Microviridin
The structure of microviridin B
Microviridins are a class of serine protease inhibitors produced by various genera of cyanobacteria. Microviridins are characterized by tricyclic depsipeptide structure and are members of the RiPP family of natural products.
The first microviridin was isolated from Microcystis viridis (NIES-102) and its structure was reported in 1990.[1]
The known microviridins include microviridins A-L.
Toxicity
Microviridin J has been found to disrupt molting in the invertebrate Daphnia pulicaria, probably as a result of its protease inhibitory effects [2]
See also
References
- ↑ Ishitsuka MO, Kusumi T, Kakisawa H, Kunimitsu K, Watanabe MM (1990). “Microviridin. A novel tricyclic depsipeptide from the toxic cyanobacterium Microsystis viridis”. J. Am. Chem. Soc. 112 (22): 8180-8182. doi: 10.1021/ja00178a060.
- ↑ Thomas Rohrlack; Kirsten Christoffersen; Melanie Kaebernick; Brett A. Neilan (2004). "Cyanobacterial Protease Inhibitor Microviridin J Causes a Lethal Molting Disruption in Daphnia pulicaria". Applied and Environmental Microbiology. 70 (8): 5047–5050. doi:10.1128/AEM.70.8.5047-5050.2004. PMC 492328
. PMID 15294849.
External links
- "Microviridins D-F, serine protease inhibitors from the cyanobacterium Oscillatoria agardhii (NIES-204)". Tetrahedron. 52: 8159–8168. doi:10.1016/0040-4020(96)00377-8.
- "Post-translational Modification in Microviridin Biosynthesis". ChemBioChem. 9: 3066–3073. doi:10.1002/cbic.200800560.
- http://aem.asm.org/content/76/11/3568.short
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