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J. Biochem, 1998, Vol. 123, No. 6 1097-1103
© 1998 Japanese Biochemical Society

research-article

Chemical Modification of L-Phenylalanine Oxidase from Pseudomonas sp. P-501 by Phenylglyoxal. Identification of One Essential Arginyl Residue

Etsuko B. Mukouyama1, Takuya Hirose2 and Haruo Suzuki

Department of Biosciences, Faculty of Science, Kitasato University Kitasato, Sagamihara, Kanagawa 228-8555

1To whom correspondence should be addressed. E-mail: mukoyama{at}jet.sci.kitasato-u.ac.jp

L-Phenylalanine oxidase from Pseudomonas sp. P-501 was irreversibly inactivated by the arginine-specific reagents, phenylglyoxal (PGO) and p-hydroxyphenylglyoxal (HPG). The inactivation by PGO and HPG follows pseudo-first-order kinetics with second-order rate constants of 10.6 and 15.1 M–1.min–1, respectively, and a single arginyl residue was modified specifically. The effective protection by substrate L-phenylalanine against the inactivation by these reagents strongly suggests that the arginyl residue is located in the substrate binding site. SDS/PAGE analysis of the enzyme modified with [14C]PGO revealed that the arginyl residue was in the ß subunit of the enzyme. The fragment containing the 14C-labeled arginyl residue was purified from the enzymatic digests of the labeled B subunit by HPLC and sequenced. The modification of Arg-35 in the ß subunit was identified. The sequence around Arg-35 shows homology to the corresponding regions of tryptophan-2-monooxygenases.

2Present address: Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University, Urawa 338-8570.


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