Eritadenine from Edible Mushrooms Inhibits Activity of Angiotensin Converting Enzyme in Vitro

摘要

The inhibition of angiotensin converting enzyme (ACE) activity was determined in vitro by mushroom-derived eritadenine (EA), which was analyzed in 11 principal Korean edible mushrooms. EA inhibited ACE activity with 0.091 mu M IC50, whereas the IC50 of captopril (CP), which is a reference compound, was 0.025 mu M. Kinetic measurements of ACE reaction in the substrate of hippuryl-L-histidyl-L-leucine (HHL) with or without EA revealed that the V-max (0.0465 O.D/30 mM) was unchanged, but the the K-m increased from 2.063 to 3.887 mM, indicating that EA competes with HHL for the active site. When EA was analyzed by HPLC, Lentinus edodes with a soft cap contained the highest amount EA (642.8 mg%); however, Phellinus linteus with a hard cap contained the least amount of EA (9.4 mg%). These results indicate that EA was a strong competitive inhibitor for ACE, and edible mushrooms with soft caps contained a significant amount of EA.