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Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity of the thiol aminopeptidase PepC, a bacterial bleomycin hydrolase.

机译:实验证明C末端残基在细菌博来霉素水解酶巯基氨肽酶PepC的严格氨肽酶活性中具有重要作用。

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摘要

PepCs isolated from lactic acid bacteria and bleomycin hydrolases of eukaryotic organisms are strict aminopeptidases which belong to the papain family of thiol peptidases. The structural basis of the enzymic specificity of the lactococcal PepC has been investigated by site-directed mutagenesis. The deletion of the C-terminal residue (Ala-435) abolished the aminopeptidase activity, whereas this deletion led to a new peptidase specificity. The enzymic properties of wild-type and mutant PepCs demonstrate that the terminal alpha-carboxy group plays a key role in the strict aminopeptidase activity.
机译:从乳酸菌和真核生物的博来霉素水解酶分离的PepC是严格的氨基肽酶,其属于巯基肽酶的木瓜蛋白酶家族。已通过定点诱变研究了乳球菌PepC的酶学特异性的结构基础。 C末端残基(Ala-435)的缺失消除了氨肽酶的活性,而这种缺失导致了新的肽酶特异性。野生型和突变型PepCs的酶学性质表明,末端α-羧基在严格的氨肽酶活性中起关键作用。

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