Jan 1, 1983

Regulation of bacterial glycogen synthesis

Molecular and Cellular Biochemistry
Jack PreissP A Baecker


The formation of the alpha 1,4 glucosidic linkages of bacterial glycogen occurs first by synthesis of ADPglucose from ATP and alpha glucose 1-P and then transfer of the glucose moiety from the formed sugar nucleotide to a pre-existing glucan primer. Unlike mammalian glycogen synthesis, regulation occurs at the synthesis of the sugar nucleotide. Generally glycolytic intermediates activate ADPglucose synthesis while AMP, ADP and/or Pi inhibit ADPglucose synthesis. A variation of activator specificity is is seen when the enzyme is isolated from different bacteria and is thought to be related to the predominant type of carbon assimilation or dissimilation pathways present in the particular organism. Evidence indicating that the allosteric activation effects observed in vitro are physiologically pertinent for the regulation of glycogen synthesis is reviewed. The recent experiments in identifying the allosteric activator site of the Escherichia coli ADPglucose pyrophosphorylase as well as other chemical modification studies identifying amino acid residues essential for allosteric activation and for catalytic activity are discussed. Evidence is also presented for the covalent modification of the Rhodopseudomonas sphaeroides ADPglucose...Continue Reading

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Mentioned in this Paper

Biochemical Pathway
Covalent Interaction
Alkalescens-Dispar Group
Enzymes, antithrombotic
Hereditary Orotic Aciduria, Type 1
Enzyme Activity
Rhodobacter sphaeroides
Oligonucleotide Primers
Enzymes for Treatment of Wounds and Ulcers

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