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


     

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 (22)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Greene, T. W.
Right arrow Articles by Okita, T. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Greene, T. W.
Right arrow Articles by Okita, T. W.
Agricola
Right arrow Articles by Greene, T. W.
Right arrow Articles by Okita, T. W.

PLANT PHYSIOLOGY , Vol 112, Issue 3 1315-1320, Copyright © 1996 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Aspartic Acid 413 Is Important for the Normal Allosteric Functioning of ADP-Glucose Pyrophosphorylase

T. W. Greene, R. L. Woodbury and T. W. Okita
Institute of Biological Chemistry (T.W.G., R.L.W., T.W.O.), Plant Physiology Program (T.W.G.), and Genetics and Cell Biology Program (R.L.W.), Washington State University, Pullman, Washington 99164-6340

As part of a structure-function analysis of the higher-plant ADP-glucose pyrophosphorylase (AGP), we used a random mutagenesis approach in combination with a novel bacterial complementation system to isolate over 100 mutants that were defective in glycogen production (T.W. Greene, S.E. Chantler, M.L. Khan, G.F. Barry, J. Preiss, T.W. Okita [1996] Proc Natl Acad Sci USA 93: 1509-1513). One mutant of the large subunit M27 was identified by its capacity to only partially complement a mutation in the structural gene for the bacterial AGP (glg C), as determined by its light-staining phenotype when cells were exposed to I2 vapors. Enzyme-linked immunosorbent assay and enzymatic pyrophosphorylysis assays of M27 cell extracts showed that the level of expression and AGP activity was comparable to those of cells that expressed the wild-type recombinant enzyme. Kinetic analysis indicated that the M27 AGP displays normal Michaelis constant values for the substrates glucose-1-phosphate and ATP but requires 6- to 10-fold greater levels of 3-phosphoglycerate (3-PGA) than the wild-type recombinant enzyme for maximum activation. DNA sequence analysis showed that M27 contains a single point mutation that resulted in the replacement of aspartic acid 413 to alanine. Substitution of a lysine residue at this site almost completely abolished activation by 3-PGA. Aspartic acid 413 is adjacent to a lysine residue that was previously identified by chemical modification studies to be important in the binding of 3-PGA (K. Ball, J. Preiss [1994] J Biol Chem 269: 24706-24711). The kinetic properties of M27 corroborate the importance of this region in the allosteric regulation of a higher-plant AGP.


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
N. Georgelis, J. R. Shaw, and L. C. Hannah
Phylogenetic Analysis of ADP-Glucose Pyrophosphorylase Subunits Reveals a Role of Subunit Interfaces in the Allosteric Properties of the Enzyme
Plant Physiology, September 1, 2009; 151(1): 67 - 77.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
G. Seibold, S. Dempf, J. Schreiner, and B. J. Eikmanns
Glycogen formation in Corynebacterium glutamicum and role of ADP-glucose pyrophosphorylase
Microbiology, April 1, 2007; 153(4): 1275 - 1285.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
J. M. Cross, M. Clancy, J. R. Shaw, T. W. Greene, R. R. Schmidt, T. W. Okita, and L. C. Hannah
Both Subunits of ADP-Glucose Pyrophosphorylase Are Regulatory
Plant Physiology, May 1, 2004; 135(1): 137 - 144.
[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
 Plant Cell PhysiolHome page
C. H. Harn, J. M. Bae, S. S. Lee, S. R. Min, and J. R. Liu
Presence of Multiple cDNAs Encoding an Isoform of ADP-Glucose Pyrophosphorylase Large Subunit from Sweet Potato and Characterization of Expression Levels
Plant Cell Physiol., November 1, 2000; 41(11): 1235 - 1242.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. W. Greene and L. C. Hannah
Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
PNAS, October 27, 1998; 95(22): 13342 - 13347.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. W. Greene, I. H. Kavakli, M. L. Kahn, and T. W. Okita
Generation of up-regulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics
PNAS, August 18, 1998; 95(17): 10322 - 10327.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
T. W. Greene and L. C. Hannah
Maize Endosperm ADP–Glucose Pyrophosphorylase SHRUNKEN2 and BRITTLE2 Subunit Interactions
PLANT CELL, August 1, 1998; 10(8): 1295 - 1306.
[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 © 1996 by the American Society of Plant Biologists