title: Posttranslational Peptide-Modification Enzymes in Action: Key Roles for Leaders and Glutamate.
abstract: In this issue of Cell Chemical Biology, Ortega et al. (2016) determine the structure of another lantibiotic dehydratase with a tRNA(Glu)-dependent mechanism of modification. Moreover, they identify a common recognition motif involved in leader peptide binding in a number of different peptide-modification enzymes. These findings open up new mining possibilities and allow novel approaches in peptide engineering.
authors.affiliation: Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 7, 9747 AG Groningen, the Netherlands.
authors.forename: Manuel
authors.initials: M
authors.lastname: Montalbán-López
authors.affiliation: Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 7, 9747 AG Groningen, the Netherlands. Electronic address: o.p.kuipers@rug.nl.
authors.forename: Oscar P
authors.initials: OP
authors.lastname: Kuipers
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry; D001426:Bacterial Proteins / Q000378:metabolism; D001430:Bacteriocins / Q000737:chemistry*; D001665:Binding Sites; D004798:Enzymes / Q000235:genetics; D005798:Genes, Bacterial; D018698:Glutamic Acid / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D001430:Bacteriocins; D004798:Enzymes; D010455:Peptides; D021382:Protein Sorting Signals; D018698:Glutamic Acid