The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae
► Pgm1, Pgm2, and Pgm3 accept glucose-1-P and ribose-1-P as substrates in vitro. ► Ribose-1-P is formed in vivo upon perturbation of energetic equilibrium. ► Ribose-1-P only hyper-accumulates in mutants carrying a deletion in PGM3. ► Pgm3 is the major phosphoribomutase in yeast. The phosphoglucomuta...
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| Veröffentlicht in: | FEBS letters 2012-11, Vol.586 (23), p.4114-4118 |
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| creator | Walther, Thomas Baylac, Audrey Alkim, Ceren Vax, Amélie Cordier, Hélène François, Jean Marie |
| description | ► Pgm1, Pgm2, and Pgm3 accept glucose-1-P and ribose-1-P as substrates in vitro. ► Ribose-1-P is formed in vivo upon perturbation of energetic equilibrium. ► Ribose-1-P only hyper-accumulates in mutants carrying a deletion in PGM3. ► Pgm3 is the major phosphoribomutase in yeast.
The phosphoglucomutases (PGM) Pgm1, Pgm2, and Pgm3 of the yeast Saccharomyces cerevisiae were tested for their ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins were studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate. All tested enzymes were active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins had almost equal kinetic properties on ribose-1-phosphate, but Pgm2 had a 2000 times higher preference for glucose-1-phosphate when compared to Pgm3. The in vivo function of the PGMs was characterized by monitoring ribose-1-phosphate kinetics following a perturbation of the purine nucleotide balance. Only mutants with a deletion of PGM3 hyper-accumulated ribose-1-phosphate. We conclude that Pgm3 functions as the major phosphoribomutase in vivo. |
| doi_str_mv | 10.1016/j.febslet.2012.09.042 |
| format | Article |
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The phosphoglucomutases (PGM) Pgm1, Pgm2, and Pgm3 of the yeast Saccharomyces cerevisiae were tested for their ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins were studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate. All tested enzymes were active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins had almost equal kinetic properties on ribose-1-phosphate, but Pgm2 had a 2000 times higher preference for glucose-1-phosphate when compared to Pgm3. The in vivo function of the PGMs was characterized by monitoring ribose-1-phosphate kinetics following a perturbation of the purine nucleotide balance. Only mutants with a deletion of PGM3 hyper-accumulated ribose-1-phosphate. We conclude that Pgm3 functions as the major phosphoribomutase in vivo.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2012.09.042</identifier><identifier>PMID: 23103740</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Glucosephosphates - metabolism ; Life Sciences ; Phosphoglucomutase - genetics ; Phosphoglucomutase - metabolism ; Phosphoribomutase ; Purine nucleotide metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Substrate Specificity ; Yeast</subject><ispartof>FEBS letters, 2012-11, Vol.586 (23), p.4114-4118</ispartof><rights>2012 Federation of European Biochemical Societies</rights><rights>FEBS Letters 586 (2012) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6438-a354cadfbff77e949fa61d96f140f9c95c7db7d86e448aab75319fe975f1b46a3</citedby><cites>FETCH-LOGICAL-c6438-a354cadfbff77e949fa61d96f140f9c95c7db7d86e448aab75319fe975f1b46a3</cites><orcidid>0000-0001-9884-5535 ; 0000-0003-1634-621X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2012.09.042$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2012.09.042$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23103740$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01268257$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Walther, Thomas</creatorcontrib><creatorcontrib>Baylac, Audrey</creatorcontrib><creatorcontrib>Alkim, Ceren</creatorcontrib><creatorcontrib>Vax, Amélie</creatorcontrib><creatorcontrib>Cordier, Hélène</creatorcontrib><creatorcontrib>François, Jean Marie</creatorcontrib><title>The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>► Pgm1, Pgm2, and Pgm3 accept glucose-1-P and ribose-1-P as substrates in vitro. ► Ribose-1-P is formed in vivo upon perturbation of energetic equilibrium. ► Ribose-1-P only hyper-accumulates in mutants carrying a deletion in PGM3. ► Pgm3 is the major phosphoribomutase in yeast.
The phosphoglucomutases (PGM) Pgm1, Pgm2, and Pgm3 of the yeast Saccharomyces cerevisiae were tested for their ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins were studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate. All tested enzymes were active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins had almost equal kinetic properties on ribose-1-phosphate, but Pgm2 had a 2000 times higher preference for glucose-1-phosphate when compared to Pgm3. The in vivo function of the PGMs was characterized by monitoring ribose-1-phosphate kinetics following a perturbation of the purine nucleotide balance. Only mutants with a deletion of PGM3 hyper-accumulated ribose-1-phosphate. We conclude that Pgm3 functions as the major phosphoribomutase in vivo.</description><subject>Glucosephosphates - metabolism</subject><subject>Life Sciences</subject><subject>Phosphoglucomutase - genetics</subject><subject>Phosphoglucomutase - metabolism</subject><subject>Phosphoribomutase</subject><subject>Purine nucleotide metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Substrate Specificity</subject><subject>Yeast</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV1v0zAUhi0EYmXwE0C5hIsEO3b8cYW2aVuRikDaEJeW4xxTV0ld7LSo_x5n6XY7LizLx895feQHofcEVwQT_nlTOWhTD2NVY1JXWFWY1S_QgkhBS8q4fIkWGBNWNkLRM_QmpQ3OZ0nUa3RWU4KpYHiBft2vofhx-40Wv2ELBWxt6CAVY64OZhNisVuHlFf0bRj2o0lQ-O3D9RFMGos7Y-3axDAcbW6zEOHgkzfwFr1ypk_w7rSfo5831_dXy3L1_fbr1cWqtJxRWRraMGs61zonBCimnOGkU9wRhp2yqrGia0UnOTAmjWlFQ4lyoETjSMu4oefo05y7Nr3eRT-YeNTBeL28WOmplj-Hy7oRB5LZjzO7i-HPHtKoB58s9L3ZQtgnTSiTTBIq2fMoUSLDhKqMNjNqY0gpgnsag2A9qdIbfVKlJ1UaK51V5b4Ppyf27QDdU9ejmwwsZ-Cv7-H4f6n65vqyvpu8T9pJjbHgTOaoL3MUZBUHD1En67Nr6HwEO-ou-Gem_QffJbwl</recordid><startdate>20121130</startdate><enddate>20121130</enddate><creator>Walther, Thomas</creator><creator>Baylac, Audrey</creator><creator>Alkim, Ceren</creator><creator>Vax, Amélie</creator><creator>Cordier, Hélène</creator><creator>François, Jean Marie</creator><general>Elsevier B.V</general><general>Wiley</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0001-9884-5535</orcidid><orcidid>https://orcid.org/0000-0003-1634-621X</orcidid></search><sort><creationdate>20121130</creationdate><title>The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae</title><author>Walther, Thomas ; Baylac, Audrey ; Alkim, Ceren ; Vax, Amélie ; Cordier, Hélène ; François, Jean Marie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6438-a354cadfbff77e949fa61d96f140f9c95c7db7d86e448aab75319fe975f1b46a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Glucosephosphates - metabolism</topic><topic>Life Sciences</topic><topic>Phosphoglucomutase - genetics</topic><topic>Phosphoglucomutase - metabolism</topic><topic>Phosphoribomutase</topic><topic>Purine nucleotide metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Substrate Specificity</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Walther, Thomas</creatorcontrib><creatorcontrib>Baylac, Audrey</creatorcontrib><creatorcontrib>Alkim, Ceren</creatorcontrib><creatorcontrib>Vax, Amélie</creatorcontrib><creatorcontrib>Cordier, Hélène</creatorcontrib><creatorcontrib>François, Jean Marie</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Walther, Thomas</au><au>Baylac, Audrey</au><au>Alkim, Ceren</au><au>Vax, Amélie</au><au>Cordier, Hélène</au><au>François, Jean Marie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2012-11-30</date><risdate>2012</risdate><volume>586</volume><issue>23</issue><spage>4114</spage><epage>4118</epage><pages>4114-4118</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>► Pgm1, Pgm2, and Pgm3 accept glucose-1-P and ribose-1-P as substrates in vitro. ► Ribose-1-P is formed in vivo upon perturbation of energetic equilibrium. ► Ribose-1-P only hyper-accumulates in mutants carrying a deletion in PGM3. ► Pgm3 is the major phosphoribomutase in yeast.
The phosphoglucomutases (PGM) Pgm1, Pgm2, and Pgm3 of the yeast Saccharomyces cerevisiae were tested for their ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins were studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate. All tested enzymes were active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins had almost equal kinetic properties on ribose-1-phosphate, but Pgm2 had a 2000 times higher preference for glucose-1-phosphate when compared to Pgm3. The in vivo function of the PGMs was characterized by monitoring ribose-1-phosphate kinetics following a perturbation of the purine nucleotide balance. Only mutants with a deletion of PGM3 hyper-accumulated ribose-1-phosphate. We conclude that Pgm3 functions as the major phosphoribomutase in vivo.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>23103740</pmid><doi>10.1016/j.febslet.2012.09.042</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0001-9884-5535</orcidid><orcidid>https://orcid.org/0000-0003-1634-621X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection |
| subjects | Glucosephosphates - metabolism Life Sciences Phosphoglucomutase - genetics Phosphoglucomutase - metabolism Phosphoribomutase Purine nucleotide metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Substrate Specificity Yeast |
| title | The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae |
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