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Resurrecting the ancestral enzymatic role of a modulatory subunit.
Ballicora MA, Dubay JR, Devillers CH, Preiss J. Ballicora MA, et al. Among authors: preiss j. J Biol Chem. 2005 Mar 18;280(11):10189-95. doi: 10.1074/jbc.M413540200. Epub 2005 Jan 4. J Biol Chem. 2005. PMID: 15632142 Free article.
Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin.
Ballicora MA, Frueauf JB, Fu Y, Schürmann P, Preiss J. Ballicora MA, et al. Among authors: preiss j. J Biol Chem. 2000 Jan 14;275(2):1315-20. doi: 10.1074/jbc.275.2.1315. J Biol Chem. 2000. PMID: 10625679 Free article.
The main type of regulation of this enzyme is allosteric, and its activity is controlled by the ratio of activator, 3-phosphoglycerate to inhibitor, P(i). It was reported (Fu, Y., Ballicora, M. A., Leykam, J. F., and Preiss, J. (1998) J. Biol. Chem. 27 …
The main type of regulation of this enzyme is allosteric, and its activity is controlled by the ratio of activator, 3-phosphoglycerate to in …
Alteration of inhibitor selectivity by site-directed mutagenesis of Arg(294) in the ADP-glucose pyrophosphorylase from Anabaena PCC 7120.
Frueauf JB, Ballicora MA, Preiss J. Frueauf JB, et al. Among authors: preiss j. Arch Biochem Biophys. 2002 Apr 15;400(2):208-14. doi: 10.1016/S0003-9861(02)00015-2. Arch Biochem Biophys. 2002. PMID: 12054431
Previous alanine scanning mutagenesis of ADP-glucose pyrophosphorylase from Anabaena PCC 7120 indicated that Arg(294) plays a role in inhibition by orthophosphate [J. Sheng, J. Preiss, Biochemistry 36 (1997) 13077]. In this study, analysis of several site-dir …
Previous alanine scanning mutagenesis of ADP-glucose pyrophosphorylase from Anabaena PCC 7120 indicated that Arg(294) plays a role in inhibi …
ADP-glucose pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits.
Frueauf JB, Ballicora MA, Preiss J. Frueauf JB, et al. Among authors: preiss j. Plant J. 2003 Feb;33(3):503-11. doi: 10.1046/j.1365-313x.2003.01643.x. Plant J. 2003. PMID: 12581308 Free article.
Asp142 in the homotetrameric ADP-glucose pyrophosphorylase (ADP-Glc PPase) enzyme from Escherichia coli was demonstrated to be involved in catalysis of this enzyme [Frueauf, J.B., Ballicora, M.A. and Preiss J. (2001) J. Biol. Chem., 276, 46319-46325]. …
Asp142 in the homotetrameric ADP-glucose pyrophosphorylase (ADP-Glc PPase) enzyme from Escherichia coli was demonstrated to be involved in c …
448 results