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Metalloprotease inhibitors are cellular inhibitors of the matrix metalloprotease (or metalloproteinase) family of proteins (MMP). Several other proteins have similar inhibitory effects, however none as effective (netrins, procollagen C-terminal proteinase enhancer (PCPE), reversion-inducing cysteine-rich protein with Kazal motifs (RECK) and tissue factor pathway inhibitor (TFPI-2)). They might have other biological activities which have yet been fully characterised. There are three classes of commonly used inhibitors for metalloproteinases. * ''In vitro'', EDTA, 1,10-phenanthroline and other chelating compounds lower the concentration of metal to the point where the metal is removed from the enzyme active site. * Classical lock and key inhibitors such as phosphoramidon and bestatin bind tightly by approximating the transition state of the hydrolysis of the peptide, preventing it from acting on other substrates. * Protein inhibitors such as α2-macroglobulin are known to work with metalloproteinases. ==References== 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「Metalloprotease inhibitor」の詳細全文を読む スポンサード リンク
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