Table 2 Activity assessment of the different PAL variants within the ammonia addition and ammonia elimination reactions of meta-substituted cinnamic acids 2e–h and rac-phenylalanines 1e–h, respectively.

From: Towards a general approach for tailoring the hydrophobic binding site of phenylalanine ammonia-lyases

  1. n.d. not determinable, during enzyme kinetics the non-linear range of the Michaelis–Menten curve was not obtained using substrate concentration allowed by the solubility of the tested compounds.
  2. n.a. no activity detected.
  3. “–” no determination/measurement was performed.
  4. #During the ammonia additions the enantiomeric excess of the obtained l-phenylalanine analogues was also monitored, in all cases ee > 99% have been obtained.
  5. *Except in case of the l-1e (ee = 93.6%) produced within the ammonia addition reaction of 2e catalyzed by L133A AtPAL.
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