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Xiaolong Chen, Nonlawat Boonyalai, Catherine Lau, Salinthip Thipayang, Yuhong Xu, Michael Wright and Andrew D. Miller Multiple catalytic activities of Escherichia coli lysyl-tRNA synthetase (LysU) are dissected by site-directed mutagenesis FEBS Journal 280

Article first published online: 29 NOV 2012 | DOI: 10.1111/febs.12053

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Escherichia coli lysyl-tRNA synthetase (LysU) converts ATP to diadenosine tri- and tetraphosphates (Ap3A/Ap4A) in the presence of L-lysine, Mg2+ and Zn2+. We report that residue E264 is crucial for Zn2+ promotion of Ap4A/Ap3A synthesis in wild-type enzyme, with mutants E264K/Q/N unexpectedly catalysing the production of glycerol-3-phosphate from ATP and glycerol, but showing little formation of Ap4A/Ap3A.

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