A peptide dehydratase with core strength
Ribosomally synthesized and post-translationally modified peptide (RiPP) natural products typically rely on substrate recognition through remote protein–protein interaction sites. Now, an atypical dehydratase, whose activity is directed by neighboring azole modifications, has been shown to produce a...
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| Veröffentlicht in: | Nature chemical biology 2024-05, Vol.20 (5), p.546-548 |
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| creator | Richter, Daniel Vagstad, Anna Lisa |
| description | Ribosomally synthesized and post-translationally modified peptide (RiPP) natural products typically rely on substrate recognition through remote protein–protein interaction sites. Now, an atypical dehydratase, whose activity is directed by neighboring azole modifications, has been shown to produce a highly modified peptide hybrid bearing dehydroamino acids, enabling the synthesis of members of the dehydrazole family of RiPPs. |
| doi_str_mv | 10.1038/s41589-024-01605-5 |
| format | Article |
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| fulltext | fulltext |
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| ispartof | Nature chemical biology, 2024-05, Vol.20 (5), p.546-548 |
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| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | 631/45/611 Acids Biochemical Engineering Biochemistry Biology Bioorganic Chemistry Biosynthesis Catalysis Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Dehydration Dehydrogenases Enzymes Genomes Humans Hybrid bearings Hydro-Lyases - chemistry Hydro-Lyases - metabolism Natural products News & Views news-and-views Oxidation Peptides Peptides - chemistry Peptides - metabolism Pharmaceuticals Post-translation Proteins Specialty products Substrates |
| title | A peptide dehydratase with core strength |
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