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12-Oxophytodienoate-10,11-Reductase: Occurrence of Two Isoenzymes
of Different Specificity against Stereoisomers of 12-Oxophytodienoic
Acid1
Florian Schaller,
Peter Hennig, and
Elmar W. Weiler*
Lehrstuhl für Pflanzenphysiologie, Ruhr-Universität,
D-44780 Bochum, Germany
The reduction of 12-oxophytodienoic
acid (OPDA) to
3-oxo-2(2 [Z]-pentenyl)-cyclopentane-1-octanoic acid
is catalyzed by 12-oxophytodienoate-10,11-reductase (OPR). Analysis of
the isomer preference of OPR has indicated that the activity is
composed of two isoenzymes exhibiting different stereoselectivities.
The two isoforms of OPR have been separated, using protein extracts of
Rock Harlequin (Corydalis sempervirens) as the starting material. OPRI, the enzyme reported
earlier from the same species and corresponding to the cloned OPR from
Arabidopsis, utilized
9R,13R-OPDA >>
9S,13R-OPDA but not the
13S-configured isomers, whereas the new activity, OPRII,
effectively reduced all four OPDA isomers, including the natural
9S,13S-OPDA
(cis-[+]-OPDA). OPRII activity is characterized in
detail. The enzyme's enzymatic, biochemical, and immunological
properties prove that it is a close relative of OPRI. The roles of OPRI
and OPRII in octadecanoid biology are discussed.
1
This work was supported by the Deutsche
Forschungsgemeinschaft, Bonn, and Fonds der Chemischen Industrie,
Frankfurt (literature provision).
*
Corresponding author; e-mail
elmar.weiler{at}ruhr-uni-bochum.de; fax 49-234-709-4187.
Plant Physiol. (1998) 118: 1345-1351
Copyright Clearance Center: 0032-0889/98/118//07
© 1998 American Society of Plant Physiologists
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