A potent kinin-inactivating enzyme from the mushroom Tricholoma conglobatum, Shimeji kininase, liberated angiotensin II and the dipeptide, H-His-Leu-OH, from angiotensin I. Thus, this enzyme was considered to have both kininase and angiotensin I converting activities like kininase II (angiotensin I converting enzyme, EC 3.4.15.1), which is widely distributed in mammals of various species. On the other hand, this enzyme had angiotensinase activity in addition to angiotensin I converting activity. However, the rate of angiotensin II hydrolysis was very slow as compared with that of kinin hydrolysis ; the molar ratio of angiotensin II hydrolysis to bradykinin hydrolysis was about 1 : 70.
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