A role of lysine-43 in the inactivation of rat prorenin.

Suzuki F, Tosaki I, Shiratori Y, Nagai M, Murakami K, Nakamura Y

Department of Biotechnology, Faculty of Agriculture, Gifu University, Ibaraki, Japan.

Clin Exp Pharmacol Physiol Suppl. 1995 Dec;22(1):S15-4. doi: 10.1111/j.1440-1681.1995.tb02859.x.

Abstract

Lysine-43 (Lys43) in the prosegment region was located within 3 x 10(-1) of catalytic sites, Asp81 and Asp266, in a stereo structure model of rat prorenin. 2. A mutant prorenin, Lys43Leu, was produced to elucidate a role of Lys43 in the inactivation of prorenin. Lys43Leu as well as the wild type were inactive at a neutral pH, and activated at an acidic pH. Its acid-activation speed was three times higher than that of the wild type. The mutant prorenin was more labile than the wild type at 55 degrees C and a neutral pH. 3. These results indicate that Lys43 forms ionic bonds with Asp81 and Asp266 to inactivate and stabilize prorenin.

摘要