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FEMS Microbiol Lett ; 364(3)2017 02 01.
Article in English | MEDLINE | ID: mdl-28119371

ABSTRACT

Escherichia coli accumulate or degrade glycogen depending on environmental carbon supply. Glycogen phosphorylase (GlgP) and glycogen debranching enzyme (GlgX) are known to act on the glycogen polymer, while maltodextrin phosphorylase (MalP) is thought to remove maltodextrins released by GlgX. To examine the roles of these enzymes in more detail, single, double and triple mutants lacking all their activities were produced. GlgX and GlgP were shown to act directly on the glycogen polymer, while MalP most likely catabolised soluble malto-oligosaccharides. Interestingly, analysis of a triple mutant lacking all three enzymes indicates the presence of another enzyme that can release maltodextrins from glycogen.


Subject(s)
Escherichia coli Proteins/genetics , Escherichia coli/genetics , Escherichia coli/metabolism , Glycogen/metabolism , Escherichia coli Proteins/metabolism , Genes, Bacterial , Glucosyltransferases/genetics , Glucosyltransferases/metabolism , Glycogen Debranching Enzyme System/genetics , Glycogen Phosphorylase/genetics , Glycogen Phosphorylase/metabolism , Polysaccharides/metabolism
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