Partial purification and characterization of UDPG:t-cinnamate glucosyltransferase in the root of sweet potato, Ipomoea batatas Lam.

Abstract:

:Previously, we isolated t-cinnamoyl-D-glucose as a possible intermediate in chlorogenic acid biosynthesis from sweet potato root. The enzyme which catalyzes the formation of t-cinnamoyl-D-glucose has been purified 539-fold from sweet potato root (Ipomoea batatas Lam.) and characterized. It required UDP-glucose as a glucosyl donor. Its molecular weight was estimated to be 45,000 by gel filtration chromatography through Sephadex G-100. Its Km values were 0.2 mM for t-cinnamic acid and 0.1 mM for UDP-glucose. It also showed activity toward various aromatic carboxylic acids other than t-cinnamic acid with the following relative activities at the concentration of 1.8 mM: t-cinnamic acid, 100; p-coumaric acid, 57; o-coumaric acid, 52; caffeic acid, 15; benzoic acid, 71; ferulic acid, 27; 4-hydroxyl-3-methoxy-benzoic acid, 35. When p-coumaric acid was used as a substrate, the enzyme introduced the glucosyl group exclusively to a carboxyl group, not to a hydroxyl group on a benzene ring. It was inhibited by p-chloromercuribenzoate and HgCl2. Its activity in the extract from sliced root decreased during the first 28 h after slicing, then increased to the original level by 75 h. The apparent decrease seemed to be caused by the appearance of an inhibitory factor of high molecular weight in the tissue extract.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Shimizu T,Kojima M

doi

10.1093/oxfordjournals.jbchem.a134586

subject

Has Abstract

pub_date

1984-01-01 00:00:00

pages

205-12

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

95

pub_type

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