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Tobacco Etch Virus protease : ウィキペディア英語版 | TEV protease
TEV protease (also called Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV).〔 It is a member of the PA clan of chymotrypsin-like proteases.〔 Due to its high sequence specificity it is frequently used for the controlled cleavage of fusion proteins ''in vitro'' and ''in vivo''. == Origin ==
The tobacco etch virus encodes its entire genome as a single massive polyprotein (350 kDa). This is cleaved into functional units by the three proteases: P1 protease (1 cleavage site), helper-component protease (1 cleavage site) and TEV protease (7 cleavage sites).〔UniProt: TEV polyprotein: 〕 The native protease also contains an internal self-cleavage site. This site is slowly cleaved to inactivate the enzyme (the physiological reason for this is unknown).
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「TEV protease」の詳細全文を読む
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