The activation of glycolysis performed by the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system
Influence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) on glycolysis was investigated. The addition of GAPN—which oxidizes glyceraldehyde-3-phosphate directly to the 3-phosphoglyceric acid—led to the strong increase in the rate of lactate accumulation in the rat muscle extr...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2003-01, Vol.300 (1), p.149-154 |
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| creator | Arutyunov, D.Y Muronetz, V.I |
| description | Influence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) on glycolysis was investigated. The addition of GAPN—which oxidizes glyceraldehyde-3-phosphate directly to the 3-phosphoglyceric acid—led to the strong increase in the rate of lactate accumulation in the rat muscle extract with low ADP content. The lactate accumulation was also observed in the presence of GAPN in rat muscle extract, which contained only ATP and no ADP. This can be the evidence of the “futile cycle” stimulated by GAPN. Here ADP can be regenerated from ATP by the phosphoglycerate kinase reaction. The high resistance of GAPN from
Streptococcus mutans towards inactivation by natural oxidant—H
2O
2 was showed. This feature distinguishes GAPN from phosphorylating glyceraldehyde-3-phosphate dehydrogenase, which is very sensitive to modification by hydrogen peroxide. A possible role of the oxidants and non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the regulation of glycolysis is discussed. |
| doi_str_mv | 10.1016/S0006-291X(02)02802-4 |
| format | Article |
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Streptococcus mutans towards inactivation by natural oxidant—H
2O
2 was showed. This feature distinguishes GAPN from phosphorylating glyceraldehyde-3-phosphate dehydrogenase, which is very sensitive to modification by hydrogen peroxide. A possible role of the oxidants and non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the regulation of glycolysis is discussed.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(02)02802-4</identifier><identifier>PMID: 12480534</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Diphosphate - metabolism ; Adenosine Triphosphate - metabolism ; Animals ; Futile cycle ; Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) - metabolism ; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism ; Glycolysis ; Hydrogen peroxide ; In Vitro Techniques ; Kinetics ; Lactic Acid - metabolism ; Models, Biological ; Muscles - metabolism ; Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase ; Oxidation-Reduction ; Phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase ; Phosphorylation ; Rabbits ; Rats ; Regulation of glycolysis ; Streptococcus mutans - enzymology ; Uncoupling of oxidation and phosphorylation</subject><ispartof>Biochemical and biophysical research communications, 2003-01, Vol.300 (1), p.149-154</ispartof><rights>2002 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2394-dc08b6644a908c0362cf1e214c5800c8a14e6293953449e9a992a2ef5fbf93d73</citedby><cites>FETCH-LOGICAL-c2394-dc08b6644a908c0362cf1e214c5800c8a14e6293953449e9a992a2ef5fbf93d73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X02028024$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12480534$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arutyunov, D.Y</creatorcontrib><creatorcontrib>Muronetz, V.I</creatorcontrib><title>The activation of glycolysis performed by the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Influence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) on glycolysis was investigated. The addition of GAPN—which oxidizes glyceraldehyde-3-phosphate directly to the 3-phosphoglyceric acid—led to the strong increase in the rate of lactate accumulation in the rat muscle extract with low ADP content. The lactate accumulation was also observed in the presence of GAPN in rat muscle extract, which contained only ATP and no ADP. This can be the evidence of the “futile cycle” stimulated by GAPN. Here ADP can be regenerated from ATP by the phosphoglycerate kinase reaction. The high resistance of GAPN from
Streptococcus mutans towards inactivation by natural oxidant—H
2O
2 was showed. This feature distinguishes GAPN from phosphorylating glyceraldehyde-3-phosphate dehydrogenase, which is very sensitive to modification by hydrogen peroxide. A possible role of the oxidants and non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the regulation of glycolysis is discussed.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Futile cycle</subject><subject>Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) - metabolism</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</subject><subject>Glycolysis</subject><subject>Hydrogen peroxide</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Lactic Acid - metabolism</subject><subject>Models, Biological</subject><subject>Muscles - metabolism</subject><subject>Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase</subject><subject>Oxidation-Reduction</subject><subject>Phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase</subject><subject>Phosphorylation</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Regulation of glycolysis</subject><subject>Streptococcus mutans - enzymology</subject><subject>Uncoupling of oxidation and phosphorylation</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LxDAQhoMoun78BCUn0UN1kqbd5CSy-AWCBxW8hWw63Y20zZp0hV787dZu0aOHYWB43hnmfQk5ZnDBgOWXzwCQJ1yxtzPg58Al8ERskQkDBQlnILbJ5BfZI_sxvgMwJnK1S_YYFxKyVEzI18sSqbGt-zSt8w31JV1UnfVVF12kKwylDzUWdN7Rticb3ySrpY99ha7qJc1i4DGYqsBlV2CSjoBpkQ6j4BfYmIjUNcOO2hdY0djFFutDslOaKuLR2A_I6-3Ny-w-eXy6e5hdPyaWp0okhQU5z3MhjAJpIc25LRlyJmwmAaw0TGDOVar6n4RCZZTihmOZlfNSpcU0PSCnm72r4D_WGFtdu2ixqkyDfh31lEupMiH_BZmaqhHMNqANPsaApV4FV5vQaQb6JyE9JKR_7NfA9ZCQFr3uZDywnvfG_qnGSHrgagNg78enw6CjddhYLFxA2-rCu39OfAM1z6Kq</recordid><startdate>20030103</startdate><enddate>20030103</enddate><creator>Arutyunov, D.Y</creator><creator>Muronetz, V.I</creator><general>Elsevier Inc</general><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>C1K</scope><scope>7X8</scope></search><sort><creationdate>20030103</creationdate><title>The activation of glycolysis performed by the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system</title><author>Arutyunov, D.Y ; Muronetz, V.I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2394-dc08b6644a908c0362cf1e214c5800c8a14e6293953449e9a992a2ef5fbf93d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adenosine Diphosphate - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Futile cycle</topic><topic>Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) - metabolism</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</topic><topic>Glycolysis</topic><topic>Hydrogen peroxide</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Lactic Acid - metabolism</topic><topic>Models, Biological</topic><topic>Muscles - metabolism</topic><topic>Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase</topic><topic>Oxidation-Reduction</topic><topic>Phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase</topic><topic>Phosphorylation</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Regulation of glycolysis</topic><topic>Streptococcus mutans - enzymology</topic><topic>Uncoupling of oxidation and phosphorylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arutyunov, D.Y</creatorcontrib><creatorcontrib>Muronetz, V.I</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arutyunov, D.Y</au><au>Muronetz, V.I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The activation of glycolysis performed by the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2003-01-03</date><risdate>2003</risdate><volume>300</volume><issue>1</issue><spage>149</spage><epage>154</epage><pages>149-154</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Influence of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) on glycolysis was investigated. The addition of GAPN—which oxidizes glyceraldehyde-3-phosphate directly to the 3-phosphoglyceric acid—led to the strong increase in the rate of lactate accumulation in the rat muscle extract with low ADP content. The lactate accumulation was also observed in the presence of GAPN in rat muscle extract, which contained only ATP and no ADP. This can be the evidence of the “futile cycle” stimulated by GAPN. Here ADP can be regenerated from ATP by the phosphoglycerate kinase reaction. The high resistance of GAPN from
Streptococcus mutans towards inactivation by natural oxidant—H
2O
2 was showed. This feature distinguishes GAPN from phosphorylating glyceraldehyde-3-phosphate dehydrogenase, which is very sensitive to modification by hydrogen peroxide. A possible role of the oxidants and non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the regulation of glycolysis is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12480534</pmid><doi>10.1016/S0006-291X(02)02802-4</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2003-01, Vol.300 (1), p.149-154 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Diphosphate - metabolism Adenosine Triphosphate - metabolism Animals Futile cycle Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) - metabolism Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism Glycolysis Hydrogen peroxide In Vitro Techniques Kinetics Lactic Acid - metabolism Models, Biological Muscles - metabolism Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase Oxidation-Reduction Phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase Phosphorylation Rabbits Rats Regulation of glycolysis Streptococcus mutans - enzymology Uncoupling of oxidation and phosphorylation |
| title | The activation of glycolysis performed by the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system |
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