Structure via PubChem · Public domain (PubChem)
teleocidin A1
Sign in to saveLyngbyatoxin-a is a type of alkaloid cyanotoxin produced by certain cyanobacteria species, most notably Moorea producens (formerly classified as Lyngbya majuscula). It is produced as defense mechanism to ward off any would-be predators of the bacterium, being a potent blister agent as well as carcinogen. Low concentrations cause a common skin condition known as seaweed dermatitis.
Chemical data
- Formula
- C27H39N3O2
- Molecular weight
- 437.6 g/mol
- IUPAC name
- (10S,13S)-5-[(3R)-3,7-dimethylocta-1,6-dien-3-yl]-13-(hydroxymethyl)-9-methyl-10-propan-2-yl-3,9,12-triazatricyclo[6.6.1.04,15]pentadeca-1,4,6,8(15)-tetraen-11-one
- SMILES
- CC(C)[C@H]1C(=O)N[C@@H](CC2=CNC3=C(C=CC(=C23)N1C)[C@](C)(CCC=C(C)C)C=C)CO
- InChIKey
- KISDGNGREAJPQR-OICBGKIFSA-N
- XLogP
- 6.2
- Polar surface area
- 68.4 Ų
- H-bond donors
- 3
- H-bond acceptors
- 3
- Formal charge
- 0
via PubChem
Wikidata facts
- Mass
- 437.304
Show 4 more facts
- chemical formula
- C₂₇H₃₉N₃O₂
- canonical SMILES
- CC(C)C1C(=O)NC(CC2=CNC3=C(C=CC(=C23)N1C)C(C)(CCC=C(C)C)C=C)CO
- isomeric SMILES
- CC(C)[C@H]1C(=O)N[C@@H](CC2=CNC3=C(C=CC(=C23)N1C)[C@](C)(CCC=C(C)C)C=C)CO
- found in taxon
- Streptomyces
Sources (2)
via Wikidata · CC0
~1 min read
Encyclopedic overview
2 sectionsContents
- Biosynthesis
- References
Lyngbyatoxin-a is a type of alkaloid cyanotoxin produced by certain cyanobacteria species, most notably Moorea producens (formerly classified as Lyngbya majuscula). It is produced as defense mechanism to ward off any would-be predators of the bacterium, being a potent blister agent as well as carcinogen. Low concentrations cause a common skin condition known as seaweed dermatitis.
== Biosynthesis == thumb|Lyngbyatoxin Biosynthesis reported by Gerwick et al. and Neilan et al. Lyngbyatoxin is a terpenoid indole alkaloid hybrid that belongs to the class of non-ribosomal peptides (NRPs). Lyngbyatoxin contains a nucleophilic indole ring that takes part in the activation of protein kinases. Figure 1, shows the biosynthesis of Lyngbyatoxin reported by Neilan et al. and Gerwick et al. The non-ribosomal peptide synthase (NRPS) LtxA protein condenses L-methyl-valine and L-tryptophan to form the linear dipeptide N-methyl-L-valyl-L-tryptophan. The latter is released via a NADPH-dependent reductive cleavage to form the aldehyde which is subsequently reduced to the corresponding alcohol. A P450-dependent monooxygenase called LtxB then performs the oxidation and subsequent cyclization of N-methyl-L-valyl-L-tryptophan. Finally, LtxC transfers a geranyl functional group from geranyl pyrophosphate (GPP) to carbon number 7 of the indole ring.
Excerpted from Wikipedia’s “teleocidin A1” article, available under the CC BY-SA 4.0 licence.