|Related Categories||A - H, Amino Acids, Biochemicals and Reagents, Modified Amino Acids|
Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with γ-thialysine by using a chemical mutagenesis strategy. Timms N, Windle CL, Polyakova A, et al. ChemBioChem. 14(4), 474-81, (2013)
Synthesis of 4-thia-[6-(13)C]lysine from [2- (13)C]glycine: access to site-directed isotopomers of 2-aminoethanol, 2-bromoethylamine and 4-thialysine. Maity AN, Shaikh AC, Srimurugan S, et al. Amino Acids 42(1), 309-15, (2012)
Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code. Jester BC, Levengood JD, Roy H, et al. Proc. Natl. Acad. Sci. U. S. A. 100(24), 14351-6, (2003)
Expression of Viola cyclotides by liquid chromatography-mass spectrometry and tandem mass spectrometry sequencing of intercysteine loops after introduction of charges and cleavage sites by aminoethylation. Göransson U, Broussalis AM, and Claeson P Anal. Biochem. 318(1), 107-17, (2003)
Chemical-modification rescue assessed by mass spectrometry demonstrates that gamma-thia-lysine yields the same activity as lysine in aldolase. Hopkins CE, O'Connor PB, Allen KN, et al. Protein Sci. 11(7), 1591-9, (2002)
Inhibition of lysine 2,3-aminomutase by the alternative substrate 4-thialysine and characterization of the 4-thialysyl radical intermediate. Miller J, Bandarian V, Reed GH, et al. Arch. Biochem. Biophys. 387(2), 281-8, (2001)
Evidence for conformational movement and radical mechanism in the reaction of 4-thia-L-lysine with lysine 5,6-aminomutase. Maity AN, Hsieh CP, Huang MH, et al. J. Phys. Chem. B 113(36), 12161-3, (2009)
Stringent mating-type-regulated auxotrophy increases the accuracy of systematic genetic interaction screens with Saccharomyces cerevisiae mutant arrays. Singh I, Pass R, Togay SO, et al. Genetics 181(1), 289-300, (2009)
A novel member of the GCN5-related N-acetyltransferase superfamily from Caenorhabditis elegans preferentially catalyses the N-acetylation of thialysine [S-(2-aminoethyl)-L-cysteine]. Abo-Dalo B, Ndjonka D, Pinnen F, et al. Biochem. J. 384(Pt 1), 129-37, (2004)
The importance of a critical protonation state and the fate of the catalytic steps in class A beta-lactamases and penicillin-binding proteins. Golemi-Kotra D, Meroueh SO, Kim C, et al. J. Biol. Chem. 279(33), 34665-73, (2004)
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