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Journal of Biochemistry 2004 136(5):617-627; doi:10.1093/jb/mvh169
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© 2004 The Japanese Biochemical Society

MOLECULAR BIOLOGY

Sequencing and Expression of the L-Phenylalanine Oxidase Gene from Pseudomonas sp. P-501. Proteolytic Activation of the Proenzyme

Haruo Suzuki1,2,*, Yuhki Higashi1, Mai Asano1, Masaya Suguro1, Masayuki Kigawa2, Masahiro Maeda2, Satoshi Katayama2, Etsuko B. Mukouyama2 and Koji Uchiyama3

1 Division of Biosciences, Graduate School of Fundamental Life Science, and 3 Laboratory of Embryology, 2 Department of Biosciences, School of Science, Kitasato University, Kitasato 1-15-1, Sagamihara, Kanagawa 228-8555

The nucleotide sequence encoding L-phenylalanine oxidase (deaminating and decarboxylating) (PAO) from Pseudomonas sp. P-501 was determined. The open reading frame is arranged in the order of prosequence, {alpha} subunit, dipeptide and ß subunit from the 5'- to 3'-end. Expression of the gene in Escherichia coli showed that without the prosequence, PAO is produced in small quantity as a soluble form with no visible absorption, but with the prosequence (proPAO), PAO is highly expressed and yellow. The purified proPAO contained one mol of FAD per mol of proPAO polypeptide, but had no catalytic activity. Treatment of proPAO with a mixture of Pronase and trypsin converted the noncatalytic proPAO to the catalytic form, and the Pronase-trypsin–treated proPAO showed kinetic and spectral properties comparable to the native enzyme. These results suggest that in Pseudomonas, PAO is expressed as a proenzyme that is processed by proteolysis to the active form.

* To whom correspondence should be addressed. Tel/Fax: +81-42-778-9401, E-mail: suzuki{at}sci.kitasato-u.ac.jp


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