A role of lysine-43 in the inactivation of rat prorenin.
1. 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.
Suzuki
F
F
Department of Biotechnology, Faculty of Agriculture, Gifu University, Ibaraki, Japan.
Tosaki
I
I
Shiratori
Y
Y
Nagai
M
M
Murakami
K
K
Nakamura
Y
Y
D000818:Animals; D001665:Binding Sites; D016466:CHO Cells; D002384:Catalysis; D006224:Cricetinae; D004792:Enzyme Precursors / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008239:Lysine / Q000502:physiology*; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011489:Protein Denaturation; D051381:Rats; D012083:Renin / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*
D004792:Enzyme Precursors; D012083:Renin; D008239:Lysine