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The sequence of a phenylalanine ammonia-lyase (PAL; EC: 4.3.1.24) of the thermophilic and radiotolerant bacterium  Rubrobacter xylanophilus  ( Rx PAL) was identified by screening the genomes of bacteria for members of the phenylalanine ammonia-lyase family. A synthetic gene encoding the  Rx PAL protein was cloned and overexpressed in  Escherichia coli  TOP 10 in a soluble form with an  N -terminal His 6 -tag and the recombinant  Rx PAL protein was purified by Ni-NTA affinity chromatography. The activity assay of  Rx PAL with  l -phenylalanine at various pH values exhibited a local maximum at pH 8.5 and a global maximum at pH 11.5. Circular dichroism (CD) studies showed that  Rx PAL is associated with an extensive α-helical character (far UV CD) and two distinctive near-UV CD peaks. These structural characteristics were well preserved up to pH 11.0. The extremely high pH optimum of  Rx PAL can be rationalized by a three-dimensional homology model indicating possible disulfide bridges, extensive salt-bridge formation and an excess of negative electrostatic potential on the surface. Due to these properties,  Rx PAL may be a candidate as biocatalyst in synthetic biotransformations leading to unnatural  l - or  d -amino acids or as therapeutic enzyme in treatment of phenylketonuria or leukemia.

Expression and Properties of the Highly Alkalophilic Phenylalanine Ammonia-Lyase of Thermophilic Rubrobacter xylanophilus