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Journal of Bacteriology, June 2005, p. 4286-4289, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4286-4289.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Biochemical Characterization of a Prokaryotic Phenylalanine Ammonia Lyase

Longkuan Xiang1 and Bradley S. Moore1,2*

College of Pharmacy,1 Department of Chemistry, University of Arizona, Tucson, Arizona 857212

Received 6 January 2005/ Accepted 3 March 2005

The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium "Streptomyces maritimus" is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid L-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for L-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by ~200 amino acid residues.

* Corresponding author. Mailing address: College of Pharmacy, University of Arizona, Tucson, AZ 85721-0207. Phone: (520) 626-6931. Fax: (520) 626-2466. E-mail: moore{at}pharmacy.arizona.edu.

Journal of Bacteriology, June 2005, p. 4286-4289, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4286-4289.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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