Novel Listerial Glycerol Dehydrogenase- and Phosphoenolpyruvate-Dependent Dihydroxyacetone Kinase System Connected to the Pentose Phosphate Pathway

Ítems similars

• The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions
  per: Deutscher, Josef, et al.
  Publicat: (2014)
• Interaction with Enzyme IIB(Mpo) (EIIB(Mpo)) and Phosphorylation by Phosphorylated EIIB(Mpo) Exert Antagonistic Effects on the Transcriptional Activator ManR of Listeria monocytogenes
  per: Zébré, Arthur Constant, et al.
  Publicat: (2015)
• Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by phosphoenolpyruvate-dependent phosphorylation catalyzed by enzyme I and HPr of the phosphotransferase system.
  per: Deutscher, J, et al.
  Publicat: (1986)
• Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system.
  per: Deutscher, J, et al.
  Publicat: (1993)
• Rickettsia prowazekii Uses an sn-Glycerol-3-Phosphate Dehydrogenase and a Novel Dihydroxyacetone Phosphate Transport System To Supply Triose Phosphate for Phospholipid Biosynthesis
  per: Frohlich, Kyla M., et al.
  Publicat: (2010)