Molecular cloning and characterization of an endo-1,3-beta-D-glucanase from the mollusk Spisula sachalinensisстатья

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Дата последнего поиска статьи во внешних источниках: 16 декабря 2014 г.

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[1] Molecular cloning and characterization of an endo-1,3-beta-d-glucanase from the mollusk spisula sachalinensis / V. B. Kozhemyako, D. V. Rebrikov, S. A. Lukyanov et al. // Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. — 2004. — Vol. 137, no. 2. — P. 169–178. cDNA encoding the endo-1,3-beta-d-glucanase from Spisula sachalinensis (LIV) was amplified by PCR using oligonucleotides deduced from the N-terminal end peptide sequence. Predicted enzyme structure consists of 444 amino acids with a signal sequence. The mature enzyme has 316 amino acids and its deduced amino acid sequence coincides completely with the N-terminal end (38 amino acids) of the beta-1,3-glucanase (LIV) isolated from the mollusk. The enzyme sequence from Val 121 to Met 441 reveals closest homology with Pacifastacus leniusculus lipopolysaccharide- and beta-1,3-glucan-binding protein and with coelomic cytolytic factors from Lumbricus terrestris. The mollusk glucanase also shows 36% identity and 56% similarity with beta-1,3-glucanase of the sea urchin Strongylocentrotus purpuratus. It is generally considered that invertebrate glucanase-like proteins containing the bacterial glucanase motif have evolved from an ancient beta-1,3-glucanase gene, but most of them lost their glucanase activity in the course of evolution and retained only the glucan-binding activity. A more detailed evaluation of the protein folding elicited very interesting relationships between the active site of LIV and other enzymes, which hydrolyze native glucans.

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