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


     

This Article
Right arrow Full Text
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 ISI 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 ISI Web of Science (33)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fu, Y.
Right arrow Articles by Preiss, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fu, Y.
Right arrow Articles by Preiss, J.
Agricola
Right arrow Articles by Fu, Y.
Right arrow Articles by Preiss, J.

Mutagenesis of the Glucose-1-Phosphate-Binding Site of Potato Tuber ADP-Glucose Pyrophosphorylase1

Yingbin Fu, Miguel A. Ballicora, and Jack Preiss*

Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824

Lysine (Lys)-195 in the homotetrameric ADP-glucose pyrophosphorylase (ADPGlc PPase) from Escherichia coli was shown previously to be involved in the binding of the substrate glucose-1-phosphate (Glc-1-P). This residue is highly conserved in the ADPGlc PPase family. Site-directed mutagenesis was used to investigate the function of this conserved Lys residue in the large and small subunits of the heterotetrameric potato (Solanum tuberosum) tuber enzyme. The apparent affinity for Glc-1-P of the wild-type enzyme decreased 135- to 550-fold by changing Lys-198 of the small subunit to arginine, alanine, or glutamic acid, suggesting that both the charge and the size of this residue influence Glc-1-P binding. These mutations had little effect on the kinetic constants for the other substrates (ATP and Mg2+ or ADP-Glc and inorganic phosphate), activator (3-phosphoglycerate), inhibitor (inorganic phosphate), or on the thermal stability. Mutagenesis of the corresponding Lys (Lys-213) in the large subunit had no effect on the apparent affinity for Glc-1-P by substitution with arginine, alanine, or glutamic acid. A double mutant, SK198RLK213R, was also obtained that had a 100-fold reduction of the apparent affinity for Glc-1-P. The data indicate that Lys-198 in the small subunit is directly involved in the binding of Glc-1-P, whereas they appear to exclude a direct role of Lys-213 in the large subunit in the interaction with this substrate.

1   This work was supported in part by Department of Energy grant no. DE-FG02-93ER20121.
*   Corresponding author; e-mail preiss{at}pilot.msu.edu; fax 1-517-353-9334.

Plant Physiol. (1998) 117: 989-996
Copyright Clearance Center:   0032-0889/98/117/0989/08
© 1998 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
T. Ventriglia, M. L. Kuhn, M. T. Ruiz, M. Ribeiro-Pedro, F. Valverde, M. A. Ballicora, J. Preiss, and J. M. Romero
Two Arabidopsis ADP-Glucose Pyrophosphorylase Large Subunits (APL1 and APL2) Are Catalytic
Plant Physiology, September 1, 2008; 148(1): 65 - 76.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S.-K. Hwang, Y. Nagai, D. Kim, and T. W. Okita
Direct Appraisal of the Potato Tuber ADP-glucose Pyrophosphorylase Large Subunit in Enzyme Function by Study of a Novel Mutant Form
J. Biol. Chem., March 14, 2008; 283(11): 6640 - 6647.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
N. Georgelis, E. L. Braun, J. R. Shaw, and L. C. Hannah
The Two AGPase Subunits Evolve at Different Rates in Angiosperms, yet They Are Equally Sensitive to Activity-Altering Amino Acid Changes When Expressed in Bacteria
PLANT CELL, May 1, 2007; 19(5): 1458 - 1472.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. M. Bejar, X. Jin, M. A. Ballicora, and J. Preiss
Molecular Architecture of the Glucose 1-Phosphate Site in ADP-glucose Pyrophosphorylases
J. Biol. Chem., December 29, 2006; 281(52): 40473 - 40484.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
A. A. Iglesias, M. A. Ballicora, J. I. Sesma, and J. Preiss
Domain Swapping between a Cyanobacterial and a Plant Subunit ADP-Glucose Pyrophosphorylase
Plant Cell Physiol., April 1, 2006; 47(4): 523 - 530.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. A. Ballicora, J. R. Dubay, C. H. Devillers, and J. Preiss
Resurrecting the Ancestral Enzymatic Role of a Modulatory Subunit
J. Biol. Chem., March 18, 2005; 280(11): 10189 - 10195.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Crevillen, M. A. Ballicora, A. Merida, J. Preiss, and J. M. Romero
The Different Large Subunit Isoforms of Arabidopsis thaliana ADP-glucose Pyrophosphorylase Confer Distinct Kinetic and Regulatory Properties to the Heterotetrameric Enzyme
J. Biol. Chem., August 1, 2003; 278(31): 28508 - 28515.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
M. A. Ballicora, A. A. Iglesias, and J. Preiss
ADP-Glucose Pyrophosphorylase, a Regulatory Enzyme for Bacterial Glycogen Synthesis
Microbiol. Mol. Biol. Rev., June 1, 2003; 67(2): 213 - 225.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Koller, M. P. Washburn, B. M. Lange, N. L. Andon, C. Deciu, P. A. Haynes, L. Hays, D. Schieltz, R. Ulaszek, J. Wei, et al.
From the Cover: Proteomic survey of metabolic pathways in rice
PNAS, September 3, 2002; 99(18): 11969 - 11974.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. B. Frueauf, M. A. Ballicora, and J. Preiss
Aspartate Residue 142 Is Important for Catalysis by ADP-glucose Pyrophosphorylase from Escherichia coli
J. Biol. Chem., November 30, 2001; 276(49): 46319 - 46325.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. A. Ballicora, J. B. Frueauf, Y. Fu, P. Schurmann, and J. Preiss
Activation of the Potato Tuber ADP-glucose Pyrophosphorylase by Thioredoxin
J. Biol. Chem., January 14, 2000; 275(2): 1315 - 1320.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
S. Lal, J.-H. Choi, J. R. Shaw, and L. C. Hannah
A Splice Site Mutant of Maize Activates Cryptic Splice Sites, Elicits Intron Inclusion and Exon Exclusion, and Permits Branch Point Elucidation
Plant Physiology, October 1, 1999; 121(2): 411 - 418.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
Y. Fu, M. A. Ballicora, J. F. Leykam, and J. Preiss
Mechanism of Reductive Activation of Potato Tuber ADP-glucose Pyrophosphorylase
J. Biol. Chem., September 25, 1998; 273(39): 25045 - 25052.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. A. Ballicora, Y. Fu, N. M. Nesbitt, and J. Preiss
ADP-Glucose Pyrophosphorylase from Potato Tubers. Site-Directed Mutagenesis Studies of the Regulatory Sites
Plant Physiology, September 1, 1998; 118(1): 265 - 274.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
I. H. Kavakli, J.-S. Park, C. J. Slattery, P. R. Salamone, J. Frohlick, and T. W. Okita
Analysis of Allosteric Effector Binding Sites of Potato ADP-glucose Pyrophosphorylase through Reverse Genetics
J. Biol. Chem., October 26, 2001; 276(44): 40834 - 40840.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1998 by the American Society of Plant Biologists