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- W1663535880 abstract "Streptomyces subtilisin inhibitor (SSI), a dimeric protein that strongly inhibits subtilisins, was shown to form tight inhibitory complexes with Streptomyces griseus proteases A and B (SGPA and SGPB). The apparent dissociation constants of the SGPA-SSI and SGPB-SSI complexes were found to be orders of magnitude less than those of subtilisin-SSI complexes. Using the known atomic coordinates for SGPA arid SSI, the highly complementary nature of the surface geometries of the two proteins was confirmed by a computer graphics study, which led to a pro posed structure for the SGPA-SSI complex. Kinetic studies further suggested that the SSI dimer can bind two molecules of either SGPA or SGPB, and the 2:1-complexes (consisting of one inhibitor dimer and one enzyme molecule) apparently possess lower intrinsic dissociation constants than the 2:2-complexes. It was also shown that both of SGPA and SGPB are inhibited by both soybean trypsin inhibitor (Kunitz) and bovine pancreatic trypsin inhibitor (Kunitz), but far less strongly than by SSI." @default.
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- W1663535880 date "1985-11-01" @default.
- W1663535880 modified "2023-10-17" @default.
- W1663535880 title "Interactions of Streptomyces Subtilisin Inhibitor with Streptomyces griseus Proteases A and B. Enzyme Kinetic and Computer Simulation Studies1" @default.
- W1663535880 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a135393" @default.
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