M.A.
  
• (2009) Working outside the protein-synthesis rules: insights into nonribosomal peptide synthesis. J. Pept. Sci. 15, 799-807
  Marahiel, M.A.
  
• (2010) Daptomycin, a bacterial lipopeptide synthesized by a nonribosomal machinery. J. Biol. Chem. 285, 27501-27508
  Robbel, L. and Marahiel, M.
  
• (2010) Erythrochelin – a hydroxamate-type siderophore predicted from the genome of Saccharopolyspora erythraea. FEBS J. 277, 663-676
  Robbel, L., Knappe, T., Linne, U., Xiulan, Xie and Marahiel, M.A.
  
• (2010) Functional dissection of surfactin synthetase initiation module reveals insights into the mechanism of lipoinitiation. Chem. Biol. 17, 872-880
  Kraas, F.I., Helmetag, V., Wittmann, M., Strieker, M. and Marahiel, M.A.
  
• (2010) Nonribosomal peptide synthetases: structures and dynamics. Curr. Opin.Struct. Biol. 20, 234-240
  Strieker, M., Tanovic, A. and Marahiel, M.
  
• (2011) A four enzyme pathway for 3,5- dihydroxy-4-methyl-anthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin. Biochemistry 50, 5680-5692
  Giessen, T.W., Kraas, F.I. and Marahiel, M.A.
  
• (2011) Biosynthesis of the siderophore Rhodochelin requires the coordinated expression of three independent gene clusters in Rhodococcus jostii RHA1. J. Amer. Chem. Soc. 133, 4587-4595
  Bosello, M., Robbel, L., Linne, U., Xie, X. and Marahiel, M.
  
• (2011) Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin. Biochemistry 50, 6073-6080
  Robbel, L., Helmetag, V., Knappe, T.A. and Marahiel, M.A.
  
• (2011) Identification and characterization of the lysobactin biosynthetic gene cluster reveals mechanistic insights into an unusual termination module architecture. Chem. Biol. 18, 655-664
  Hou, J., Robbel, L. and Marahiel, M.A.
  
• (2012) An enzymatic pathway for the biosynthesis of the formylhydroxyornithine required for rhodochelin iron coordination. Biochemistry 51, 3059-3066
  Bosello, M., Mielcarek, A., Giessen, T.W. and Marahiel, M.A.
  (See online at https://doi.org/10.1021/bi201837f)
• (2012) Exploring the mechanism of lipid transfer during biosynthesis of the acidic lipopeptide antibiotic CDA. FEBS Lett. 586, 283-288
  Kraas, F.I., Giessen, T.W. and Marahiel, M.A.
  (See online at https://doi.org/10.1016/j.febslet.2012.01.003)
• (2012) Isolation, structure elucidation and biosynthesis of an unusual hydroxamic acid ester-containing siderophore from Actinosynnema mirum. J. Nat. Prod. 75, 905- 914
  Giessen, T.W., Franke, K.B., Knappe, T.A., Kraas, F.I., Bosello, M., Xie, X., Linne, U. and Marahiel, M.A.
  (See online at https://doi.org/10.1021/np300046k)
• (2013) Nonribosomal Peptide Synthesis. Handbook of Biologically Active Peptides. Chapter 21, S. 138-149. Adademic Press
  Grünewald, J. and Marahiel, M.A.
  
• (2013). Structural characterization of the heterobactin siderophores from Rhodococcus erythropolis PR4 and elucidation of their biosynthetic machinery. J. Nat. Products 76, 2382-2390
  Bosello, M., Zeyadi, M., Kraas, F.I., Linne, U., Xie, X. and Marahiel, M.A.
  (See online at https://doi.org/10.1021/np4006579)
• (2014) Crystal structure of a PCP/Sfp Complex reveals the structural basis for carrier protein posttranslational modification. Chem. Biol. 21, 552-5562
  Tufar, P., Rahighi, S., Kraas, F.I., Kirchner, D.K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M.A. and Dötsch, V.
  (See online at https://doi.org/10.1016/j.chembiol.2014.02.014)