Evolutionary trees of proteins analysed by means of computer comparative methods were reconstructed and the level of the structure and functional relationship was revealed. The distance between the percent amino acid contents was used to classify a group of toxins from the sea anemone Radianthus macrodactylus, which proved to belong to long neurotoxins. The scores were calculated by the pattern recognition method. By the use of the distance values, ten phospholipases A2 were divided into two groups, containing representatives of the most closely related organisms.
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Beilstein J Org Chem
July 2020
Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
Liquid cultures of sp. SI9, isolated from the outer tissue of the sea anemone , was found to produce three new -isocrotonyl-3-hydroxybutyric acid derivatives, -isocrotonyl-3-hydroxypentanoic acid (), -isocrotonyl-3-hydroxyhexanoic acid (), and -()-2-hexenoyl-3-hydroxybutyric acid (), together with the known -isocrotonyl-3-hydroxybutyric acid (). The structures of - were established by NMR spectroscopy and mass spectrometry, coupled with anisotropy-based chiral analysis, revealing the same -configuration for all congeners -.
View Article and Find Full Text PDFMar Drugs
July 2012
G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 159, Pr. 100 let Vladivostoku, Vladivostok 690022, Russian Federation.
The primary structure of a new Kunitz-type protease inhibitor InhVJ from the sea anemone Heteractis crispa (Radianthus macrodactylus) was determined by protein sequencing and cDNA cloning. InhVJ amino acid sequence was shown to share high sequence identity (up to 98%) with the other known Kunitz-type sea anemones sequences. It was determined that the P1 Thr at the reactive site resulted in a decrease of the K(i) of InhVJ to trypsin and α-chymotrypsin (7.
View Article and Find Full Text PDFBiochemistry (Mosc)
October 2011
Pacific Institute of Bioorganic Chemistry, Far Eastern Branch of the Russian Academy of Sciences, Vladivostok, Russia.
A new actinoporin Hct-S4 (molecular mass 19,414 ± 10 Da) belonging to the sphingomyelin-inhibited α-pore forming toxin (α-PFT) family was isolated from the tropical sea anemone Heteractis crispa (also called Radianthus macrodactylus) and purified by methods of protein chemistry. The N-terminal nucleotide sequence (encoding 20 amino acid residues) of actinoporin Hct-S4 was determined. Genes encoding 18 new isoforms of H.
View Article and Find Full Text PDFThe influence of different environmental values of the pH and temperature on the spatial organization of serine proteinase inhibitor from the sea anemone Heteractis crispa (=Radianthus macrodactylus) on the level of tertiary and secondary structure was studied by CD spectroscopy. The molecule InhVJ was shown to possess a high conformational thermo- and pH-stability. We determined the point of conformational thermotransition of polypeptide (70 degrees C) after which the molecule gets denaturational stable state with conservation of 80% proteinase inhibitory activity.
View Article and Find Full Text PDFInt J Biol Sci
November 2011
Department of Biochemistry and Molecular Biology, Second Military Medical University, Shanghai, China.
A new Cytolysin, termed as Gigantoxin-4, was isolated from the sea anemone Stichodactyla gigantea and found to be highly homologous with Cytolysin-3 (HMg III) from Heteractis magnifica, RTX-A from Radianthus macrodactylus, and Sticholysin-1 (St I) and Sticholysin-2 (St II) from Stichodactyla helianthus (homology 82%, 86%, 82% and 86% respectively). Its 20 N-terminal residues were identified and the full-length cDNA sequence was obtained by reverse transcription-polymerase chain reaction (RT-PCR). Multiple sequence alignments with other Cytolysins of the actinoporin family clearly indicated that Gigantoxin-4 belongs to this protein family.
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