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PubMed for id: 2531003950
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A positive selection approach identifies residues important for folding of Salmonella enterica Pat, an N(ε)-lysine acetyltransferase that regulates central metabolism enzymes.
Res Microbiol. 2012 Jul;163(6-7):427-35. doi: 10.1016/j.resmic.2012.05.008. Epub 2012 Jun 4.
Res Microbiol. 2012.
PMID: 22677774
Free PMC article.
Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism.
Thao S, Escalante-Semerena JC.
Thao S, et al.
mBio. 2011 Oct 18;2(5):e00216-11. doi: 10.1128/mBio.00216-11. Print 2011.
mBio. 2011.
PMID: 22010215
Free PMC article.
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Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux.
Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, Yao J, Li H, Xie L, Zhao W, Yao Y, Ning ZB, Zeng R, Xiong Y, Guan KL, Zhao S, Zhao GP.
Wang Q, et al.
Science. 2010 Feb 19;327(5968):1004-7. doi: 10.1126/science.1179687.
Science. 2010.
PMID: 20167787
Free PMC article.
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Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica.
Starai VJ, Escalante-Semerena JC.
Starai VJ, et al.
J Mol Biol. 2004 Jul 23;340(5):1005-12. doi: 10.1016/j.jmb.2004.05.010.
J Mol Biol. 2004.
PMID: 15236963
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