Purification and cDNA cloning of UDP-D-glucuronate carboxy-lyase (UDP-D-xylose synthase) from pea seedlings

被引：27

作者：

Kobayashi, M ^{[1
]}

Nakagawa, H ^{[1
]}

Suda, I ^{[1
]}

Miyagawa, I ^{[1
]}

Matoh, T ^{[1
]}

机构：

[1] Kyoto Univ, Div Appl Life Sci, Grad Sch Agr, Lab Plant Nutr, Kyoto 6068502, Japan

来源：

PLANT AND CELL PHYSIOLOGY | 2002年 / 43卷 / 11期

基金：

日本学术振兴会;

关键词：

Pisum sativum; UDP-D-glucuronate carboxylyase (EC 4.1.1.35) UDP-D-xylose;

D O I：

10.1093/pcp/pcf157

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

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.

引用

页码：1259 / 1265

页数：7

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