Kinin-inactivating enzyme from the mushroom Tricholoma conglobatum. VI. Actions on angiotensins I and II.

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Abstract
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. This enzyme has 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. This enzyme had angiotensinase activity in addition to angiotensin I converting activity in rat uterus. The rate of angiotensin II hydrolysis was very slow compared with that of kinin hydrolysis; the molar ratio of angiotensin II hydrolysis to bradykinin hydrolysis was .apprx. 1:70.