酿酒酵母蛋白酶yscA的底物特异性。

T Dreyer
{"title":"酿酒酵母蛋白酶yscA的底物特异性。","authors":"T Dreyer","doi":"10.1007/BF02908301","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"54 3","pages":"85-97"},"PeriodicalIF":0.0000,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02908301","citationCount":"23","resultStr":"{\"title\":\"Substrate specificity of proteinase yscA from saccharomyces cerevisiae.\",\"authors\":\"T Dreyer\",\"doi\":\"10.1007/BF02908301\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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.</p>\",\"PeriodicalId\":9616,\"journal\":{\"name\":\"Carlsberg Research Communications\",\"volume\":\"54 3\",\"pages\":\"85-97\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1989-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/BF02908301\",\"citationCount\":\"23\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Carlsberg Research Communications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/BF02908301\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Carlsberg Research Communications","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF02908301","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
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。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信