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The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases.
TLDR
General rules for the structural basis of substrate recognition in adenylation domains of multimodular peptide synthetases can be used to rationally alter the specificity of adenyation domains and to predict from the primary sequence the Specificity of biochemically uncharacterized adenYLation domains. Expand
Siderophore-Based Iron Acquisition and Pathogen Control
TLDR
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. Expand
A new enzyme superfamily - the phosphopantetheinyl transferases.
TLDR
This work has identified a large family of proteins having 12-22 % similarity with ACPS, which are putative P-pant transferases, and found three of these proteins, E. coli EntD and o195, and subtilis Sfp, have been overproduced, purified and found to have P- pant transferase activity. Expand
Biosynthesis of nonribosomal peptides
TLDR
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. Expand
Structural basis for the activation of phenylalanine in the non‐ribosomal biosynthesis of gramicidin S
TLDR
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. Expand
Nonribosomal peptides: from genes to products.
TLDR
This review focuses on recent results in NRPS research and highlights how this knowledge can be exploited for biotechnological purposes. Expand
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
TLDR
These findings place proline isomerases at the intersection of protein folding, signal transduction, trafficking, assembly and cell cycle regulation. Expand
A superfamily of proteins that contain the cold-shock domain.
TLDR
The discovery of a domain--the cold-shock domain--that shows strikingly high homology and similar RNA-binding properties to CSPs in a growing number of eukaryotic nucleic-acid-binding proteins suggests that these proteins have an ancient origin. Expand
Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. TheExpand
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