A specific enzyme hydrolyzing 6-O(4-O)-indole-3-ylacetyl-beta-D-glucose in immature kernels of Zea mays.

Abstract:

:The purification of 6-O(4-O)-indole-3-ylacetyl-beta-D-glucose (IAGlc) hydrolase from immature kernels of maize (Zea mays) was undertaken to separate this enzyme from 1-O-IAGlc hydrolase and beta-glucosidase. Partially purified 6-O(4-O)-IAGlc hydrolase was found to be the specific enzyme catalyzing hydrolysis of stable esters of IAA and glucose. Among a range of ester conjugates tested as substrates, only 6-O(4-O)-IAA-glucose and IBA-glucose isomers were effectively hydrolyzed. No activity against p-nitrophenyl-beta-D-glucopyranoside, a synthetic substrate for beta-glucosidase, was detected in the enzyme preparation. The enzyme is probably involved in the regulation of the IAA levels by the target release of free auxin from ester-linked conjugates, its inactive storage forms.

journal_name

J Plant Physiol

authors

Jakubowska A,Kowalczyk S

doi

10.1016/j.jplph.2004.05.015

subject

Has Abstract

pub_date

2005-02-01 00:00:00

pages

207-13

issue

2

eissn

0176-1617

issn

1618-1328

journal_volume

162

pub_type

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