Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum
Glutamate is industrially produced by fermentation using Corynebacterium glutamicum. The key factor for efficient glutamate production by this microorganism has been considered to be a metabolic change at the 2-oxoglutarate dehydrogenase (ODH) branch point caused by a decrease in ODH activity under...
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creator | Hasegawa, Takuo Hashimoto, Ken-Ichi Kawasaki, Hisashi Nakamatsu, Tsuyoshi |
description | Glutamate is industrially produced by fermentation using
Corynebacterium glutamicum. The key factor for efficient glutamate production by this microorganism has been considered to be a metabolic change at the 2-oxoglutarate dehydrogenase (ODH) branch point caused by a decrease in ODH activity under glutamate-overproducing conditions. However, this change would be insufficient because the ODH branch is merely the final branch in the glutamate biosynthetic pathway, and efficient glutamate production requires a balanced supply of acetyl-CoA and oxaloacetate (OAA), which are condensed to form a precursor of glutamate, namely, citrate. Therefore, there must be another (other) change(s) in metabolic flux. In this study, we demonstrated that a decrease in pyruvate dehydrogenase (PDH) activity catalyzes the conversion of pyruvate to acetyl-CoA. It is speculated that carbon flux from pyruvate to acetyl-CoA decreases under glutamate-overproducing conditions. Furthermore, an increase in pyruvate carboxylase (PC) activity, which catalyzes the reaction of pyruvate to OAA, is evident under glutamate-overproducing conditions, except under biotin-limited condition, which may lead to an increase in carbon flux from pyruvate to OAA. These data suggest that a novel metabolic change occurs at the pyruvate node, leading to a high yield of glutamate through adequate partitioning of the carbon flux. |
doi_str_mv | 10.1263/jbb.105.12 |
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Corynebacterium glutamicum. The key factor for efficient glutamate production by this microorganism has been considered to be a metabolic change at the 2-oxoglutarate dehydrogenase (ODH) branch point caused by a decrease in ODH activity under glutamate-overproducing conditions. However, this change would be insufficient because the ODH branch is merely the final branch in the glutamate biosynthetic pathway, and efficient glutamate production requires a balanced supply of acetyl-CoA and oxaloacetate (OAA), which are condensed to form a precursor of glutamate, namely, citrate. Therefore, there must be another (other) change(s) in metabolic flux. In this study, we demonstrated that a decrease in pyruvate dehydrogenase (PDH) activity catalyzes the conversion of pyruvate to acetyl-CoA. It is speculated that carbon flux from pyruvate to acetyl-CoA decreases under glutamate-overproducing conditions. Furthermore, an increase in pyruvate carboxylase (PC) activity, which catalyzes the reaction of pyruvate to OAA, is evident under glutamate-overproducing conditions, except under biotin-limited condition, which may lead to an increase in carbon flux from pyruvate to OAA. These data suggest that a novel metabolic change occurs at the pyruvate node, leading to a high yield of glutamate through adequate partitioning of the carbon flux.</description><subject>Acetyl Coenzyme A - metabolism</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Corynebacterium glutamicum</subject><subject>Corynebacterium glutamicum - enzymology</subject><subject>Down-Regulation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glutamate overproduction</subject><subject>Glutamic Acid - biosynthesis</subject><subject>Industrial Microbiology</subject><subject>metabolic change</subject><subject>Oxaloacetic Acid - metabolism</subject><subject>pyruvate</subject><subject>pyruvate carboxylase</subject><subject>Pyruvate Carboxylase - metabolism</subject><subject>pyruvate dehydrogenase</subject><subject>Pyruvate Dehydrogenase Complex - metabolism</subject><subject>Pyruvic Acid - metabolism</subject><issn>1389-1723</issn><issn>1347-4421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c2r1DAQAPAgiu-5evEP0ILoQegzk4-mPcriFzzwoO8c0nTSl6VN16RdWP96U7YoiOApM8OPYSZDyHOgN8Aq_u7QtjdAZU4ekGvgQpVCMHi4xnVTgmL8ijxJ6UApKKrgMbmCmjVSgbgm_f7ehB5T4UOB4ed5xMLY2Z_87HPRzMV8j8XxHJeTmbEIU4er7IdlNmOulNMJ4zFO3WJ96Iv9FM8B29wBo1_GzXm7jE_JI2eGhM-2d0fuPn74vv9c3n799GX__ra0ksq5hI61CsGgcBwpUFc5pdrada00DqGFCvISLVIHtGmM4UJWkoqu4aauBXR8R95c-uahfiyYZj36ZHEYTMBpSVpRzmlTV_-F0EguV70jr_6Ch2mJIS-hQQjgrFFyVW8vysYppYhOH6MfTTxroHq9ks5XyrHMScYvtpZLO2L3h25nyeD1BkyyZnDRBOvTb8coVUywdYmXF-fMpE0fs7n7xihwSmvFmVjnEheB-dNPHqNO1mOw2PmIdtbd5P814S8GXrXl</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Hasegawa, Takuo</creator><creator>Hashimoto, Ken-Ichi</creator><creator>Kawasaki, Hisashi</creator><creator>Nakamatsu, Tsuyoshi</creator><general>Elsevier B.V</general><general>Osaka, Japan: Society for Bioscience and Bioengineering, Japan; Amsterdam, the Netherlands: Distributed outside Japan by Elsevier Science</general><general>Elsevier Science</general><general>Elsevier Limited</general><scope>FBQ</scope><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>P64</scope><scope>7X8</scope></search><sort><creationdate>2008</creationdate><title>Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum</title><author>Hasegawa, Takuo ; Hashimoto, Ken-Ichi ; Kawasaki, Hisashi ; Nakamatsu, Tsuyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-1d2b7e1ae4f3e010f6f77b8fdb5afe1b161017be0f1099aa3456504d93a8841d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Acetyl Coenzyme A - metabolism</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Corynebacterium glutamicum</topic><topic>Corynebacterium glutamicum - enzymology</topic><topic>Down-Regulation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glutamate overproduction</topic><topic>Glutamic Acid - biosynthesis</topic><topic>Industrial Microbiology</topic><topic>metabolic change</topic><topic>Oxaloacetic Acid - metabolism</topic><topic>pyruvate</topic><topic>pyruvate carboxylase</topic><topic>Pyruvate Carboxylase - metabolism</topic><topic>pyruvate dehydrogenase</topic><topic>Pyruvate Dehydrogenase Complex - metabolism</topic><topic>Pyruvic Acid - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hasegawa, Takuo</creatorcontrib><creatorcontrib>Hashimoto, Ken-Ichi</creatorcontrib><creatorcontrib>Kawasaki, Hisashi</creatorcontrib><creatorcontrib>Nakamatsu, Tsuyoshi</creatorcontrib><collection>AGRIS</collection><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>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of bioscience and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hasegawa, Takuo</au><au>Hashimoto, Ken-Ichi</au><au>Kawasaki, Hisashi</au><au>Nakamatsu, Tsuyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum</atitle><jtitle>Journal of bioscience and bioengineering</jtitle><addtitle>J Biosci Bioeng</addtitle><date>2008</date><risdate>2008</risdate><volume>105</volume><issue>1</issue><spage>12</spage><epage>19</epage><pages>12-19</pages><issn>1389-1723</issn><eissn>1347-4421</eissn><coden>JFBIEX</coden><abstract>Glutamate is industrially produced by fermentation using
Corynebacterium glutamicum. The key factor for efficient glutamate production by this microorganism has been considered to be a metabolic change at the 2-oxoglutarate dehydrogenase (ODH) branch point caused by a decrease in ODH activity under glutamate-overproducing conditions. However, this change would be insufficient because the ODH branch is merely the final branch in the glutamate biosynthetic pathway, and efficient glutamate production requires a balanced supply of acetyl-CoA and oxaloacetate (OAA), which are condensed to form a precursor of glutamate, namely, citrate. Therefore, there must be another (other) change(s) in metabolic flux. In this study, we demonstrated that a decrease in pyruvate dehydrogenase (PDH) activity catalyzes the conversion of pyruvate to acetyl-CoA. It is speculated that carbon flux from pyruvate to acetyl-CoA decreases under glutamate-overproducing conditions. Furthermore, an increase in pyruvate carboxylase (PC) activity, which catalyzes the reaction of pyruvate to OAA, is evident under glutamate-overproducing conditions, except under biotin-limited condition, which may lead to an increase in carbon flux from pyruvate to OAA. These data suggest that a novel metabolic change occurs at the pyruvate node, leading to a high yield of glutamate through adequate partitioning of the carbon flux.</abstract><cop>Amsterdarm</cop><pub>Elsevier B.V</pub><pmid>18295714</pmid><doi>10.1263/jbb.105.12</doi><tpages>8</tpages></addata></record> |
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subjects | Acetyl Coenzyme A - metabolism Bacterial Proteins - metabolism Biological and medical sciences Biotechnology Corynebacterium glutamicum Corynebacterium glutamicum - enzymology Down-Regulation Fundamental and applied biological sciences. Psychology glutamate overproduction Glutamic Acid - biosynthesis Industrial Microbiology metabolic change Oxaloacetic Acid - metabolism pyruvate pyruvate carboxylase Pyruvate Carboxylase - metabolism pyruvate dehydrogenase Pyruvate Dehydrogenase Complex - metabolism Pyruvic Acid - metabolism |
title | Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum |
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