Overproduction of glycolytic enzymes in yeast
Eight different enzyymes for glycolysis and alcoholic fermentation were overproduced in a common Saccharomyces cerevisiae strain by placing their genes on multicopy vectors. The specific enzyme activities were increased between 3·7‐and 13·9‐fold above the wild‐type level. The overproduction of the d...
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| Veröffentlicht in: | Yeast (Chichester, England) England), 1989-07, Vol.5 (4), p.285-290 |
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| creator | Schaaff, Ine Heinisch, Jürgen Zimmermann, Friedrich K. |
| description | Eight different enzyymes for glycolysis and alcoholic fermentation were overproduced in a common Saccharomyces cerevisiae strain by placing their genes on multicopy vectors. The specific enzyme activities were increased between 3·7‐and 13·9‐fold above the wild‐type level. The overproduction of the different glycolytic enzymes had no effect on the rate of ethanol formation, even with those enzymes that catalyse irreversible steps: hexokinase, phosphofructokinase and pyruvate kinase. Also the simultaneous increase in the activities of pairs of enzymes such as pyruvate kinase and phosphofructokinase or pyruvate decarboxylase and alcohol dehyrogenase, did not increase the rate of ethanol production. The levels of key glycolytic metabolites were also normal, compared to the reference strain. |
| doi_str_mv | 10.1002/yea.320050408 |
| format | Article |
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The specific enzyme activities were increased between 3·7‐and 13·9‐fold above the wild‐type level. The overproduction of the different glycolytic enzymes had no effect on the rate of ethanol formation, even with those enzymes that catalyse irreversible steps: hexokinase, phosphofructokinase and pyruvate kinase. Also the simultaneous increase in the activities of pairs of enzymes such as pyruvate kinase and phosphofructokinase or pyruvate decarboxylase and alcohol dehyrogenase, did not increase the rate of ethanol production. The levels of key glycolytic metabolites were also normal, compared to the reference strain.</description><identifier>ISSN: 0749-503X</identifier><identifier>EISSN: 1097-0061</identifier><identifier>DOI: 10.1002/yea.320050408</identifier><identifier>PMID: 2528863</identifier><identifier>CODEN: YESTE3</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Alcohol Dehydrogenase - biosynthesis ; Alcohol Dehydrogenase - genetics ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Escherichia coli - genetics ; ethanol ; ethanol production ; Fundamental and applied biological sciences. Psychology ; Genetic Vectors ; Genetics ; Glycolysis ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; Hexokinase - biosynthesis ; Hexokinase - genetics ; metabolic flux ; Microbiology ; Mission oriented research ; Mycology ; Phosphofructokinase-1 - biosynthesis ; Phosphofructokinase-1 - genetics ; Plasmids ; Pyruvate Decarboxylase - biosynthesis ; Pyruvate Decarboxylase - genetics ; Pyruvate Kinase - biosynthesis ; Pyruvate Kinase - genetics ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Transformation, Genetic</subject><ispartof>Yeast (Chichester, England), 1989-07, Vol.5 (4), p.285-290</ispartof><rights>Copyright © 1989 John Wiley & Sons Ltd.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4628-e3e2d05cf5bb8f87f49b484eda68da24e3cf09b2e1fe269aa1b43003d37f3fe23</citedby><cites>FETCH-LOGICAL-c4628-e3e2d05cf5bb8f87f49b484eda68da24e3cf09b2e1fe269aa1b43003d37f3fe23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fyea.320050408$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fyea.320050408$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7364020$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2528863$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schaaff, Ine</creatorcontrib><creatorcontrib>Heinisch, Jürgen</creatorcontrib><creatorcontrib>Zimmermann, Friedrich K.</creatorcontrib><title>Overproduction of glycolytic enzymes in yeast</title><title>Yeast (Chichester, England)</title><addtitle>Yeast</addtitle><description>Eight different enzyymes for glycolysis and alcoholic fermentation were overproduced in a common Saccharomyces cerevisiae strain by placing their genes on multicopy vectors. The specific enzyme activities were increased between 3·7‐and 13·9‐fold above the wild‐type level. The overproduction of the different glycolytic enzymes had no effect on the rate of ethanol formation, even with those enzymes that catalyse irreversible steps: hexokinase, phosphofructokinase and pyruvate kinase. Also the simultaneous increase in the activities of pairs of enzymes such as pyruvate kinase and phosphofructokinase or pyruvate decarboxylase and alcohol dehyrogenase, did not increase the rate of ethanol production. The levels of key glycolytic metabolites were also normal, compared to the reference strain.</description><subject>Alcohol Dehydrogenase - biosynthesis</subject><subject>Alcohol Dehydrogenase - genetics</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Escherichia coli - genetics</subject><subject>ethanol</subject><subject>ethanol production</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Vectors</subject><subject>Genetics</subject><subject>Glycolysis</subject><subject>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</subject><subject>Hexokinase - biosynthesis</subject><subject>Hexokinase - genetics</subject><subject>metabolic flux</subject><subject>Microbiology</subject><subject>Mission oriented research</subject><subject>Mycology</subject><subject>Phosphofructokinase-1 - biosynthesis</subject><subject>Phosphofructokinase-1 - genetics</subject><subject>Plasmids</subject><subject>Pyruvate Decarboxylase - biosynthesis</subject><subject>Pyruvate Decarboxylase - genetics</subject><subject>Pyruvate Kinase - biosynthesis</subject><subject>Pyruvate Kinase - genetics</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Transformation, Genetic</subject><issn>0749-503X</issn><issn>1097-0061</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1Lw0AQxRdRaq0ePQo5iLfU2a9scixSP6DQi4Kels1mViL5qNlEiX-9Ky31pqcHMz_ezHuEnFOYUwB2PaKZcwYgQUB6QKYUMhUDJPSQTEGJLJbAn4_JifdvAJRKlk7IhAVJEz4l8foDu03XFoPty7aJWhe9VqNtq7EvbYTN11ijj8omCmd8f0qOnKk8nu10Rp5ul4839_Fqffdws1jFViQsjZEjK0BaJ_M8dalyIstFKrAwSVoYJpBbB1nOkDpkSWYMzQUH4AVXjocRn5GrrW_47H1A3-u69BaryjTYDl6rjIFSSv4LUskzKUPSGYm3oO1a7zt0etOVtelGTUH_9KhDQL3vMfAXO-Mhr7HY07viwv5ytzfemsp1prGl32OKJwIYBExtsc-ywvHvm_plufh94BtSFYqc</recordid><startdate>198907</startdate><enddate>198907</enddate><creator>Schaaff, Ine</creator><creator>Heinisch, Jürgen</creator><creator>Zimmermann, Friedrich K.</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>198907</creationdate><title>Overproduction of glycolytic enzymes in yeast</title><author>Schaaff, Ine ; Heinisch, Jürgen ; Zimmermann, Friedrich K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4628-e3e2d05cf5bb8f87f49b484eda68da24e3cf09b2e1fe269aa1b43003d37f3fe23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Alcohol Dehydrogenase - biosynthesis</topic><topic>Alcohol Dehydrogenase - genetics</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Escherichia coli - genetics</topic><topic>ethanol</topic><topic>ethanol production</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Vectors</topic><topic>Genetics</topic><topic>Glycolysis</topic><topic>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</topic><topic>Hexokinase - biosynthesis</topic><topic>Hexokinase - genetics</topic><topic>metabolic flux</topic><topic>Microbiology</topic><topic>Mission oriented research</topic><topic>Mycology</topic><topic>Phosphofructokinase-1 - biosynthesis</topic><topic>Phosphofructokinase-1 - genetics</topic><topic>Plasmids</topic><topic>Pyruvate Decarboxylase - biosynthesis</topic><topic>Pyruvate Decarboxylase - genetics</topic><topic>Pyruvate Kinase - biosynthesis</topic><topic>Pyruvate Kinase - genetics</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Transformation, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schaaff, Ine</creatorcontrib><creatorcontrib>Heinisch, Jürgen</creatorcontrib><creatorcontrib>Zimmermann, Friedrich K.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Yeast (Chichester, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schaaff, Ine</au><au>Heinisch, Jürgen</au><au>Zimmermann, Friedrich K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overproduction of glycolytic enzymes in yeast</atitle><jtitle>Yeast (Chichester, England)</jtitle><addtitle>Yeast</addtitle><date>1989-07</date><risdate>1989</risdate><volume>5</volume><issue>4</issue><spage>285</spage><epage>290</epage><pages>285-290</pages><issn>0749-503X</issn><eissn>1097-0061</eissn><coden>YESTE3</coden><abstract>Eight different enzyymes for glycolysis and alcoholic fermentation were overproduced in a common Saccharomyces cerevisiae strain by placing their genes on multicopy vectors. The specific enzyme activities were increased between 3·7‐and 13·9‐fold above the wild‐type level. The overproduction of the different glycolytic enzymes had no effect on the rate of ethanol formation, even with those enzymes that catalyse irreversible steps: hexokinase, phosphofructokinase and pyruvate kinase. Also the simultaneous increase in the activities of pairs of enzymes such as pyruvate kinase and phosphofructokinase or pyruvate decarboxylase and alcohol dehyrogenase, did not increase the rate of ethanol production. The levels of key glycolytic metabolites were also normal, compared to the reference strain.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>2528863</pmid><doi>10.1002/yea.320050408</doi><tpages>6</tpages></addata></record> |
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| ispartof | Yeast (Chichester, England), 1989-07, Vol.5 (4), p.285-290 |
| issn | 0749-503X 1097-0061 |
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| subjects | Alcohol Dehydrogenase - biosynthesis Alcohol Dehydrogenase - genetics Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Escherichia coli - genetics ethanol ethanol production Fundamental and applied biological sciences. Psychology Genetic Vectors Genetics Glycolysis Growth, nutrition, metabolism, transports, enzymes. Molecular biology Hexokinase - biosynthesis Hexokinase - genetics metabolic flux Microbiology Mission oriented research Mycology Phosphofructokinase-1 - biosynthesis Phosphofructokinase-1 - genetics Plasmids Pyruvate Decarboxylase - biosynthesis Pyruvate Decarboxylase - genetics Pyruvate Kinase - biosynthesis Pyruvate Kinase - genetics Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Transformation, Genetic |
| title | Overproduction of glycolytic enzymes in yeast |
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