Alanine : glyoxylate aminotransferase of Saccharomyces cerevisiae–encoding gene AGX1 and metabolic significance
Alanine : glyoxylate aminotransferase is one of three different enzymes used for glycine synthesis in Saccharomyces cerevisiae. The open reading frame YFL030w (named AGX1 in the following), encoding this enzyme, was identified by comparing enzyme specific activities in knockout strains. While 100% a...
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| Veröffentlicht in: | Yeast (Chichester, England) England), 2004-01, Vol.21 (1), p.63-73 |
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| creator | Schlösser, Thomas Gätgens, Cornelia Weber, Ulrike Stahmann, K.‐Peter |
| description | Alanine : glyoxylate aminotransferase is one of three different enzymes used for glycine synthesis in Saccharomyces cerevisiae. The open reading frame YFL030w (named AGX1 in the following), encoding this enzyme, was identified by comparing enzyme specific activities in knockout strains. While 100% activity was detectable in the parental strain, 2% was found in a YFL030w::kanMX4 strain. The ORF found at that locus was suspected to encode alanine : glyoxylate aminotransferase because its predicted amino acid sequence showed 23% identity to the human homologue. Since the YFL030w::kanMX4 strain showed no glycine auxtrophic phenotype, AGX1 was replaced by KanMX4 in a Δ GLY1Δ SHM1Δ SHM2 background. These background mutations, which cause inactivation of threonine aldolase, mitochondrial and cytosolic serine hydroxymethyltransferase, respectively, lead to a conditional glycine auxotrophy. This means that growth is not possible on glucose but on ethanol as the sole carbon source. Additional disruption of AGX1 revealed a complete glycine auxotrophy. Complementation was observed by transformation with a plasmid‐encoded AGX1. Copyright © 2003 John Wiley & Sons, Ltd. |
| doi_str_mv | 10.1002/yea.1058 |
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The open reading frame YFL030w (named AGX1 in the following), encoding this enzyme, was identified by comparing enzyme specific activities in knockout strains. While 100% activity was detectable in the parental strain, 2% was found in a YFL030w::kanMX4 strain. The ORF found at that locus was suspected to encode alanine : glyoxylate aminotransferase because its predicted amino acid sequence showed 23% identity to the human homologue. Since the YFL030w::kanMX4 strain showed no glycine auxtrophic phenotype, AGX1 was replaced by KanMX4 in a Δ GLY1Δ SHM1Δ SHM2 background. These background mutations, which cause inactivation of threonine aldolase, mitochondrial and cytosolic serine hydroxymethyltransferase, respectively, lead to a conditional glycine auxotrophy. This means that growth is not possible on glucose but on ethanol as the sole carbon source. Additional disruption of AGX1 revealed a complete glycine auxotrophy. Complementation was observed by transformation with a plasmid‐encoded AGX1. Copyright © 2003 John Wiley & Sons, Ltd.</description><identifier>ISSN: 0749-503X</identifier><identifier>EISSN: 1097-0061</identifier><identifier>DOI: 10.1002/yea.1058</identifier><identifier>PMID: 14745783</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Alanine - metabolism ; alanine : glyoxylate aminotransferase ; amino acid metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; DNA, Fungal - chemistry ; DNA, Fungal - genetics ; fungi ; Glycine - biosynthesis ; Glyoxylates - metabolism ; Humans ; Models, Chemical ; Molecular Sequence Data ; Mutagenesis, Insertional ; Orotic Acid - analogs & derivatives ; Orotic Acid - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Selection, Genetic ; Sequence Alignment ; Transaminases - genetics ; Transaminases - metabolism</subject><ispartof>Yeast (Chichester, England), 2004-01, Vol.21 (1), p.63-73</ispartof><rights>Copyright © 2003 John Wiley & Sons, Ltd.</rights><rights>Copyright 2003 John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3488-c0200303f4e737e18d7233cc0bfcc9ff8f91bd80e072e1f64a353384c966e20b3</citedby><cites>FETCH-LOGICAL-c3488-c0200303f4e737e18d7233cc0bfcc9ff8f91bd80e072e1f64a353384c966e20b3</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.1058$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fyea.1058$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14745783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schlösser, Thomas</creatorcontrib><creatorcontrib>Gätgens, Cornelia</creatorcontrib><creatorcontrib>Weber, Ulrike</creatorcontrib><creatorcontrib>Stahmann, K.‐Peter</creatorcontrib><title>Alanine : glyoxylate aminotransferase of Saccharomyces cerevisiae–encoding gene AGX1 and metabolic significance</title><title>Yeast (Chichester, England)</title><addtitle>Yeast</addtitle><description>Alanine : glyoxylate aminotransferase is one of three different enzymes used for glycine synthesis in Saccharomyces cerevisiae. The open reading frame YFL030w (named AGX1 in the following), encoding this enzyme, was identified by comparing enzyme specific activities in knockout strains. While 100% activity was detectable in the parental strain, 2% was found in a YFL030w::kanMX4 strain. The ORF found at that locus was suspected to encode alanine : glyoxylate aminotransferase because its predicted amino acid sequence showed 23% identity to the human homologue. Since the YFL030w::kanMX4 strain showed no glycine auxtrophic phenotype, AGX1 was replaced by KanMX4 in a Δ GLY1Δ SHM1Δ SHM2 background. These background mutations, which cause inactivation of threonine aldolase, mitochondrial and cytosolic serine hydroxymethyltransferase, respectively, lead to a conditional glycine auxotrophy. This means that growth is not possible on glucose but on ethanol as the sole carbon source. Additional disruption of AGX1 revealed a complete glycine auxotrophy. Complementation was observed by transformation with a plasmid‐encoded AGX1. Copyright © 2003 John Wiley & Sons, Ltd.</description><subject>Alanine - metabolism</subject><subject>alanine : glyoxylate aminotransferase</subject><subject>amino acid metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>DNA, Fungal - chemistry</subject><subject>DNA, Fungal - genetics</subject><subject>fungi</subject><subject>Glycine - biosynthesis</subject><subject>Glyoxylates - metabolism</subject><subject>Humans</subject><subject>Models, Chemical</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Insertional</subject><subject>Orotic Acid - analogs & derivatives</subject><subject>Orotic Acid - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Selection, Genetic</subject><subject>Sequence Alignment</subject><subject>Transaminases - genetics</subject><subject>Transaminases - metabolism</subject><issn>0749-503X</issn><issn>1097-0061</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFO3DAQhq0KVLZQiSeofKp6CYzjZO30tlptaSUkDhSJniJnMl5cJTbYWWhuvANvyJM0sCtx4jRz-PRJ_8fYsYATAZCfjmSmp9Qf2ExApTKAudhjM1BFlZUgrw_Yp5T-AghR5vojOxCFKkql5YzdLTrjnSf-na-7MfwbOzMQN73zYYjGJ0vRJOLB8kuDeGNi6EekxJEi3bvkDD0_PpHH0Dq_5muaTIuza8GNb3lPg2lC55Ant_bOOjQe6YjtW9Ml-ry7h-zqx-r38md2fnH2a7k4z1AWWmcIOYAEaQtSUpHQrcqlRITGIlbWaluJptVAoHISdl4YWUqpC6zmc8qhkYfs69Z7G8PdhtJQ9y4hddNeCptUC1UVErScwG9bEGNIKZKtb6PrTRxrAfVL3nrKW7_kndAvO-em6al9A3c9JyDbAg-uo_FdUf1ntXgV_gdxyYX1</recordid><startdate>20040115</startdate><enddate>20040115</enddate><creator>Schlösser, Thomas</creator><creator>Gätgens, Cornelia</creator><creator>Weber, Ulrike</creator><creator>Stahmann, K.‐Peter</creator><general>John Wiley & Sons, Ltd</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20040115</creationdate><title>Alanine : glyoxylate aminotransferase of Saccharomyces cerevisiae–encoding gene AGX1 and metabolic significance</title><author>Schlösser, Thomas ; Gätgens, Cornelia ; Weber, Ulrike ; Stahmann, K.‐Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3488-c0200303f4e737e18d7233cc0bfcc9ff8f91bd80e072e1f64a353384c966e20b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Alanine - metabolism</topic><topic>alanine : glyoxylate aminotransferase</topic><topic>amino acid metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>DNA, Fungal - chemistry</topic><topic>DNA, Fungal - genetics</topic><topic>fungi</topic><topic>Glycine - biosynthesis</topic><topic>Glyoxylates - metabolism</topic><topic>Humans</topic><topic>Models, Chemical</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Insertional</topic><topic>Orotic Acid - analogs & derivatives</topic><topic>Orotic Acid - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Selection, Genetic</topic><topic>Sequence Alignment</topic><topic>Transaminases - genetics</topic><topic>Transaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schlösser, Thomas</creatorcontrib><creatorcontrib>Gätgens, Cornelia</creatorcontrib><creatorcontrib>Weber, Ulrike</creatorcontrib><creatorcontrib>Stahmann, K.‐Peter</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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><jtitle>Yeast (Chichester, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schlösser, Thomas</au><au>Gätgens, Cornelia</au><au>Weber, Ulrike</au><au>Stahmann, K.‐Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alanine : glyoxylate aminotransferase of Saccharomyces cerevisiae–encoding gene AGX1 and metabolic significance</atitle><jtitle>Yeast (Chichester, England)</jtitle><addtitle>Yeast</addtitle><date>2004-01-15</date><risdate>2004</risdate><volume>21</volume><issue>1</issue><spage>63</spage><epage>73</epage><pages>63-73</pages><issn>0749-503X</issn><eissn>1097-0061</eissn><abstract>Alanine : glyoxylate aminotransferase is one of three different enzymes used for glycine synthesis in Saccharomyces cerevisiae. The open reading frame YFL030w (named AGX1 in the following), encoding this enzyme, was identified by comparing enzyme specific activities in knockout strains. While 100% activity was detectable in the parental strain, 2% was found in a YFL030w::kanMX4 strain. The ORF found at that locus was suspected to encode alanine : glyoxylate aminotransferase because its predicted amino acid sequence showed 23% identity to the human homologue. Since the YFL030w::kanMX4 strain showed no glycine auxtrophic phenotype, AGX1 was replaced by KanMX4 in a Δ GLY1Δ SHM1Δ SHM2 background. These background mutations, which cause inactivation of threonine aldolase, mitochondrial and cytosolic serine hydroxymethyltransferase, respectively, lead to a conditional glycine auxotrophy. This means that growth is not possible on glucose but on ethanol as the sole carbon source. Additional disruption of AGX1 revealed a complete glycine auxotrophy. Complementation was observed by transformation with a plasmid‐encoded AGX1. Copyright © 2003 John Wiley & Sons, Ltd.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>14745783</pmid><doi>10.1002/yea.1058</doi><tpages>11</tpages></addata></record> |
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| subjects | Alanine - metabolism alanine : glyoxylate aminotransferase amino acid metabolism Amino Acid Sequence Animals Base Sequence DNA, Fungal - chemistry DNA, Fungal - genetics fungi Glycine - biosynthesis Glyoxylates - metabolism Humans Models, Chemical Molecular Sequence Data Mutagenesis, Insertional Orotic Acid - analogs & derivatives Orotic Acid - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Selection, Genetic Sequence Alignment Transaminases - genetics Transaminases - metabolism |
| title | Alanine : glyoxylate aminotransferase of Saccharomyces cerevisiae–encoding gene AGX1 and metabolic significance |
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