{"title":"Biosynthèse de l'arginine chez la levure I. Le sort de la Nα-acétylornithine","authors":"R.H. De Deken","doi":"10.1016/0006-3002(63)91026-6","DOIUrl":null,"url":null,"abstract":"<div><p>An enzyme, transferring the acetyl group of <em>N</em>-<em>α</em>-acetylornithine to the amino group of glutamate, has been demonstrated for <em>Saccharomyces cerevisiae</em>. On the other hand, the enzymic reduction of <em>N</em>-<em>α</em>-acetylglutamate with the formation of <em>N</em>-<em>α</em>-acetyl-glutamic-<em>γ</em>-semialdehyde has been reported previously. The absence of transacetylase in an arginine-requiring mutant (gene <em>ar</em><sub>7</sub>) as well as the above findings prove that: </p><ul><li><span>1.</span><span><p>1. The biosynthesis of ornithine, in yeast, proceeds through acetylated intermediates.</p></span></li><li><span>2.</span><span><p>2. The transacetylase is the only functional pathway for the conversion of <em>N</em>-<em>α</em>-acetylornithine to ornithine, in spite of the simultaneous presence of an <em>N</em>-<em>α</em>-acetylornithinase (<em>N</em>-<em>α</em>-acetylornithine amidohydrolase).</p></span></li></ul><p>At least two steps in the biosynthesis of ornithine are repressible by arginine.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 606-616"},"PeriodicalIF":0.0000,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91026-6","citationCount":"32","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et biophysica acta","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0006300263910266","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 32
Abstract
An enzyme, transferring the acetyl group of N-α-acetylornithine to the amino group of glutamate, has been demonstrated for Saccharomyces cerevisiae. On the other hand, the enzymic reduction of N-α-acetylglutamate with the formation of N-α-acetyl-glutamic-γ-semialdehyde has been reported previously. The absence of transacetylase in an arginine-requiring mutant (gene ar7) as well as the above findings prove that:
1.
1. The biosynthesis of ornithine, in yeast, proceeds through acetylated intermediates.
2.
2. The transacetylase is the only functional pathway for the conversion of N-α-acetylornithine to ornithine, in spite of the simultaneous presence of an N-α-acetylornithinase (N-α-acetylornithine amidohydrolase).
At least two steps in the biosynthesis of ornithine are repressible by arginine.