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


     


Plant Physiology 89:1150-1157 (1989)
© 1989 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 Guy, R. D.
Right arrow Articles by Turpin, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Guy, R. D.
Right arrow Articles by Turpin, D. H.
Agricola
Right arrow Articles by Guy, R. D.
Right arrow Articles by Turpin, D. H.
Metabolism and Enzymology

Significance of Phosphoenolpyruvate Carboxylase during Ammonium Assimilation

Carbon Isotope Discrimination in Photosynthesis and Respiration by the N-Limited Green Alga Selenastrum minutum1

Robert D. Guy, Greg C. Vanlerberghe and David H. Turpin

Department of Biology, Queen's University, Kingston, Ontario, Canada, K7L 3N6

The effect of N-assimilation on the partitioning of carbon fixation between phosphoenolpyruvate carboxylase (PEPcase) and ribulose bisphosphate carboxylase/oxygenase (Rubisco) was determined by measuring stable carbon isotope discrimination during photosynthesis by an N-limited green alga, Selenastrum minutum (Naeg.) Collins. This was facilitated by a two process model accounting for simultaneous CO2 fixation and respiratory CO2 release. Discrimination by control cells was consistent with the majority of carbon being fixed by Rubisco. During nitrogen assimilation however, discrimination was greatly reduced indicating an enhanced flux through PEPcase which accounted for upward of 70% of total carbon fixation. This shift toward anaplerotic metabolism supports a large increase in tricarboxylic acid cycle activity primarily between oxaloacetate and {alpha}-ketoglutarate thereby facilitating the provision of carbon skeletons for amino acid synthesis. This provides an example of a unique set of conditions under which anaplerotic carbon fixation by PEPcase exceeds photosynthetic carbon fixation by Rubisco in a C3 organism.


1 Supported by the Natural Sciences and Engineering Research Council of Canada.




This article has been cited by other articles:


Home page
J Exp BotHome page
G. Tcherkez and M. Hodges
How stable isotopes may help to elucidate primary nitrogen metabolism and its interaction with (photo)respiration in C3 leaves
J. Exp. Bot., May 1, 2008; 59(7): 1685 - 1693.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
P. J. McGinn and F. M.M. Morel
Expression and Inhibition of the Carboxylating and Decarboxylating Enzymes in the Photosynthetic C4 Pathway of Marine Diatoms
Plant Physiology, January 1, 2008; 146(1): 300 - 309.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
E.H. Murchie, S. Ferrario-Mery, M-H. Valadier, and C.H. Foyer
Short-term nitrogen-induced modulation of phosphoenolpyruvate carboxylase in tobacco and maize leaves
J. Exp. Bot., August 1, 2000; 51(349): 1349 - 1356.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
V. L. Knowles, C. S. Smith, C. R. Smith, and W. C. Plaxton
Structural and Regulatory Properties of Pyruvate Kinase from the Cyanobacterium Synechococcus PCC 6301
J. Biol. Chem., June 8, 2001; 276(24): 20966 - 20972.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1989 by the American Society of Plant Biologists