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Plant and Cell Physiology, 1986, Vol. 27, No. 8 1451-1460
© 1986

Article

Metabolism of p-Hydroxybenzoate via Hydroxyquinol by Trichosporon cutaneum WY2-2: Characterization of the Pathway using Superoxide Dismutase as a Stabilizer of Hydroxyquinol1

Katsunori Suzuki2 and Masao Itoh3

Department of Agricultural Chemistry, Faculty of Agriculture, Nagoya University Nagoya 464, Japan

Trichosporon cutaneum WY2-2 was shown to metabolize p-hydroxybenzoate via protocatechuate and hydroxyquinol. Using superoxide dismutase as a stabilizer of hydroxyquinol, the conversion of protocatechuate to hydroxyquinol and the ring fission process of hydroxyquinol were confirmed. Hydroxyquinol was chemically identified as the product of protocatechuate hydroxylase reaction. Partially purified protocatechuate hydroxylase was highly specific for protocatechuate; its Km values for protocatechuate and NADH were 17.6 and 12.4 µM, respectively. It catalyzed equimolar CO2 formation, NADH oxidation and O2 consumption from protocatechuate. Hydroxyquinol dioxygenase was highly specific for hydroxyquinol, with a Km of 2.9 µM.

1A preliminary account of this work was presented at the 81st Meeting of the Chubu-branch of Agricultural Chemical Society of Japan, Gifu, October, 1980.

2Present address: Biological Institute, Faculty of Science, Nagoya University, Nagoya 464, Japan.

3Present address: Shin Nihon Chemical Co. Ltd... 19-10, Showa-cho, Anjoh, Aichi 446, Japan.

(Received November 15, 1985; Accepted August 27, 1986)
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