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On the Specificity of a Rennin-like Enzyme from Mucor pusillus
Authors:Tatsushi Oka  Katsuhiko Ishino  Hiroshige Tsuzuki  Kazuyuki Morihara  Kei Arima
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
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  /></span>(the arrows show the bond split) are found as efficient substrates for the enzyme. The main points of cleavage in oxidized insulin B chain are; Phe-Val (<i>1–2</i>), Ala-Leu (<i>14–15</i>), Leu-Tyr (<i>15–16</i>), Tyr-Leu (<i>16–17</i>), and Phe-Phe (<i>24–25</i>).</p>The specificity of the <i>M. pusillus</i> enzyme is almost identical with that of the rennin-like enzyme from <i>Mucor miehei</i>, and similar to those of usual acid proteinases possessing tryp- sinogen activating ability, except that the latter enzymes show specificity against basic amino acid residues at the carbonyl-side of the splitting point.</td>
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Keywords:Δ6-desaturase  gemfibrozil  rat
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