Kinetic Studies on S-PI(Pepstatin Ac)-insensitive Acid Proteinases of Scytalidium lignicolum ATCC 24568. Evidence Identifying Them with a Carboxyl Proteinase Group
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概要
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The kinetics of S-PI (Pepstatin Ac)-insensitive acid proteinases A-2 and C from S. lignicolum were studied to elucidate the essential groups for catalysis. The hydrolysis of Z-Phe-Leu-Ala-Ala by acid proteinase A-2 was studied from pH 1 to 5 at 30°C, and the Michaelis constant, Km, and the maximum velocity, V, were found for each pH. The pH-kcat/Km profile was bell-shaped. The pKe1 and pKe2 for the free enzyme were 1.53 and 3.77, respectively. Acid proteinase A-2 does not contain histidihe residues in the molecule. Accordingly, both of the essential groups are considered to be carboxyl residues. Similar experiments were done with acid proteinase C using Suc-Phe-Arg-Ala-Phe-NPhNO2 as substrate. The pKe1 and pKe2 at 30°C were 2.89 and 5.43, respectively. Based on the data at 30°C and 40°C, the heat of dissociation, ΔHe, was calculated by the equation of Vant Hoff. Both of the groups were regarded as carboxyl residues, since the ΔHe were -0.8 and 1.2kcal/mol, respectively. These results suggest that Scytalidium enzymes have active carboxyl residues participating in the actions, as do the Pepstatin-sensitive acid proteinases.
- 社団法人 日本農芸化学会の論文
著者
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Oda Kohei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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ODA Kohei
Department oj Agricultural Chemistry, College of Agriculture, University oj Osaka Prefecture
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