Enzymatic properties of dipeptidyl carboxypeptidase from Bacillus pumilus.
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.
Nagamori
Y
Y
Ezaki Glico Biochemical Research Laboratories, Osaka, Japan.
Kusaka
K
K
Fujishima
N
N
Okada
S
S
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002712:Chlorides / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism*; D004793:Enzyme Reactivators / Q000494:pharmacology; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D000806:Angiotensin-Converting Enzyme Inhibitors; D001426:Bacterial Proteins; D002712:Chlorides; D004793:Enzyme Reactivators; D008670:Metals; D004492:Edetic Acid; D010450:Endopeptidases; C020071:dipeptidyl carboxypeptidase