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Journal of Biochemistry 2006 139(3):551-555; doi:10.1093/jb/mvj049
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© 2006 The Japanese Biochemical Society.

Regular Paper

Kinetic Isotope Effect of the L-Phenylalanine Oxidase from Pseudomonas sp. P-501

Yui Ohta1, Etsuko B. Mukouyama2 and Haruo Suzuki1,2,*

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

* To whom correspondence should be addressed at: Department of Biosciences, School of Science, Kitasato University, Kitasato 1-15-1, Sagamihara, Kanagawa 228-8555. Tel/Fax: +81-42-778-9401, E-mail: suzuki{at}sci.kitasato-u.ac.jp

Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating) mainly catalyzes oxygenation when L-phenylalanine is used as the substrate, but oxidation when L-methionine is used as the substrate. Using [C{alpha}-H]-DL-methionine and [C{alpha}-D]-DL-methionine as substrate, the reductive half reaction of FAD cofactor of enzyme has been studied by stopped-flow spectrophotometry. The rate of reduction of FAD cofactor has a kinetic isotope effect (KIE) of 5.4 and 4.1 in the absence and presence of 30% glycerol, respectively. The KIE is independent of temperature, but the rates of the reductive half reaction are dependent on temperature, indicating that thermally induced motion at the active site drives the H-transfer reaction by H-tunneling.


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