On the Specificity of a Rennin-like Enzyme from Mucor pusillus |
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Authors: | Tatsushi Oka Katsuhiko Ishino Hiroshige Tsuzuki Kazuyuki Morihara Kei Arima |
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Institution: | 1. Shionogi Research Laboratory, Shionogi &2. Co., Ltd., Fukushima-ku, Osaka 553;3. Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo 113 |
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Abstract: | The specificity of a rennin-like enzyme from Mucor pusillus Lindt was determined using synthetic peptides and oxidized insulin B chain as substrates. The results indicate that the enzyme exhibits specificity against aromatic, bulky or hydrophobic amino acid residues at both sides of the splitting point. The susceptibility of peptide substrates increases with the increase of their molecular size, indicating the significance of secondary interaction for hydrolysis. Z-tetrapeptides such as | |
Keywords: | Δ6-desaturase gemfibrozil rat |
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