Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system.

Míreanna Comhchosúla

• ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes.
  le: Deutscher, J, et al.
  Foilsithe: (1983)
• ATP-dependent phosphorylation of serine-46 in the phosphocarrier protein HPr regulates lactose/H+ symport in Lactobacillus brevis.
  le: Ye, J J, et al.
  Foilsithe: (1994)
• 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.
  le: Ye, J J, et al.
  Foilsithe: (1996)
• 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.
  le: Deutscher, J, et al.
  Foilsithe: (1994)
• Mechanism of inducer expulsion in Streptococcus pyogenes: a two-step process activated by ATP.
  le: Reizer, J, et al.
  Foilsithe: (1983)