| Literature DB >> 28119371 |
Lindi Strydom1, Jonathan Jewell1, Michael A Meier1, Gavin M George2, Barbara Pfister2, Samuel Zeeman2, Jens Kossmann1, James R Lloyd1.
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. © FEMS 2017. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.Entities:
Keywords: Escherichia coli; Glycogen; glycogen accumulation; glycogen debranching enzyme; glycogen phosphorylase; maltodextrin phosphorylase
Mesh:
Substances:
Year: 2017 PMID: 28119371 DOI: 10.1093/femsle/fnx016
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742