Partial Purification and Some Properties of Flavonol 7-Sulfotransferase from Flaveria bidentis.

Abstract:

:A novel flavonol-specific sulfotransferase was partially purified from the shoot tips of Flaveria bidentis var. Angustifolia O.K. (Asteraceae) by chromatography on 3'-phosphoadenosine 5'-phosphate-agarose affinity column and chromatofocusing on Mono P. The latter step resulted in the separation of two isoforms, both of which exhibited expressed specificity for position 7 of quercetin 3,3'- and quercetin 3,4'-disulfate. The 7-sulfotransferase isoforms I and II had a pH optimum of 7.5 in phosphate buffer, apparent pl values of 6.5 and 6.3, and an M(r) of 35,000. They had no requirement for divalent cations and were not inhibited by EDTA or SH group reagents. Their K(m) values for both the sulfate donor and flavonol acceptor were of the same order of magnitude (0.20-0.46 micromolar). This enzyme, together with the recently reported flavonol 3-, 3'-, and 4'-sulfotransferases from F. chloraefolia (L Varin, RK Ibrahim [1989] Plant Physiol 90: 977-981) form the complement involved in the biosynthesis of polysulfated flavonols in this genus. A proposed sequential order for the enzymatic sulfation in both species is described.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Varin L,Ibrahim RK

doi

10.1104/pp.95.4.1254

subject

Has Abstract

pub_date

1991-04-01 00:00:00

pages

1254-8

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

95

pub_type

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