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Metabolism and Enzymology

Partial Purification and Properties of an Inducible Uridine 5'-Diphosphate-Glucose-Salicylic Acid Glucosyltransferase from Oat Roots ¹

Department of Agronomy, University of Wisconsin, Madison, Wisconsin 53706

A salicylic acid (SA)-inducible uridine 5'-diphosphate (UDP)-glucose:SA 3-O-glucosyltransferase was extracted from oat (Avena sativa L. cv Dal) roots. Reverse phase high-performance liquid chromatography or anion exchange chromatography was used to separate SA from the product, -O-D-glucosylsalicylic acid. The soluble enzyme was purified 176-fold with 5% recovery using a combination of pH fractionation, anion exchange, gel filtration, and chromatofocusing chromatography. The partially purified protein had a native molecular weight of about 50,000, an apparent isoelectric point at pH 5.0, and maximum activity at pH 5.5. The enzyme had a K_m of 0.28 mM for UDP-glucose and was highly specific for this sugar donor. More than 20 hydroxybenzoic and hydroxycinnamic acid derivatives were assayed as potential glucose acceptors. UDP-glucose:SA 3-O-glucosyltransferase activity was highly specific toward SA (K_m = 0.16 mM). The enzyme was inhibited by UDP and uridine 5'-triphosphate but not by up to 7.5 mM uridine 5'-monophosphate.

³ Present address: Institut für Landwirtschaftliche Botanik, Meckenheimer Allee 176, D-5300 Bonn, Federal Republic of Germany.

⁴ Present address: American Malting Barley Association, Inc., 735 North Water Street, Milwaukee, WI 53202.

¹ Support to N.E.B. by U.S. Department of Agriculture CRGO grant No. 85-CRCR-1-1572, University of Wisconsin-Madison Graduate School project No. 900317, and the College of Agricultural and Life Sciences, University of Wisconsin-Madison.

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