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d-Fucose Metabolism in a Pseudomonad

II. OXIDATION OF d-FUCOSE TO d-FUCONO--LACTONE BY AN l-ARABINO-ALDOSE DEHYDROGENASE AND HYDROLYSIS OF THE LACTONE BY A LACTONASE

From the ¹ From the Department of Biochemistry, Michigan State University, East Lansing, Michigan 48823

A soluble aldose dehydrogenase has been purified 284-fold from a pseudomonad capable of using d-fucose as a sole carbon source. Only sugars that possessed the l-arabino configuration at C-2 through C-4, namely d-fucose, d-galactose, 6-iodo-6-deoxy-d-galactose, l-arabinose, and certain 2- and 3-deoxy derivatives (abequose and 2-deoxy-d-galactose), served as substrates. Forty-nine other carbohydrates and related compounds tested neither served as substrates nor inhibited the enzyme. The apparent K_m values for d-fucose, d-galactose, and l-arabinose were 0.50, 0.17, and 0.14 mm, respectively, at pH 8.1, and were 4- to 13-fold higher at the apparent pH optimum of 9.4. Both NAD⁺ and NADP⁺ served as coenzymes. The enzyme was insensitive to thiols and thiol group reagents, and was not activated by divalent cations. The product of d-fucose oxidation was identified as d-fucono--lactone. The enzyme is induced by growth of the organism on either d-fucose, d-galactose, or l-arabinose.

A lactonase which catalyzes the hydrolysis of d-fucono--lactone to d-fuconate was also demonstrated in extracts.

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