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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5968
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pubmed:dateCreated |
2010-2-19
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pubmed:abstractText |
Lysine acetylation regulates many eukaryotic cellular processes, but its function in prokaryotes is largely unknown. We demonstrated that central metabolism enzymes in Salmonella were acetylated extensively and differentially in response to different carbon sources, concomitantly with changes in cell growth and metabolic flux. The relative activities of key enzymes controlling the direction of glycolysis versus gluconeogenesis and the branching between citrate cycle and glyoxylate bypass were all regulated by acetylation. This modulation is mainly controlled by a pair of lysine acetyltransferase and deacetylase, whose expressions are coordinated with growth status. Reversible acetylation of metabolic enzymes ensure that cells respond environmental changes via promptly sensing cellular energy status and flexibly altering reaction rates or directions. It represents a metabolic regulatory mechanism conserved from bacteria to mammals.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Citric Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glyceraldehyde-3-Phosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Group III Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Isocitrate Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-9203
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pubmed:author |
pubmed-author:ChenYangY,
pubmed-author:GuanKun-LiangKL,
pubmed-author:LiHongH,
pubmed-author:NingZhi-BinZB,
pubmed-author:OrrV BVB,
pubmed-author:RodT OTO,
pubmed-author:WangQijunQ,
pubmed-author:XieLuL,
pubmed-author:XiongHuiH,
pubmed-author:XiongYueY,
pubmed-author:YaoYufengY,
pubmed-author:ZengRongR,
pubmed-author:ZhangYakunY,
pubmed-author:ZhaoGuo-PingGP,
pubmed-author:ZhaoShiminS,
pubmed-author:ZhaoWeiW
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pubmed:issnType |
Electronic
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pubmed:day |
19
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pubmed:volume |
327
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1004-7
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pubmed:dateRevised |
2010-5-25
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pubmed:meshHeading |
pubmed-meshheading:20167787-Acetylation,
pubmed-meshheading:20167787-Acetyltransferases,
pubmed-meshheading:20167787-Amino Acid Sequence,
pubmed-meshheading:20167787-Bacterial Proteins,
pubmed-meshheading:20167787-Citric Acid,
pubmed-meshheading:20167787-Energy Metabolism,
pubmed-meshheading:20167787-Enzymes,
pubmed-meshheading:20167787-Gene Expression Regulation, Bacterial,
pubmed-meshheading:20167787-Gluconeogenesis,
pubmed-meshheading:20167787-Glucose,
pubmed-meshheading:20167787-Glyceraldehyde-3-Phosphate Dehydrogenases,
pubmed-meshheading:20167787-Glycolysis,
pubmed-meshheading:20167787-Group III Histone Deacetylases,
pubmed-meshheading:20167787-Isocitrate Lyase,
pubmed-meshheading:20167787-Lysine,
pubmed-meshheading:20167787-Metabolic Networks and Pathways,
pubmed-meshheading:20167787-Multienzyme Complexes,
pubmed-meshheading:20167787-Mutation,
pubmed-meshheading:20167787-Protein Processing, Post-Translational,
pubmed-meshheading:20167787-Protein-Serine-Threonine Kinases,
pubmed-meshheading:20167787-Recombinant Proteins,
pubmed-meshheading:20167787-Salmonella typhimurium
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pubmed:year |
2010
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pubmed:articleTitle |
Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux.
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pubmed:affiliation |
State Key Laboratory of Genetic Engineering, Department of Microbiology, School of Life Sciences and Institute of Biomedical Sciences, Fudan University, Shanghai 200032, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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