麹菌 (Aspergillus oryzae), 細菌 (Bacillus suubtilis) およびブタ腎臓のアミノペプチダーゼの各種合成基質に対する作用特性

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The substrate specificities of aminopeptidase from Aspergillus oryzae (AOP), aminopeptidase I and II from Bacillus subtilis (BSP-I, BSP-II) and leucine aminopeptidase from swine kidney (LAP) were investigated with various synthetic peptides. AOP rapidly hydrolyzed tripeptides, such as Leu-Gly-Gly, Leu-Ala-Gly and Leu-Gln-Gly, and mod-erately hydrolyzed Gly-Gly-Val, Leu-Gly-Gly-NH2, Ala-Leu-Gly and Ala-Gly-Leu. The enzyme slowly hdrolyzed Pro-Gln-Gly, Pro-Leu-Gly and Leu-Lys-Lys, but scarcely hydrolyzed Leu-Gly and Leu-NH2. BSP-I rapidly hydrolyzed Leu-Ala-Gly, Pro-Gln-Gly, Ala-Leu-Gly and Leu-Gln-Gly, and moderately hydrolyzed Leu-Gly-Gly and Ala-Gly-Leu, but scarcely hydrolyzed Leu-Gly and Leu-NH2. BSP-II rapidly hydrolyzed Ala-Leu-Gly, Leu-Gly-Gly and Leu-Ala-Gly, and moderately hydrolyzed Gly-Gly-Val, Leu-Gln-Gly, Ala-Gly-Leu and Pro-Gln-Gly, but hardly hydrolyzed Leu-Gly and Leu-NH2. BSP-I preferentially hydrolyzed Pro-Gln-Gly and Leu-Gln-Gly rather than BSP-II, while BSP-II hydro-lyzed Ala-Leu-Gly, Ala-Gly-Leu, Gly-Gly-Val, Leu-Gly-Gly and Leu-Ala-Gly more rapidly than BSP-I. LAP preferentially hydrolyzed various oligopep-tides that possessed L-Leu and L-Pro as the N-terminal amino acid, except Ala-Leu-Gly, and also hydrolyzed Leu-NH2 and Leu-Gly-GIy-NH2.
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