Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 80:202-205 (1986)
© 1986 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vick, B. A.
Right arrow Articles by Zimmerman, D. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vick, B. A.
Right arrow Articles by Zimmerman, D. C.
Agricola
Right arrow Articles by Vick, B. A.
Right arrow Articles by Zimmerman, D. C.
Articles

Characterization of 12-Oxo-Phytodienoic Acid Reductase in Corn

The Jasmonic Acid Pathway

Brady A. Vick and Don C. Zimmerman

United States Department of Agriculture, Agricultural Research Service, State University Station, Fargo, North Dakota 58105, Metabolism and Radiation Research Laboratory, State University Station, Fargo, North Dakota 58105

12-Oxo-phytodienoic acid reductase, an enzyme of the biosynthetic pathway that converts linolenic acid to jasmonic acid, has been characterized from the kernel and seedlings of corn (Zea mays L.). The molecular weight of the enzyme, estimated by gel filtration, was 54,000. Optimum enzyme activity was observed over a broad pH range, from pH 6.8 to 9.0. The enzyme had a Km of 190 micromolar for its substrate, 12-oxo-phytodienoic acid. The preferred reductant was NADPH, for which the enzyme exhibited a Km of 13 micromolar, compared with 4.2 millimolar for NADH. Reductase activity was low in the corn kernel but increased five-fold by the fifth day after germination and then gradually declined.





This article has been cited by other articles:


Home page
Plant Cell PhysiolHome page
Y. Ishiga, A. Funato, T. Tachiki, K. Toyoda, T. Shiraishi, T. Yamada, and Y. Ichinose
Expression of the 12-Oxophytodienoic Acid 10,11-Reductase Gene in the Compatible Interaction between Pea and Fungal Pathogen
Plant Cell Physiol., October 15, 2002; 43(10): 1210 - 1220.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
F. Schaller, P. Hennig, and E. W. Weiler
12-Oxophytodienoate-10,11-Reductase: Occurrence of Two Isoenzymes of Different Specificity against Stereoisomers of 12-Oxophytodienoic Acid
Plant Physiology, December 1, 1998; 118(4): 1345 - 1351.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
H. Weber, B. A. Vick, and E. E. Farmer
Dinor-oxo-phytodienoic acid: A new hexadecanoid signal in the jasmonate family
PNAS, September 16, 1997; 94(19): 10473 - 10478.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. A. Stelmach, A. Muller, P. Hennig, S. Gebhardt, M. Schubert-Zsilavecz, and E. W. Weiler
A Novel Class of Oxylipins, sn1-O-(12-Oxophytodienoyl)-sn2-O-(hexadecatrienoyl)-monogalactosyl Diglyceride, from Arabidopsis thaliana
J. Biol. Chem., April 13, 2001; 276(16): 12832 - 12838.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
A. Stintzi and J. Browse
The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis
PNAS, September 12, 2000; 97(19): 10625 - 10630.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1986 by the American Society of Plant Biologists