Ontology highlight
ABSTRACT:
SUBMITTER: Ballicora MA
PROVIDER: S-EPMC1951854 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Ballicora Miguel A MA Erben Esteban D ED Yazaki Terutaka T Bertolo Ana L AL Demonte Ana M AM Schmidt Jennifer R JR Aleanzi Mabel M Bejar Clarisa M CM Figueroa Carlos M CM Fusari Corina M CM Iglesias Alberto A AA Preiss Jack J
Journal of bacteriology 20070511 14
ADP-glucose pyrophosphorylase (ADP-Glc PPase) is the enzyme responsible for the regulation of bacterial glycogen synthesis. To perform a structure-function relationship study of the Escherichia coli ADP-Glc PPase enzyme, we studied the effects of pentapeptide insertions at different positions in the enzyme and analyzed the results with a homology model. We randomly inserted 15 bp in a plasmid with the ADP-Glc PPase gene. We obtained 140 modified plasmids with single insertions of which 21 were i ...[more]