Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases

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• 作者：Chen ; Jinq-May ; Rawlings ; Neil D. ; Stevens ; Richard A.E. ; Barrett ; Alan J.
• 关键词：Legumain ; Caspase ; Clostripain ; Gingipain ; Peptidase clan
• 刊名：FEBS Letters
• 出版年：1998
• 出版时间：December 28, 1998
• 年：1998
• 卷：441
• 期：3
• 页码：361-365
• 全文大小：544 K

文摘

We show by site-directed mutagenesis that the catalytic residues of mammalian legumain, a recently discovered lysosomal asparaginycysteine endopeptidase, form a catalytic dyad in the motif His-Gly-spacer-Ala-Cys. We note that the same motif is present in the caspases, aspartate-specific endopeptidases central to the process of apoptosis in animal cells, and also in the families of clostripain and gingipain which are arginyl/lysyl endopeptidases of pathogenic bacteria. We propose that the four families have similar protein folds, are evolutionarily related in clan CD, and have common characteristics including substrate specificities dominated by the interactions of the S1 subsite.