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

共 31 条

[1]

ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999

[2] BIOSYNTHESIS OF URIDINE DIPHOSPHATE D-XYLOSE .I. URIDINE DIPHOSPHATE GLUCURONATE CARBOXY-LYASE OF WHEAT GERM [J].

ANKEL, H ;

FEINGOLD, DS .

BIOCHEMISTRY, 1965, 4 (11) :2468-&

[3] EXPANSION OF THE MAMMALIAN 3-BETA-HYDROXYSTEROID DEHYDROGENASE PLANT DIHYDROFLAVONOL REDUCTASE SUPERFAMILY TO INCLUDE A BACTERIAL CHOLESTEROL DEHYDROGENASE, A BACTERIAL UDP-GALACTOSE-4-EPIMERASE, AND OPEN READING FRAMES IN VACCINIA VIRUS AND FISH LYMPHOCYSTIS DISEASE VIRUS [J].

BAKER, ME ;

BLASCO, R .

FEBS LETTERS, 1992, 301 (01) :89-93

[4] Functional cloning and characterization of a UDP-glucuronic acid decarboxylase:: The pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis [J].

Bar-Peled, M ;

Griffith, CL ;

Doering, TL .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (21) :12003-12008

[5] PURIFICATION AND PROPERTIES OF AN ENZYME FROM CELL SUSPENSION CULTURES OF PARSLEY CATALYZING SYNTHESIS OF UDP-APIOSE AND UDP-D-XYLOSE FROM UDP-D-GLUCURONIC ACID [J].

BARON, D ;

WELLMANN, E ;

GRISEBACH, H .

BIOCHIMICA ET BIOPHYSICA ACTA, 1972, 258 (01) :310-+

[6] Protein motifs .9. The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins [J].

Bellamacina, CR .

FASEB JOURNAL, 1996, 10 (11) :1257-1269

[7] A bifunctional epimerase-reductase acts downstream of the MUR1 gene product and completes the de novo synthesis of GDP-L-fucose in Arabidopsis [J].

Bonin, CP ;

Reiter, WD .

PLANT JOURNAL, 2000, 21 (05) :445-454

[8] The MUR1 gene of Arabidopsis thaliana encodes an isoform of GDP-D-mannose-4,6-dehydratase, catalyzing the first step in the de novo synthesis of GDP-L-fucose [J].

Bonin, CP ;

Potter, I ;

Vanzin, GF ;

Reiter, WD .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (05) :2085-2090

[9] The mur4 mutant of arabidopsis is partially defective in the de novo synthesis of uridine diphospho L-arabinose [J].

Burget, EG ;

Reiter, WD .

PLANT PHYSIOLOGY, 1999, 121 (02) :383-389

[10] Functional expression of uridine 5'-diphospho-glucose 4-epimerase (EC 5.1.3.2) from Arabidopsis thaliana in Saccharomyces cerevisiae and Escherichia coli [J].

Dormann, P ;

Benning, C .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1996, 327 (01) :27-34

← 1 2 3 4 →