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J. Biochem, 1976, Vol. 79, No. 6 1263-1272
© 1976 Japanese Biochemical Society

research-article

Purification and Characterization of Methioninase from Pseudomonas putida

Susumu ITO, Taro NAKAMURA and Yoshitomo EGUCHI

Department of Microbial Engineering and Technology, Faculty of Agriculture, Hokkaido University Kita-ku, Sapporo, Hokkaido 060

Methioninase of Pseudomonas putida was purified to homogeneity, as judged by poly aery lamide gel electrophoresis, with a specific activity 270-fold higher than that of the crude extract.

1. The purified enzyme had an S20, w of 8.37, a molecular weight of 160, 000, and an isoelectric point of 5.6.

2. A break in the Arrhenius plot was observed at 40° and the activation energies below and above this temperature were 15.5 and 2.97 kcal per mole, respectively.

3. In addition to L-methionine, various S-substituted derivatives of homocysteine and cysteine could serve as substrates. D-Methionine, 2-oxo-4-methylthiobutanoate, and related non sulfur-containing amino acids were inert. Equimolar formation of {alpha}-ketobutyrate and CH3SH was observed with methionine as a substrate.

4. In addition to the protein peak at 278 nm, two absorption maxima were observed at 345 and 430 nm at pH 7.5. Hydroxylamine removed the enzyme-bound pyridoxal phosphate, resulting in almost complete resolution with the concomitant disappearance of both peaks. Reconstruction of the treated enzyme could be achieved by addition of the cofactor; the Km value was calculated to be 0.37 µM.

5. The reported purified enzyme should be designated as L-methionine methanethiol-lyase (deaminating).


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