ID 62131
著者
香西, 美甫 徳島大学
小博, 裕子 徳島大学
杉山, 典子 徳島大学
山口, 安亮 徳島大学
キーワード
Inorganic pyrophosphatase
Site-directed mutagenesis
Submit interaction
Thermostability
Thermus thermophilus
資料タイプ
紀要論文
抄録
Inorganic pyrophosphatase (EC. 3.6.1.1) from Thermus thermophilus (Tth PPase) forms the thermostable
hexamer,and it was suggested from X-ray studies that its intersubunit interactions stabilize the whole molecule.
However,the contribution of Thr138 at the intertrimer interface to quatemary structure and thermostability was
unknown functionally. Therefore,we prepared four Thr138-substituted variants (T138A,V ,N ,and H) by
site-directed mutagenesis. Then,thermostabilities of the enzyme activity and the quatemary structure for T138V
and A were decreased relative to those of the wild type Tth PPase,whereas T138H and N variants remained
much hexamer contents and the enzyme activity than T138V and A. Therefore,we suggest that the polar group
in Thr138 of Tth PPase is more crucial than the methyl group for thermostability and quatemary structure,and it
may contribute to the formation of stable trimer-trimer interface.
掲載誌名
徳島大学総合科学部自然科学研究 = Natural Science Research, The University of Tokushima
ISSN
09146385
cat書誌ID
AN10065859
出版者
徳島大学総合科学部
22
開始ページ
65
終了ページ
73
並び順
65
発行日
2008-12-25
EDB ID
179284
フルテキストファイル
言語
eng
部局
理工学系