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Uridine 5'-Diphosphate-Glucose Dehydrogenase from Soybean Nodules

Douglas C. Stewart1 and Les Copeland*

Department of Agricultural Chemistry and Soil Science, University of Sydney, Sydney, New South Wales, Australia 2006

A highly purified preparation of uridine 5'-diphosphate (UDP)-glucose (Glc) dehydrogenase (DH; EC 1.1.1.22) has been characterized from soybean (Glycine max L.) nodules. The enzyme had native and subunit molecular masses of approximately 272 and 50 kD, respectively. UDP-Glc DH displayed typical hyperbolic substrate kinetics and had Km values for UDP-Glc and NAD+ of 0.05 and 0.12 mm, respectively. Thymidine 5'-diphosphate-Glc and UDP-galactose could replace UDP-Glc as the sugar nucleotide substrate to some extent, but the enzyme had no activity with NADP+. Soybean nodule UDP-Glc DH was labile in the absence of NAD+ and was inhibited by a heat-stable, low-molecular-mass solute in crude extracts of soybean nodules. UDP-Glc DH was also isolated from developing soybean seeds and shoots of 5-d-old wheat and canola seedlings and was shown to have similar affinities for UDP-Glc and NAD+ as those of the soybean nodule enzyme. UDP-Glc DH from all of these sources was most active in young, rapidly growing tissues.

1   Present address: Department of Plant Science, The Waite Agricultural Research Institute, University of Adelaide, Glen Osmond, SA, Australia 5064.
*   Corresponding author; e-mail copeland{at}spiro.biz.usyd.edu.au; fax 61-2-9351-5108.

Plant Physiol. (1998) 116: 349-355
Copyright Clearance Center:   0032-0889/98/116/0349/07
© 1998 American Society of Plant Physiologists




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