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


     


Plant Physiology 82:695-699 (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 Web of Science
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 Web of Science (35)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bauwe, H.
Right arrow Articles by Chollet, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bauwe, H.
Right arrow Articles by Chollet, R.
Agricola
Right arrow Articles by Bauwe, H.
Right arrow Articles by Chollet, R.
Articles

Kinetic Properties of Phosphoenolpyruvate Carboxylase from C3, C4, and C3-C4 Intermediate Species of Flaveria (Asteraceae) 1

Hermann Bauwe and Raymond Chollet

Zentralinstitut für Genetik und Kulturpflanzenforschung der Akademie der Wissenschaften der DDR, DDR-4325 Gatersleben (GDR), Department of Agricultural Biochemistry, East Campus, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0718

Flaveria cronquistii (C3), F. chloraefolia (C3-C4), F. floridana (C3-C4), F. pubescens (C3-C4), F. anomala (C3-C4), F. linearis (C3-C4), F. brownii (C4), F. palmeri (C4), F. trinervia (C4) and F. australasica (C4), comprising 10 out of the 21 known species of the genus Flaveria (Asteraceae), were included in a comparative study of the kinetic and regulatory properties of green leaf phosphoenolpyruvate (PEP) carboxylase. At least three kinetically distinct enzyme-forms were identified on the basis of their affinities for PEP and the degree of allosterism with respect to this substrate. The kinetic properties of PEP carboxylase of most of the species seemingly were modified in vivo depending on the growth conditions of the plants. Km(PEPfree)-values of the enzyme from the five C3-C4 intermediate species ranged from 6 micromolar (F. chloraefolia, low light-grown) to 38 micromolar (F. pubescens, high light-grown). In contrast, the Km for PEP of PEP carboxylase from the C3 species F. cronquistii (13 micromolar) apparently was not influenced by growth conditions. The response of the enzyme from the C3 and C3-C4 species was hyperbolic in all cases. A second isoform with a lower affinity for PEP (88-100 micromolar), but also hyperbolic kinetics was found in the C4 species F. brownii, whereas in the three other C4 species examined a PEP carboxylase with a still lower affinity for PEP (187-221 micromolar) and sigmoidal kinetics was present. These isozyme-related kinetic data were supported by analyses of the elution behavior of the enzyme during anion-exchange chromatography on DEAE-Trisacryl M. The results are discussed with respect to the evolution of C4 photosynthesis in the Flaveria genus.


1 Supported in part by National Science Foundation Grant No. DMB-8415292 and published as Paper No. 8049, Journal Series, Nebraska Agricultural Research Division.




This article has been cited by other articles:


Home page
Plant CellHome page
M. Akyildiz, U. Gowik, S. Engelmann, M. Koczor, M. Streubel, and P. Westhoff
Evolution and Function of a cis-Regulatory Module for Mesophyll-Specific Gene Expression in the C4 Dicot Flaveria trinervia
PLANT CELL, November 1, 2007; 19(11): 3391 - 3402.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Bot.Home page
A. D. McKown, J.-M. Moncalvo, and N. G. Dengler
Phylogeny of Flaveria (Asteraceae) and inference of C4 photosynthesis evolution
Am. J. Botany, November 1, 2005; 92(11): 1911 - 1928.
[Abstract] [Full Text] [PDF]


Home page
ANN BOT (LOND)Home page
P. WESTHOFF and U. GOWIK
Evolution of C4 Phosphoenolpyruvate Carboxylase. Genes and Proteins: a Case Study with the Genus Flaveria
Ann. Bot., January 1, 2004; 93(1): 13 - 23.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
O. E. Blasing, P. Westhoff, and P. Svensson
Evolution of C4 Phosphoenolpyruvate Carboxylase in Flaveria, a Conserved Serine Residue in the Carboxyl-terminal Part of the Enzyme Is a Major Determinant for C4-specific Characteristics
J. Biol. Chem., September 1, 2000; 275(36): 27917 - 27923.
[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