酵母蛋白酶对激素原的加工。

Enzyme Pub Date : 1991-01-01 DOI:10.1159/000468899
Y Bourbonnais, D Germain, L Latchinian-Sadek, G Boileau, D Y Thomas
{"title":"酵母蛋白酶对激素原的加工。","authors":"Y Bourbonnais,&nbsp;D Germain,&nbsp;L Latchinian-Sadek,&nbsp;G Boileau,&nbsp;D Y Thomas","doi":"10.1159/000468899","DOIUrl":null,"url":null,"abstract":"<p><p>Investigations of the precursors of alpha-pheromone and killer toxin in the yeast Saccharomyces cerevisiae have defined the genes coding (KEX1 and KEX2) for the proteases which are responsible for their processing. In addition to processing at pairs of basic residues it is evident that yeast can also process at monobasic sites. We present data on the Kex1p and Kex2p enzymes, their cellular localization, and their post-translational modification. In addition initial characterisation of the monobasic specific protease and the isolation of mutants defective in this activity are presented. The use of the yeast system as a model for the processing of mammalian prohormones is discussed.</p>","PeriodicalId":11933,"journal":{"name":"Enzyme","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000468899","citationCount":"15","resultStr":"{\"title\":\"Prohormone processing by yeast proteases.\",\"authors\":\"Y Bourbonnais,&nbsp;D Germain,&nbsp;L Latchinian-Sadek,&nbsp;G Boileau,&nbsp;D Y Thomas\",\"doi\":\"10.1159/000468899\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Investigations of the precursors of alpha-pheromone and killer toxin in the yeast Saccharomyces cerevisiae have defined the genes coding (KEX1 and KEX2) for the proteases which are responsible for their processing. In addition to processing at pairs of basic residues it is evident that yeast can also process at monobasic sites. We present data on the Kex1p and Kex2p enzymes, their cellular localization, and their post-translational modification. In addition initial characterisation of the monobasic specific protease and the isolation of mutants defective in this activity are presented. The use of the yeast system as a model for the processing of mammalian prohormones is discussed.</p>\",\"PeriodicalId\":11933,\"journal\":{\"name\":\"Enzyme\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1159/000468899\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Enzyme\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000468899\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000468899","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15

摘要

对酵母α -信息素和杀伤毒素前体的研究已经确定了负责它们加工的蛋白酶的编码基因(KEX1和KEX2)。除了在碱基残基对上加工外,酵母显然也能在碱基位点上加工。我们介绍了Kex1p和Kex2p酶的数据,它们的细胞定位,以及它们的翻译后修饰。此外,单基特异性蛋白酶的初步表征和这种活性缺陷突变体的分离也被提出。本文讨论了利用酵母系统作为哺乳动物激素原加工的模型。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Prohormone processing by yeast proteases.

Investigations of the precursors of alpha-pheromone and killer toxin in the yeast Saccharomyces cerevisiae have defined the genes coding (KEX1 and KEX2) for the proteases which are responsible for their processing. In addition to processing at pairs of basic residues it is evident that yeast can also process at monobasic sites. We present data on the Kex1p and Kex2p enzymes, their cellular localization, and their post-translational modification. In addition initial characterisation of the monobasic specific protease and the isolation of mutants defective in this activity are presented. The use of the yeast system as a model for the processing of mammalian prohormones is 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
期刊最新文献
Functional hepatocellular heterogeneity for the production of plasma proteins. Liver cell heterogeneity: functions of non-parenchymal cells. Hepatocyte heterogeneity in the metabolism of carbohydrates. Zonal liver cell heterogeneity. Hepatocyte heterogeneity in the metabolism of amino acids and ammonia.
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1