酿酒酵母蛋白酶yscA的底物特异性。

T Dreyer
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引用次数: 23

摘要

蛋白酶yscA是一种位于酵母细胞溶酶体样液泡中的胞内天冬氨酸蛋白酶。对变性蛋白底物的特异性是通过蛋白酶yscA消化后裂解产物的分离和鉴定来确定的,并与在类似条件下使用胃蛋白酶获得的特异性进行比较。蛋白酶yscA对它所切割的肽键具有比胃蛋白酶更强的选择性,但与胃蛋白酶和溶酶体组织蛋白酶d一样,对被切割键两侧的大疏水残基也表现出同样的偏好。Phe、Leu和Glu在底物亚基P1和P'1中的Phe、Ile、Leu和Ala有利,而Val在P'1中不有利。讨论了蛋白酶yscA作为水解酶成熟酶的作用。
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Substrate specificity of proteinase yscA from saccharomyces cerevisiae.

Proteinase yscA is an intracellular aspartic proteinase located in the lysosome-like vacuole of the yeast cell. The specificity towards denatured protein substrates was determined by separation and identification of cleavage products after digestions with proteinase yscA, and compared to that obtained with pepsin used under similar conditions. Proteinase yscA is more selective towards the peptide bonds it cleaves than pepsin, but shows the same preference for large hydrophobic residues on both sides of the cleaved bond as pepsin and lysosomal cathepsin D. Phe, Leu and Glu are favoured in substrate subsite P1 and Phe, Ile, Leu and Ala in P'1, whereas Val is unfavoured in P'1. The implications for the role of proteinase yscA as hydrolase maturase are discussed.

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