Isoenzyme der malatdehydrogenase und ihre regulation in Saccharomyces cerevisiae

Irene Witt, Rainer Kronau, Helmut Holzer
{"title":"Isoenzyme der malatdehydrogenase und ihre regulation in Saccharomyces cerevisiae","authors":"Irene Witt,&nbsp;Rainer Kronau,&nbsp;Helmut Holzer","doi":"10.1016/0926-6593(66)90142-1","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. From <em>Saccharomyces cerevisiae</em>, incubated on a glucose-free medium with acetate as the only carbon source, two different malate dehydrogenases (<span>l</span>-malate: NAD<sup>+</sup> oxidoreductase, EC 1.1.1.37) have been isolated by DEAE-cellulose ion-exchange chromatography. One of these enzymes was only found in the mitochondria and is called enzyme A or m-malate dehydrogenase; the other enzyme was found in the extramitochondrial c-space and is called enzyme B or c-malate dehydrogenase. At present it cannot be decided whether m-malate dehydrogenase also exists in the c-space or leaks when the mitochondria are injured.</p></span></li><li><span>2.</span><span><p>2. The reaction velocity plotted against the concentration of oxaloacetic acid showed a characteristic substrate inhibition in the case of m-malate dehydrogenase In contrast, c-malate dehydrogenase showed no substrate inhibition. This difference corresponds to the behaviour of m-malate dehydrogenase and c-malate dehydrogenase from liver.</p></span></li><li><span>3.</span><span><p>3. In yeast grown on glucose only m-malate dehydrogenase could be found, but after incubating the cells on acetate as the sole carbon source, both m-malate dehydrogenase and c-malate dehydrogenase were found. In reference to earlier experiments concerning the regulation of malate dehydrogenase activity in yeast, it is concluded that a repression of c-malate dehydrogenase synthesis by glucose occurs. This regulating mechanism is useful for the cell, because in the glycoxylate cycle c-malate dehydrogenase participates in the gluconeogenesis from acetate or ethanol. This enzyme is not necessary when glucose is in the medium.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90142-1","citationCount":"84","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366901421","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 84

Abstract

  • 1.

    1. From Saccharomyces cerevisiae, incubated on a glucose-free medium with acetate as the only carbon source, two different malate dehydrogenases (l-malate: NAD+ oxidoreductase, EC 1.1.1.37) have been isolated by DEAE-cellulose ion-exchange chromatography. One of these enzymes was only found in the mitochondria and is called enzyme A or m-malate dehydrogenase; the other enzyme was found in the extramitochondrial c-space and is called enzyme B or c-malate dehydrogenase. At present it cannot be decided whether m-malate dehydrogenase also exists in the c-space or leaks when the mitochondria are injured.

  • 2.

    2. The reaction velocity plotted against the concentration of oxaloacetic acid showed a characteristic substrate inhibition in the case of m-malate dehydrogenase In contrast, c-malate dehydrogenase showed no substrate inhibition. This difference corresponds to the behaviour of m-malate dehydrogenase and c-malate dehydrogenase from liver.

  • 3.

    3. In yeast grown on glucose only m-malate dehydrogenase could be found, but after incubating the cells on acetate as the sole carbon source, both m-malate dehydrogenase and c-malate dehydrogenase were found. In reference to earlier experiments concerning the regulation of malate dehydrogenase activity in yeast, it is concluded that a repression of c-malate dehydrogenase synthesis by glucose occurs. This regulating mechanism is useful for the cell, because in the glycoxylate cycle c-malate dehydrogenase participates in the gluconeogenesis from acetate or ethanol. This enzyme is not necessary when glucose is in the medium.

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
乙醚酶以及为糖衣套餐定制
1.1. 采用deae -纤维素离子交换色谱法,从酿酒酵母(Saccharomyces cerevisiae)中分离出两种不同的苹果酸脱氢酶(l-苹果酸:NAD+氧化还原酶,EC 1.1.1.37)。其中一种酶只存在于线粒体中,被称为A酶或间苹果酸脱氢酶;另一种酶位于线粒体外的c空间,称为B酶或c-苹果酸脱氢酶。目前还不能确定间苹果酸脱氢酶是否也存在于c空间,或者在线粒体损伤时是否泄漏。草酰乙酸浓度对m-苹果酸脱氢酶的反应速度有明显的底物抑制作用,而c-苹果酸脱氢酶则无底物抑制作用。这种差异对应于肝脏中m-苹果酸脱氢酶和c-苹果酸脱氢酶的行为。在葡萄糖培养基上培养的酵母中,只发现间苹果酸脱氢酶,而在醋酸盐作为唯一碳源培养的酵母中,发现间苹果酸脱氢酶和c苹果酸脱氢酶。参考早期关于酵母中苹果酸脱氢酶活性调节的实验,得出葡萄糖抑制c-苹果酸脱氢酶合成的结论。这种调节机制对细胞是有用的,因为在糖酸循环中c-苹果酸脱氢酶参与乙酸或乙醇的糖异生。当培养基中有葡萄糖时,这种酶就不需要了。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Author index Subject index Insect extramitochondrial glycerophosphate dehydrogenase II. Enzymic properties and amino acid composition of the enzyme from honeybee (Apis mellifera) thoraces The inter-relationships of low redox potential cytochrome c552 and hydrogenase in facultative anaerobes The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli
×
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