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Plant and Cell Physiology, 2002, Vol. 43, No. 11 1259-1265
© 2002 Oxford University Press

Purification and cDNA Cloning of UDP-D-Glucuronate Carboxy-lyase (UDP-D-xylose Synthase) from Pea Seedlings

Masaru Kobayashi, Hironobu Nakagawa, Izumi Suda, Isao Miyagawa and Toru Matoh1

Laboratory of Plant Nutrition, Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502 Japan

Uridine diphospho-D-glucuronate carboxy-lyase (UDP-D-xylose synthase; EC 4.1.1.35), which catalyzes the conversion of UDP-D-glucuronate to UDP-D-xylose, was purified to apparent homogenity from pea (Pisum sativum L.) seedlings. The pH optimum for enzyme activity was around 5–6, and the activity was not affected by exogeneously supplied NAD+ and NADH. The purified enzyme had a molecular weight of 250 kDa and consisted of 42 kDa polypeptides. Based on the amino acid sequence, a probe (400 bp) was prepared with degenerate primers by a reverse transcriptase-PCR. Using this probe, a clone encoding 346 amino acid residues was screened from a pea cDNA library. The recombinant protein expressed in Escherichia coli catalyzed conversion of UDP-D-glucuronate to UDP-D-xylose, confirming that the isolated clone encoded UDP-D-glucuronate carboxy-lyase.

1 Corresponding author: E-mail, matoh@kais.kyoto-u.ac.jp; Fax, +81-75-753-6128.


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