ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes.

Lignende værker

• Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system.
  af: Reizer, J, et al.
  Udgivet: (1984)
• Regulation of sugar uptake via the phosphoenolpyruvate-dependent phosphotransferase systems in Bacillus subtilis and Lactococcus lactis is mediated by ATP-dependent phosphorylation of seryl residue 46 in HPr.
  af: Ye, J J, et al.
  Udgivet: (1996)
• Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by phosphoenolpyruvate-dependent phosphorylation catalyzed by enzyme I and HPr of the phosphotransferase system.
  af: Deutscher, J, et al.
  Udgivet: (1986)
• Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis.
  af: Deutscher, J, et al.
  Udgivet: (1994)
• Mechanism and regulation of phosphate transport in Streptococcus pyogenes.
  af: Reizer, J, et al.
  Udgivet: (1987)