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Originally published In Press as doi:10.1074/jbc.M201774200 on May 21, 2002

J. Biol. Chem., Vol. 277, Issue 30, 26858-26864, July 26, 2002
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Enzymatic Hydrolysis of Pyridoxine-5'-beta -D-glucoside Is Catalyzed by Intestinal Lactase-Phlorizin Hydrolase*

Amy D. MackeyDagger , George N. Henderson§, and Jesse F. Gregory IIIDagger

From the Dagger  Food Science and Human Nutrition Department, Institute of Food and Agricultural Sciences, University of Florida, Gainesville, Florida 32611 and the § Division of Endocrinology and Metabolism, Department of Medicine, College of Medicine, University of Florida, Gainesville, Florida 32610

An obligatory step in the mammalian nutritional utilization of pyridoxine-5'-beta -D-glucoside (PNG) is the intestinal hydrolysis of its beta -glucosidic bond that releases pyridoxine (PN). This laboratory previously reported the purification and partial characterization of a novel cytosolic enzyme, designated PNG hydrolase, which hydrolyzed PNG. An investigation of the subcellular distribution of intestinal PNG hydrolysis found substantial hydrolytic activity in the total membrane fraction, of which 40-50% was localized to brush border membrane. To investigate the possible role of a brush border beta -glucosidase in the hydrolysis of PNG, lactase phlorizin hydrolase (LPH) was purified from rat small intestinal mucosa. LPH hydrolyzed PNG with a Km of 1.0 ± 0.1 mM, a Vmax of 0.11 ± 0.01 µmol/min·mg protein, and a kcat of 1.0 s-1. LPH-catalyzed PNG hydrolysis was inhibited by glucose, lactose, and cellobiose but not by PN. Specific blockage of the phlorizin hydrolase site of LPH using 2',4'-dintrophenyl-2-fluoro-2-deoxy-beta -D-glucopyranoside did not reduce PNG hydrolysis. Evidence of transferase activity was also obtained. Reaction mixtures containing LPH, PNG, and lactose yielded the formation of another PN derivative that was identified as a pyridoxine disaccharide. These results indicate that LPH may play an important role in the bioavailability of PNG, but further characterization is needed to assess its physiological function.

*  This work was supported by National Institutes of Health Grants DK 37481, T32 DK07667, and RR-00082 and is Florida Agricultural Experiment Station Journal Series No. R-08682.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Food Science and Human Nutrition Dept., P.O. Box 110370, University of Florida, Gainesville, FL 32611-0370. Tel.: 352-392-1991 (ext. 225); Fax: 352-392-4515; E-mail: jfgy@ufl.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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