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Unveiling the World of Anabaena Peptides: Structure, Function, and Significance by T Krishnamurthy·1986·Cited by 323—Toxicpeptidesfrom two European Microcystis aeruginosa and one CanadianAnabaenaflos-aquae species of freshwater cyanobacteria (blue-green algae) were 

:members of the cyanopeptolin class of cyanobacterial peptides

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a family of cyclic peptides containing six amino acid residues by T Krishnamurthy·1986·Cited by 323—Toxicpeptidesfrom two European Microcystis aeruginosa and one CanadianAnabaenaflos-aquae species of freshwater cyanobacteria (blue-green algae) were 

The intricate world of cyanobacteria, particularly those belonging to the Anabaena genus, has yielded a fascinating array of peptides. These cyanobacterial metabolites with a cyclic peptide structure have garnered significant scientific interest due to their diverse biological activities and complex synthesis pathways. Among the most extensively studied are the anabaenopeptins (APs), a prominent family of cyclic hexapeptides that are commonly occurring cyanobacteria metabolites.

Anabaena peptides are not a monolithic group; they represent a wide spectrum of molecular structures and functionalities. Research has identified various classes, including anabaenopeptins, anabaenolysins, and cyanobactins. Anabaenopeptins, for instance, are characterized by a family of cyclic peptides containing six amino acid residues. Their synthesis is a testament to nature's biochemical ingenuity, as they are synthesized nonribosomally as cyclic hexapeptides through sophisticated enzymatic machinery. This process involves nonribosomal peptide synthetase (NRPS) systems, as evidenced by studies investigating structural elucidation of cyanobacterial peptides encoded by peptidesynthetase gene in Anabaena species.

The structural variability within anabaenopeptins is remarkable. While many are cyclic hexapeptides, variations in amino acid composition and the presence of exocyclic positions lead to a multitude of compounds. For example, specific studies have reported the isolation of three new cyclic peptides, anabaenopeptins NZ825, NZ841, and NZ857, from cultured Anabaena strains. Furthermore, research has delved into the evolution of Anabaenopeptin peptide structural variability, exploring the presence and recombination of genes responsible for their production. The classification extends to related compounds like anabaenopeptilides, which are described as members of the cyanopeptolin class of cyanobacterial peptides.

Beyond the anabaenopeptins, other significant peptides from Anabaena sp. have been identified. Anabaenolysins, such as anabaenolysin A and anabaenolysin B, are highlighted as two novel cyclic lipopeptides isolated from benthic cyanobacterial strains of the genus Anabaena. These compounds showcase the broader diversity of peptides produced by this genus, extending beyond purely peptide structures to include lipopeptide modifications. Another class, cyanobactins, are described as small, cyclic peptides recently found in cyanobacteria, formed through proteolytic cleavage and posttranslational modifications.

The biological significance of these anabaena peptides is a major driving force behind their study. Many of them exhibit potent biological activities, with applications ranging from pharmaceutical development to environmental monitoring. For instance, anabaenopeptins, cyclic peptides produced by cyanobacteria, have been identified as potent inhibitors of TAFIa with IC50 values as low as 1.5 nM. Some anabaenopeptins have also demonstrated activity as carboxypeptidase-A inhibitors, although the potency can vary significantly between different anabaenopeptin variants; for example, anabaenopeptins B, 7, 8E, and F9 showed no activity at a concentration of 10 µg/mL in one study.

Moreover, Anabaena species are known to produce multiple toxic and non-toxic peptides. This dual nature underscores the importance of distinguishing between different peptide types. While some anabaenopeptins and related compounds are non-toxic, others, like microcystins, are potent toxins. The presence of microcystins (inhibitors of protein phosphatases 1 and 2A) alongside other bioactive peptides in certain Anabaena strains highlights the complex chemical ecology of these organisms. In addition to these, Laxaphycins A and B are noted as the major components in an antifungal mixture of cyclic peptides from the terrestrial blue-green alga Anabaena laxa FK-1-2, showcasing their potential antimicrobial properties.

The study of anabaena peptides is intrinsically linked to understanding the broader biology of Anabaena. For example, research into nitrogen metabolism in Anabaena has revealed how peptide production can be influenced by environmental factors. Under nitrogen deficiency, Anabaena 7120 forms specialized heterocysts, and peptide sequences can indicate their positions within corresponding proteins, providing insights into cellular processes. Furthermore, the investigation of biofilm formation in Anabaena (Nostoc) has identified a wide array of biofilm-related genes, including those involved in the synthesis and translocation of EPS and key regulatory elements, which may indirectly influence peptide production or function.

The extraction and characterization of these peptides often involve sophisticated analytical techniques. HPLC chromatograms of the identified peptides present in Anabaena strain 90 are crucial for identifying and quantifying different compounds. The application of Gas Chromatography-mass Spectrometry (GC-MS) analysis of Anabaena species methanol extract has also revealed significant bioactivity

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Isolation, Co-Crystallization and Structure-Based
Perin G. et al., 2021_ Nitrogen in Anabaena.pdf
by E Entfellner·2017·Cited by 46—The APs aresynthesized nonribosomally as cyclic hexapeptideswith various amino acids at the exocyclic position. We investigated the presence and recombination 
Therefore, certain amino acid exchanges near FeMo-co might produce variant MoFe proteins in heterocyst-formingAnabaenathat redirect the electron flux through 

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