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Bacillus subtilis BPN

ISynonyms/Trade Names Bacillus subtilis, Bacillus subtilis BPN, Bacillus subtilis Carlsburg, Proteolytic enzymes, I Subtilisin BPN, Subtilisin Carlsburg [Note Commercial proteolytic enzymes are used in laundry detergents.] ... [Pg.287]

Subtilisin (EC 3.4.21.4) an extracellular, single chain, alkaline serine protease from Bacillus subtilis and related species. S. are known from four different species of Bacillus S. Carlsberg (274 amino acid residues, M, 27,277), S. BPN (275 amino acid residues, M, 27,537), S. Novo (identical with S.BPN ) and S. amylosacchariticus (275 amino acid residues, M, 27671). The observed sequence differences between different S. represent conservative substitutions and are limited to the surface amino acids. Like the pancreatic proteinases, S. has catalytic Ser22i, His64 and Asnjj residues, but it is structurally very different from the other serine proteases, e. g. the active center of S. is -Thr-Ser-Met-, whereas that of the pancreatic enzymes is -Asp-Ser-Gly- pancreatic enzymes contain 4- disulfide bridges, whereas S. contains none S. contains 31 % a-helical structure and 3 spatially separated domains, whereas the pancreatic enzymes have 10-20% a-helical structure and a high content of p-structures in both types, the active center is a substrate cleft. S. also have a broader substrate specificity than the pancreatic enzymes. This is a notable example of the convergent evolution of catalytic activity in two structurally completely different classes of proteins. S. is used in the structural elucidation... [Pg.651]


See other pages where Bacillus subtilis BPN is mentioned: [Pg.116]    [Pg.116]    [Pg.587]    [Pg.1187]    [Pg.116]    [Pg.116]    [Pg.587]    [Pg.1187]    [Pg.189]    [Pg.137]    [Pg.161]    [Pg.2239]    [Pg.229]    [Pg.326]    [Pg.236]   
See also in sourсe #XX -- [ Pg.287 ]




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