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Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site.〔 〕 They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.〔 〕 In humans, they are responsible for co-ordinating various physiological functions, including digestion, immune response, blood coagulation and reproduction.〔 ==Classification== The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For superfamilies, P = superfamily containing a mixture of nucleophile class families, S = purely serine proteases. superfamily. Within each superfamily, families are designated by their catalytic nucleophile (S = serine proteases). Families of Serine proteases 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「serine protease」の詳細全文を読む スポンサード リンク
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