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Microbiology and Molecular Biology Reviews, June 2003, p. 213-225, Vol. 67, No. 2
1092-2172/03/$08.00+0     DOI: 10.1128/MMBR.67.2.213-225.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

ADP-Glucose Pyrophosphorylase, a Regulatory Enzyme for Bacterial Glycogen Synthesis

Miguel A. Ballicora,1 Alberto A. Iglesias,2 and Jack Preiss1*

Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824,1 Bioquímica Básica de Macromoléculas, Grupo de Enzimología Molecular, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Santa Fe, Argentina2

The accumulation of {alpha}-1,4-polyglucans is an important strategy to cope with transient starvation conditions in the environment. In bacteria and plants, the synthesis of glycogen and starch occurs by utilizing ADP-glucose as the glucosyl donor for elongation of the {alpha}-1,4-glucosidic chain. The main regulatory step takes place at the level of ADP-glucose synthesis, a reaction catalyzed by ADP-Glc pyrophosphorylase (PPase). Most of the ADP-Glc PPases are allosterically regulated by intermediates of the major carbon assimilatory pathway in the organism. Based on specificity for activator and inhibitor, classification of ADP-Glc PPases has been expanded into nine distinctive classes. According to predictions of the secondary structure of the ADP-Glc PPases, they seem to have a folding pattern common to other sugar nucleotide pyrophosphorylases. All the ADP-Glc PPases as well as other sugar nucleotide pyrophosphorylases appear to have evolved from a common ancestor, and later, ADP-Glc PPases developed specific regulatory properties, probably by addition of extra domains. Studies of different domains by construction of chimeric ADP-Glc PPases support this hypothesis. In addition to previous chemical modification experiments, the latest random and site-directed mutagenesis experiments with conserved amino acids revealed residues important for catalysis and regulation.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824. Phone: (517) 353-9334. Fax: (517) 353-9334. E-mail: preiss{at}msu.edu.

Microbiology and Molecular Biology Reviews, June 2003, p. 213-225, Vol. 67, No. 2
1092-2172/03/$08.00+0     DOI: 10.1128/MMBR.67.2.213-225.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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