Active suppression of EndoPG IV by ligation of the pro-sequence from Stereum purpureum Pro-EndoPG I.
We attempted to inactivate endopolygaolacturonase from Stereum purpureum (EndoPG) IV of identical origin by linking the pro-sequence of S. purpureum Pro-EndoPG I to the C-terminus. The recombinant Pro-EndoPG IV, expressed in Escherichia coli, had no polygalacturonase (PG) activity, but activity was acquired after partial degradation of the pro-sequence with V8 protease, as was the case for Pro-EndoPG I. These results indicate that the pro-sequence of Pro-EndoPG I can suppress the PG activity of EndoPG IV.
Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki, Aomori, Japan.
Tsubasa
T
Kimura
Shun
S
Ogawa
Motoki
M
Matsuda
Tetsuya
T
Shimizu
Kazuo
K
Miyairi
D000363:Agaricales / Q000201:enzymology*; D000595:Amino Acid Sequence; D004792:Enzyme Precursors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D011096:Polygalacturonase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D004792:Enzyme Precursors; D011096:Polygalacturonase