Anabaenopeptins: What We Know So Far
Cyanobacteria are microorganisms with photosynthetic mechanisms capable of colonizing several distinct environments worldwide. They can produce a vast spectrum of bioactive compounds with different properties, resulting in an improved adaptative capacity. Their richness in secondary metabolites is r...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-07-01
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| Series: | Toxins |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2072-6651/13/8/522 |
| _version_ | 1797521961352429568 |
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| author | Patrick Romano Monteiro Samuel Cavalcante do Amaral Andrei Santos Siqueira Luciana Pereira Xavier Agenor Valadares Santos |
| author_facet | Patrick Romano Monteiro Samuel Cavalcante do Amaral Andrei Santos Siqueira Luciana Pereira Xavier Agenor Valadares Santos |
| author_sort | Patrick Romano Monteiro |
| collection | DOAJ |
| description | Cyanobacteria are microorganisms with photosynthetic mechanisms capable of colonizing several distinct environments worldwide. They can produce a vast spectrum of bioactive compounds with different properties, resulting in an improved adaptative capacity. Their richness in secondary metabolites is related to their unique and diverse metabolic apparatus, such as Non-Ribosomal Peptide Synthetases (NRPSs). One important class of peptides produced by the non-ribosomal pathway is anabaenopeptins. These cyclic hexapeptides demonstrated inhibitory activity towards phosphatases and proteases, which could be related to their toxicity and adaptiveness against zooplankters and crustaceans. Thus, this review aims to identify key features related to anabaenopeptins, including the diversity of their structure, occurrence, the biosynthetic steps for their production, ecological roles, and biotechnological applications. |
| first_indexed | 2024-03-10T08:19:58Z |
| format | Article |
| id | doaj.art-cfd4f96583c840cc9501fee3212b5c99 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-03-10T08:19:58Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-cfd4f96583c840cc9501fee3212b5c992023-11-22T10:04:07ZengMDPI AGToxins2072-66512021-07-0113852210.3390/toxins13080522Anabaenopeptins: What We Know So FarPatrick Romano Monteiro0Samuel Cavalcante do Amaral1Andrei Santos Siqueira2Luciana Pereira Xavier3Agenor Valadares Santos4Laboratory of Biotechnology of Enzymes and Biotransformation, Biological Sciences Institute, Federal University of Pará, Belém 66075-110, BrazilLaboratory of Biotechnology of Enzymes and Biotransformation, Biological Sciences Institute, Federal University of Pará, Belém 66075-110, BrazilLaboratory of Biomolecular Technology, Biological Sciences Institute, Federal University of Pará, Belém 66075-110, BrazilLaboratory of Biotechnology of Enzymes and Biotransformation, Biological Sciences Institute, Federal University of Pará, Belém 66075-110, BrazilLaboratory of Biotechnology of Enzymes and Biotransformation, Biological Sciences Institute, Federal University of Pará, Belém 66075-110, BrazilCyanobacteria are microorganisms with photosynthetic mechanisms capable of colonizing several distinct environments worldwide. They can produce a vast spectrum of bioactive compounds with different properties, resulting in an improved adaptative capacity. Their richness in secondary metabolites is related to their unique and diverse metabolic apparatus, such as Non-Ribosomal Peptide Synthetases (NRPSs). One important class of peptides produced by the non-ribosomal pathway is anabaenopeptins. These cyclic hexapeptides demonstrated inhibitory activity towards phosphatases and proteases, which could be related to their toxicity and adaptiveness against zooplankters and crustaceans. Thus, this review aims to identify key features related to anabaenopeptins, including the diversity of their structure, occurrence, the biosynthetic steps for their production, ecological roles, and biotechnological applications.https://www.mdpi.com/2072-6651/13/8/522cyanobacteriapeptideNRPSanabaenopeptin |
| spellingShingle | Patrick Romano Monteiro Samuel Cavalcante do Amaral Andrei Santos Siqueira Luciana Pereira Xavier Agenor Valadares Santos Anabaenopeptins: What We Know So Far Toxins cyanobacteria peptide NRPS anabaenopeptin |
| title | Anabaenopeptins: What We Know So Far |
| title_full | Anabaenopeptins: What We Know So Far |
| title_fullStr | Anabaenopeptins: What We Know So Far |
| title_full_unstemmed | Anabaenopeptins: What We Know So Far |
| title_short | Anabaenopeptins: What We Know So Far |
| title_sort | anabaenopeptins what we know so far |
| topic | cyanobacteria peptide NRPS anabaenopeptin |
| url | https://www.mdpi.com/2072-6651/13/8/522 |
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