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. Author manuscript; available in PMC: 2012 Apr 16.
Published in final edited form as: J Mol Biol. 2011 Aug 1;412(3):495–504. doi: 10.1016/j.jmb.2011.07.059

Figure 4.

Figure 4

Mutation of residues predicted to be important in recognition and catalysis of the second step of the transformation mediated by AcsD. The specific activity is shown as fluorescence units (FU) on the Y-axis. The data for the K563A mutant overestimate the specific activity, because the protein was not fully purified due to low levels of expression. The R501K mutant shows a reversal in specificity. It is more active with ethylene diamine than the wild type enzyme and less active with the cognate substrate L-serine.