Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases
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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DOI：
10.1016/s0014-5793(98)01574-9
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发表时间：
1998-12-28
期刊：
影响因子：
3.5
通讯作者：
Barrett, AJ
中科院分区：
文献类型：
--
作者：
Chen, JM;Rawlings, ND;Barrett, AJ
我们通过定点突变表明，哺乳动物legumain的过氧化氢残基，最近发现的溶酶体天冬酰胺半胱氨酸内肽酶，形成一个催化二联体的基序His-Gly-spacer-Ala-Cys。我们注意到，相同的基序是存在于半胱天冬酶，在动物细胞中的细胞凋亡的过程中，以及在梭菌蛋白酶和gingipain的家庭，这是乙酰/赖氨酰内肽酶的病原菌的谷氨酸特异性内肽酶。我们建议，这四个家庭有相似的蛋白质折叠，在丹CD进化相关，并有共同的特点，包括底物特异性为主的S1亚位点的相互作用。(C)1998年欧洲生物化学学会联合会。
We show by site-directed mutagenesis that the catalatic 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 dan CD, and have common characteristics including substrate specificities dominated by the interactions of the S1 subsite. (C) 1998 Federation of European Biochemical Societies.