ADP-Glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis

Ballicora, Miguel A.; Iglesias, Alberto A.; Preiss, Jack

doi:10.1128/mmbr.67.2.213-225.2003

Cited by 259Bacterial Genetics and BiotechnologyGlycogen Storage Diseases and MyoclonusBiochemical and Molecular Research

ADP-Glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis

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Ballicora, Miguel A., Iglesias, Alberto A., Preiss, Jack·2003·Microbiology and Molecular Biology Reviews

DOI 10.1128/mmbr.67.2.213-225.2003PMC PMC156471

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Abstract

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.

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Glycogen synthesis in A. platensis is strictly regulated by the amount of phosphorous in the cell, and ADP-glucose pyrophosphorylase is responsible for producing ADP-Glc, the glucosyl donor for elongation of α-1,4-glucosidic chain to synthesize glycogen.
“The glycogen synthesis in Arthrospira platensis is strictly regulated by the amount of phosphorous in the cell, and the enzyme ADP-glucose pyrophosphorylase is responsible for producing ADP-Glc, which is the glucosyl donor for the elongation of the α-1,4-glucosidic chain to synthesize glycogen [71].”
From Arthrospira platensis as a Feasible Feedstock for Bioethanol Production (2021) · cites this paper as [71]
ADP-glucose diphosphorylase (AGPase) controls glycogen synthesis in bacteria in an ATP-dependent reaction and seems to be regulated by 3PG (activator) and Pi (inhibitor).
“The enzyme ADP-glucose diphosphorylase (AGPase; EC 2.7.7.27, encoded by the agp gene, also known as glgC) controls glycogen synthesis in bacteria in an ATP-dependent reaction and seems to be regulated by 3PG (activator) and Pi (inhibitor) (Ballicora et al. 2003; Gomez-Casati et al. 2003).”
From Renewable energy from Cyanobacteria: energy production optimization by metabolic pathway engineering (2011) · cites this paper as Ballicora et al. 2003

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Authors: Ballicora, M. A., Iglesias, A. A., & Preiss, J.
Affiliations: Michigan State University (US)
Bioquímica Básica de Macromoléculas, Grupo de Enzimología Molecular, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Santa Fe, Argentina
ORCID: Ballicora, Miguel A.
Venue: Microbiology and Molecular Biology Reviews
Publisher: American Society for Microbiology
Published: 2003-06
Volume: 67
Issue: 2
Pages: 213-225
ISSN: 1092-2172 (ISSN-L)
1098-5557
DOI: 10.1128/mmbr.67.2.213-225.2003
PMC: PMC156471
OpenAlex: W2132112146
Cited by: 259
References: 109
Citations by year: 2026: 7 · 2025: 6 · 2024: 8 · 2023: 10 · 2022: 13 · 2021: 9 · 2020: 10 · 2019: 8 · 2018: 15 · 2017: 13 · 2016: 9 · 2015: 13 · 2014: 12 · 2013: 22 · 2012: 8
FWCI: 1.02
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Microbiology and Molecular Biology Reviews (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: ADP-glucose pyrophosphorylase, allosteric regulation, chimeric enzymes, site-directed mutagenesis, chemical modification, starvation adaptation
MeSH terms: Amino Acid Sequence, Bacteria, Glucans, Glycogen, Molecular Sequence Data, Nucleotidyltransferases, Plants, Protein Conformation, Sequence Alignment, Glucose-1-Phosphate Adenylyltransferase

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ADP-Glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis

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