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Enzymatic properties of dipeptidyl carboxypeptidase from Bacillus pumilus
Y Nagamori1, K Kusaka, N Fujishima
1Ezaki Glico Biochemical Research Laboratories, Osaka, Japan.
Agricultural and Biological Chemistry
|July 1, 1991
Abstract:
Enzymatic properties of dipeptidyl carboxypeptidase (DCP) from Bacillus pumilus were investigated. The enzyme was more active on tri- and tetrapeptides than angiotensin-converting enzyme (ACE) from rabbit lung. The presence of chloride ion is essential for the hydrolysis. The Km value of angiotensin I for the enzyme was 0.119 x 10(-3) M. The enzyme was not inhibited by the mammalian ACE inhibitors lisinopril and enalaprilat. The enzyme is readily inhibited by EDTA but restored by Co2+, Mn2+, and Zn2+. Therefore, it seems to be a zinc-metallo protease.