Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91026-6
R.H. De Deken
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.
{"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":"10.1016/0006-3002(63)91026-6","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":0.0,"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":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673334","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91047-3
P. Herrlich, C.E. Sekeris
{"title":"Vorkommen von Protocatechualdehyd bei einem fall von bösartigem phäochromocytom","authors":"P. Herrlich, C.E. Sekeris","doi":"10.1016/0006-3002(63)91047-3","DOIUrl":"10.1016/0006-3002(63)91047-3","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Page 750"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91047-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673352","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91057-6
G.R. Fritz, E. Knobil
{"title":"The effect of insulin on extracellular space and tissue-water content of the isolated rat diaphragm","authors":"G.R. Fritz, E. Knobil","doi":"10.1016/0006-3002(63)91057-6","DOIUrl":"10.1016/0006-3002(63)91057-6","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 773-774"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91057-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673154","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91059-X
P.H. Jellinck, Louise Irwin
{"title":"Interaction of oestrogen quinones with ethylene diamine","authors":"P.H. Jellinck, Louise Irwin","doi":"10.1016/0006-3002(63)91059-X","DOIUrl":"10.1016/0006-3002(63)91059-X","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 778-780"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91059-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91046-1
Bernard J. Finkle, Richard F. Nelson
{"title":"Enzyme reactions with phenolic compounds: a meta-O-methyltransferase in plants","authors":"Bernard J. Finkle, Richard F. Nelson","doi":"10.1016/0006-3002(63)91046-1","DOIUrl":"10.1016/0006-3002(63)91046-1","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 747-749"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91046-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74551021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
1. An enzyme which catalyses the transamination between γ-hydroxyglutamate and α-ketoglutarate was extracted from rat-liver acetone powder and purified in excess of 15-fold. Fractionation of the enzyme from a separate aspartate transaminase (L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) remained incomplete.
2.
2. [2-14C]Pyruvate was incorporated into γ-hydroxy-α-ketoglutarate and γ-hydroxyglutamate in the presence of glyoxylate in rat-liver homogenate. Specific activity values of these three compounds indicated the occurence of the following pathway: Pyruvate + glyoxylate ⇌ γ-hydroxy-α-ketoglutarate ⇌ γ-hydroxyglutamate.
3.
3. A further possible pathway of γ-hydroxy-α-ketoglutarate metabolism leading to malate and of γ-hydroxyglutamate to its decarboxylation product or to L-hydroxyproline were inferred and discussed.
{"title":"The metabolism of γ-hydroxyglutamate in rat liver II. A transaminase concerned in γ-hydroxyglutamate metabolism","authors":"Kazuoki Kuratomi, Keiko Fukunaga, Yasuko Kobayashi","doi":"10.1016/0006-3002(63)91028-X","DOIUrl":"10.1016/0006-3002(63)91028-X","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. An enzyme which catalyses the transamination between γ-hydroxyglutamate and α-ketoglutarate was extracted from rat-liver acetone powder and purified in excess of 15-fold. Fractionation of the enzyme from a separate aspartate transaminase (<span>L</span>-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) remained incomplete.</p></span></li><li><span>2.</span><span><p>2. [2-<sup>14</sup>C]Pyruvate was incorporated into γ-hydroxy-α-ketoglutarate and γ-hydroxyglutamate in the presence of glyoxylate in rat-liver homogenate. Specific activity values of these three compounds indicated the occurence of the following pathway: Pyruvate + glyoxylate ⇌ γ-hydroxy-α-ketoglutarate ⇌ γ-hydroxyglutamate.</p></span></li><li><span>3.</span><span><p>3. A further possible pathway of γ-hydroxy-α-ketoglutarate metabolism leading to malate and of γ-hydroxyglutamate to its decarboxylation product or to <span>L</span>-hydroxyproline were inferred and discussed.</p></span></li></ul></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 629-636"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91028-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673336","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91043-6
J. Green, A.T. Diplock, J. Bunyan, D. McHale
{"title":"Biosynthesis of ubiquinone and ubichromenol","authors":"J. Green, A.T. Diplock, J. Bunyan, D. McHale","doi":"10.1016/0006-3002(63)91043-6","DOIUrl":"10.1016/0006-3002(63)91043-6","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 739-741"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91043-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673349","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91048-5
James C. Peskin, Bruce B. Love
{"title":"The reaction of l-cysteine with all-trans-retinene","authors":"James C. Peskin, Bruce B. Love","doi":"10.1016/0006-3002(63)91048-5","DOIUrl":"10.1016/0006-3002(63)91048-5","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 751-753"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91048-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673145","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91051-5
Hugues J.-P. Ryser
{"title":"Comparison of the incorporation of tyrosine and its iodinated analogs into the proteins of Ehrlich ascites tumor cells and rat-liver slices","authors":"Hugues J.-P. Ryser","doi":"10.1016/0006-3002(63)91051-5","DOIUrl":"10.1016/0006-3002(63)91051-5","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 759-762"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91051-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673148","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1963-12-13Epub Date: 2003-02-09DOI: 10.1016/0006-3002(63)91061-8
S.R. Wagle , H.P. Morris , George Weber
{"title":"Phosphopyruvate carboxylase in liver tumors of different growth rates","authors":"S.R. Wagle , H.P. Morris , George Weber","doi":"10.1016/0006-3002(63)91061-8","DOIUrl":"10.1016/0006-3002(63)91061-8","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 783-785"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91061-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673158","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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