A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity
Abstract A novel aldo-keto reductase (AKR) from Escherichia coli has been cloned, expressed and purified. This protein, YghZ, is distantly related (
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| Veröffentlicht in: | FEMS microbiology letters 2003-01, Vol.218 (1), p.93-99 |
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| container_title | FEMS microbiology letters |
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| creator | Grant, Anne W. Steel, Gavin Waugh, Hugh Ellis, Elizabeth M. |
| description | Abstract
A novel aldo-keto reductase (AKR) from Escherichia coli has been cloned, expressed and purified. This protein, YghZ, is distantly related ( |
| doi_str_mv | 10.1111/j.1574-6968.2003.tb11503.x |
| format | Article |
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A novel aldo-keto reductase (AKR) from Escherichia coli has been cloned, expressed and purified. This protein, YghZ, is distantly related (<40%) to mammalian aflatoxin dialdehyde reductases of the aldo-keto reductase AKR7 family and to potassium channel β-subunits in the AKR6 family. The enzyme has been placed in a new AKR family (AKR14), with the designation AKR14A1. Sequences encoding putative homologues of this enzyme exist in many other bacteria. The enzyme can reduce several aldehyde and diketone substrates, including the toxic metabolite methylglyoxal. The Km for the model substrate 4-nitrobenzaldehyde is 1.06 mM and for the endogenous dicarbonyl methylglyoxal it is 3.4 mM. Overexpression of the recombinant enzyme in E. coli leads to increased resistance to methylglyoxal. It is possible that this enzyme plays a role in the metabolism of methylglyoxal, and can influence its levels in vivo.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2003.tb11503.x</identifier><identifier>PMID: 12583903</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Aflatoxins ; Alcohol Oxidoreductases - genetics ; Alcohol Oxidoreductases - metabolism ; Aldehyde Reductase ; Aldehydes ; Aldo-keto reductase ; Aldo-Keto Reductases ; Bacteria ; Bacteriology ; Biocompatibility ; Biological and medical sciences ; Cloning, Molecular ; E coli ; Enzymes ; Escherichia coli ; Escherichia coli - drug effects ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Homology ; In Vitro Techniques ; Metabolism. Enzymes ; Metabolites ; Methylglyoxal ; Microbiology ; Molecular Sequence Data ; Open Reading Frames - genetics ; Pyruvaldehyde ; Pyruvaldehyde - toxicity ; Reductases ; Sequence Homology, Amino Acid ; Substrates ; Toxic aldehyde ; Toxicity</subject><ispartof>FEMS microbiology letters, 2003-01, Vol.218 (1), p.93-99</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2003 INIST-CNRS</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4363-a846dc9e1ece5ffbc814c83bd43d64a32caae34c74c81e22e8ff6ed7c3d279573</citedby><cites>FETCH-LOGICAL-c4363-a846dc9e1ece5ffbc814c83bd43d64a32caae34c74c81e22e8ff6ed7c3d279573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2003.tb11503.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2003.tb11503.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14487132$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12583903$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grant, Anne W.</creatorcontrib><creatorcontrib>Steel, Gavin</creatorcontrib><creatorcontrib>Waugh, Hugh</creatorcontrib><creatorcontrib>Ellis, Elizabeth M.</creatorcontrib><title>A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
A novel aldo-keto reductase (AKR) from Escherichia coli has been cloned, expressed and purified. This protein, YghZ, is distantly related (<40%) to mammalian aflatoxin dialdehyde reductases of the aldo-keto reductase AKR7 family and to potassium channel β-subunits in the AKR6 family. The enzyme has been placed in a new AKR family (AKR14), with the designation AKR14A1. Sequences encoding putative homologues of this enzyme exist in many other bacteria. The enzyme can reduce several aldehyde and diketone substrates, including the toxic metabolite methylglyoxal. The Km for the model substrate 4-nitrobenzaldehyde is 1.06 mM and for the endogenous dicarbonyl methylglyoxal it is 3.4 mM. Overexpression of the recombinant enzyme in E. coli leads to increased resistance to methylglyoxal. It is possible that this enzyme plays a role in the metabolism of methylglyoxal, and can influence its levels in vivo.</description><subject>Aflatoxins</subject><subject>Alcohol Oxidoreductases - genetics</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Aldehyde Reductase</subject><subject>Aldehydes</subject><subject>Aldo-keto reductase</subject><subject>Aldo-Keto Reductases</subject><subject>Bacteria</subject><subject>Bacteriology</subject><subject>Biocompatibility</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Homology</subject><subject>In Vitro Techniques</subject><subject>Metabolism. Enzymes</subject><subject>Metabolites</subject><subject>Methylglyoxal</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames - genetics</subject><subject>Pyruvaldehyde</subject><subject>Pyruvaldehyde - toxicity</subject><subject>Reductases</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrates</subject><subject>Toxic aldehyde</subject><subject>Toxicity</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkUFv1DAQhS1ERZfCX0ARCG5Z7NiJHaQeqqqFSltxgbPlnUxYL0682Als_j2ONqISgkN9GWn8Pc_4PUJeM7pm6bzfr1kpRV7VlVoXlPL1sGWsTPX4hKz-XD0lK8qlyhmt5Tl5HuOeUioKWj0j56woFa8pXxG4ynr_E11mXOPz7zj4LGAzwmAiZm3wXXYTYYfBws6aDLyzGZg-sz0EnJGA0cbB9IBZknY47Cb3zU3-aFxqHC3YYXpBzlrjIr5c6gX5envz5fpTvvn88e76apOD4BXPjRJVAzUyBCzbdguKCVB82wjeVMLwAoxBLkCmLsOiQNW2FTYSeFPIupT8grw7vXsI_seIcdCdjYDOmR79GDVTlSw5Uwl88xe492Po02664FSyiglRJurDiYLgYwzY6kOwnQmTZlTPQei9nt3Ws9t6DkIvQehjEr9aRozbDpsH6eJ8At4ugIlgXBuShzY-cEIoyXiRuMsT98s6nB6xgr6939TznPKk9-PhP-r8Xx_4DcGJtls</recordid><startdate>20030121</startdate><enddate>20030121</enddate><creator>Grant, Anne W.</creator><creator>Steel, Gavin</creator><creator>Waugh, Hugh</creator><creator>Ellis, Elizabeth M.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20030121</creationdate><title>A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity</title><author>Grant, Anne W. ; Steel, Gavin ; Waugh, Hugh ; Ellis, Elizabeth M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4363-a846dc9e1ece5ffbc814c83bd43d64a32caae34c74c81e22e8ff6ed7c3d279573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Aflatoxins</topic><topic>Alcohol Oxidoreductases - genetics</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Aldehyde Reductase</topic><topic>Aldehydes</topic><topic>Aldo-keto reductase</topic><topic>Aldo-Keto Reductases</topic><topic>Bacteria</topic><topic>Bacteriology</topic><topic>Biocompatibility</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Homology</topic><topic>In Vitro Techniques</topic><topic>Metabolism. Enzymes</topic><topic>Metabolites</topic><topic>Methylglyoxal</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Open Reading Frames - genetics</topic><topic>Pyruvaldehyde</topic><topic>Pyruvaldehyde - toxicity</topic><topic>Reductases</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrates</topic><topic>Toxic aldehyde</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grant, Anne W.</creatorcontrib><creatorcontrib>Steel, Gavin</creatorcontrib><creatorcontrib>Waugh, Hugh</creatorcontrib><creatorcontrib>Ellis, Elizabeth M.</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Grant, Anne W.</au><au>Steel, Gavin</au><au>Waugh, Hugh</au><au>Ellis, Elizabeth M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2003-01-21</date><risdate>2003</risdate><volume>218</volume><issue>1</issue><spage>93</spage><epage>99</epage><pages>93-99</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
A novel aldo-keto reductase (AKR) from Escherichia coli has been cloned, expressed and purified. This protein, YghZ, is distantly related (<40%) to mammalian aflatoxin dialdehyde reductases of the aldo-keto reductase AKR7 family and to potassium channel β-subunits in the AKR6 family. The enzyme has been placed in a new AKR family (AKR14), with the designation AKR14A1. Sequences encoding putative homologues of this enzyme exist in many other bacteria. The enzyme can reduce several aldehyde and diketone substrates, including the toxic metabolite methylglyoxal. The Km for the model substrate 4-nitrobenzaldehyde is 1.06 mM and for the endogenous dicarbonyl methylglyoxal it is 3.4 mM. Overexpression of the recombinant enzyme in E. coli leads to increased resistance to methylglyoxal. It is possible that this enzyme plays a role in the metabolism of methylglyoxal, and can influence its levels in vivo.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>12583903</pmid><doi>10.1111/j.1574-6968.2003.tb11503.x</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2003-01, Vol.218 (1), p.93-99 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Aflatoxins Alcohol Oxidoreductases - genetics Alcohol Oxidoreductases - metabolism Aldehyde Reductase Aldehydes Aldo-keto reductase Aldo-Keto Reductases Bacteria Bacteriology Biocompatibility Biological and medical sciences Cloning, Molecular E coli Enzymes Escherichia coli Escherichia coli - drug effects Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Homology In Vitro Techniques Metabolism. Enzymes Metabolites Methylglyoxal Microbiology Molecular Sequence Data Open Reading Frames - genetics Pyruvaldehyde Pyruvaldehyde - toxicity Reductases Sequence Homology, Amino Acid Substrates Toxic aldehyde Toxicity |
| title | A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity |
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