Functional characterization of Asp-317 mutant of human renin expressed in COS cells.
Renin is an unique aspartyl (acid) protease with optimal activity at neutral pH. It has been suggested that Ala-317 of human renin contributes to neutral optimum pH of the enzyme [(1984) FEBS Lett. 174, 102-111]. The hypothesis was verified by the characterization of mutant renin in which Ala-317 was replaced with Asp by a site-directed mutagenesis. Wild-type and mutant renins, which were expressed in COS cells, exhibited different pH-activity profiles and optimum pH of the mutant enzyme was lower than that of the wild-type enzyme. This result suggests that Ala-317 of human renin plays an important role in the determination of optimum pH of the enzyme.
Yamauchi
T
T
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Nagahama
M
M
Hori
H
H
Murakami
K
K
D000409:Alanine; D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine; D002460:Cell Line; D006224:Cricetinae; D004274:DNA, Recombinant; D004792:Enzyme Precursors / Q000096:biosynthesis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009154:Mutation; D010957:Plasmids; D012083:Renin / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014162:Transfection; D014357:Trypsin / Q000378:metabolism
D004274:DNA, Recombinant; D004792:Enzyme Precursors; D001216:Asparagine; D014357:Trypsin; D012083:Renin; D000409:Alanine