The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases.
- T. Stachelhaus, H. Mootz, M. Marahiel
- Biology, ChemistryChemistry and Biology
- 1 August 1999
Siderophore-Based Iron Acquisition and Pathogen Control
- M. Miethke, M. Marahiel
- BiologyMicrobiology and Molecular Biology Reviews
- 1 September 2007
General aspects of siderophore-mediated iron acquisition, recent findings regarding iron-related pathogen-host interactions, and current strategies for iron-dependent pathogen control will be reviewed.
Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis.
- M. Marahiel, T. Stachelhaus, H. Mootz
- BiologyChemical Reviews
- 10 November 1997
A new enzyme superfamily - the phosphopantetheinyl transferases.
- R. H. Lambalot, A. M. Gehring, C. Walsh
- BiologyChemistry and Biology
- 1996
Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
- P. G. Arnison, M. Bibb, W. A. van der Donk
- Biology, ChemistryNatural product reports (Print)
- 2013
This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The…
Structural basis for the activation of phenylalanine in the non‐ribosomal biosynthesis of gramicidin S
- E. Conti, T. Stachelhaus, M. Marahiel, P. Brick
- Biology, ChemistryEMBO Journal
- 15 July 1997
The structure of the N‐terminal adenylation subunit in a complex with AMP and L‐phenylalanine indicates a conserved mechanism of nucleotide binding and substrate activation and reveals the role of the invariant residues within the superfamily of adenYLate‐forming enzymes.
Biosynthesis of nonribosomal peptides
- Robert Finking, M. Marahiel
- Biology, Chemistry
- 19 March 2003
Along with the structure-function relationship of the core- and tailoring-domains of NRPSs, which is the main focus of this review, different biosynthetic strategies and essential enzymes for posttranslational modification and editing are discussed.
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
- S. Göthel, M. Marahiel
- BiologyCellular and Molecular Life Sciences (CMLS)
- 1 March 1999
These findings place proline isomerases at the intersection of protein folding, signal transduction, trafficking, assembly and cell cycle regulation.
A superfamily of proteins that contain the cold-shock domain.
- P. Graumann, M. Marahiel
- BiologyTIBS -Trends in Biochemical Sciences. Regular ed
- 1 August 1998
Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
- Jürgen J. May, N. Kessler, M. Marahiel, M. Stubbs
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 9 September 2002
Based on the structure and amino acid sequence alignments, an adapted specificity conferring code for aryl acid activating domains is proposed, allowing assignment of substrate specificity to gene products of previously unknown function.
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