Natural noncanonical protein splicing yields products with diverse b-amino acid residues

التفاصيل البيبلوغرافية
العنوان: Natural noncanonical protein splicing yields products with diverse b-amino acid residues
المؤلفون: Maximilian J. Helf, James Sims, Jörn Piel, Brandon I. Morinaka, Anna L. Vagstad, Muriel Gugger, Shinichi Sunagawa, Marjan Verest, Edgars Lakis, Thibault Scalvenzi
المساهمون: Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Collection des Cyanobactéries, Institut Pasteur [Paris] (IP), J.P. thanks the Swiss National Science Foundation (31003A_146992/1) and the European Union (SYNPEPTIDE and European Research Council Advanced Grant 'SynPlex') for support. S.S. is grateful for financial support by the Helmut Horten Foundation. B.I.M. was the recipient of an Alexander von Humboldt Fellowship. A.L.V. was the recipient of an ETH Postdoctoral Fellowship., European Project: 613981,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,SYNPEPTIDE(2013), Institut Pasteur [Paris]
المصدر: Science
Science, 2018, 359 (6377), pp.779-782. ⟨10.1126/science.aao0157⟩
Science, American Association for the Advancement of Science, 2018, 359 (6377), pp.779-782. ⟨10.1126/science.aao0157⟩
بيانات النشر: HAL CCSD, 2018.
سنة النشر: 2018
مصطلحات موضوعية: 0301 basic medicine, MESH: Amino Acids, MESH: Mutation, Tyramine, MESH: Amino Acid Sequence, 010402 general chemistry, medicine.disease_cause, Cyanobacteria, 01 natural sciences, MESH: Genetic Loci, 03 medical and health sciences, chemistry.chemical_compound, Biosynthesis, Bacterial Proteins, Protein splicing, MESH: Protein Splicing, medicine, Escherichia coli, Protein Splicing, Amino Acid Sequence, Amino Acids, Peptide sequence, MESH: Bacterial Proteins, Bond cleavage, chemistry.chemical_classification, Multidisciplinary, Chemistry, MESH: Escherichia coli, MESH: Cyanobacteria, Ribosomal RNA, Amides, MESH: Amides, 0104 chemical sciences, Amino acid, 030104 developmental biology, Enzyme, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Biochemistry, Genetic Loci, MESH: Protein Processing, Post-Translational, Mutation, Protein Processing, Post-Translational, MESH: Tyramine
الوصف: Protein backbone, broken and mended Small, posttranslationally modified peptides are produced by microorganisms as antimicrobial agents or to communicate with neighboring cells. Alterations to the peptide backbone can change the structure of peptides or introduce reactive chemical moieties. Morinaka et al. characterized a bacterial enzyme that excises the side chain and α-carbon of a tyrosine residue from a short peptide, leaving behind an α-ketoamide. This backbone functional group is found in some protease inhibitors and is a valuable handle for bio-orthogonal chemistry. The enzyme accepts peptide substrates with a short recognition motif, suggesting that it could be used to generate libraries of modified peptides. Science , this issue p. 779
اللغة: English
تدمد: 0036-8075
1095-9203
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a6a19830fe9433d8efaa92f9373eb42
https://hal-pasteur.archives-ouvertes.fr/pasteur-02044549
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....8a6a19830fe9433d8efaa92f9373eb42
قاعدة البيانات: OpenAIRE