結晶構造から見た酵素の反応機構 (セリンプロテアーゼ系を題材として)
1982 年 24 巻 1 号 p. 65-75
詳細
1982 年 24 巻 1 号 p. 65-75
Protein crystallography is one of the most powerful techniques for observing the interactions of enzymes with other molecules, especially small ones, at atomic resolution. This article, taking up a group of serine proteases as an example, outlines the way crystallography has been useful for elucidating the enzymatic reation mechanisms. Finally, we introduce “X-ray cryoenzymology” or “low temperture protein crystallography”, the apparently most effective technique for determining the details of the interaction of enzymes with their actual substrates, which will be a popular method in no distant future.
