Biosynthesis of bacterial glycogen: activator specificity of the ADPglucose pyrophosphorylase of Rhodopseudomonads

Abstract

The adenosine diphosphate glucose pyrophosphorylases from Rhodopseudomonas acidophila, Rhodopseudomonas blastica, Rhodopseudomonas globiformis, and Rhodopseudomonas viridis were purified to the extent that their regulatory properties could be studied. With the exception of the R. viridis enzyme, all the enzymes could be activated by pyruvate or its analog, oxamate. The most effective activator for all the enzymes was fructose 6-P. However, the R. globiformis and R. viridis ADP glucose pyrophosphorylases can also be activated by fructose 1,6-P2. Thus a new activator specificity class was observed for the R. viridis enzyme while the R. acidophila and R. blastica enzymes exhibited the same activator specificity previously observed for Rhodopseudomonas capsulata ADPglucose pyrophosphorylase. The R. globiformis enzyme, activated by fructose 6-P, fructose 1,6-P2, and by pyruvate had a similar activator specificity previously seen for the Rhodopseudomonas sphaeroides and Rhodopseudomonas gelatinosa enzymes. For some enzymes, the presence of activator increased the apparent affinity for the substrates and MgCl2. The activator also modulated the sensitivity of the R. viridis and R. acidophila enzymes to Pi inhibition and the R. blastica enzyme to AMP inhibition. ADPglucose is the glucosyl donor for glycogen synthesis in these bacteria. Thus, regulation of glycogen synthesis in these microorganisms is probably regulated by the ratio of the activator concentration to inhibitor concentration.