In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and N(ε)-lysine acetylation

Lignende værker

• New AMP-forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation.
  af: Burckhardt, Rachel M., et al.
  Udgivet: (2019)
• In Salmonella enterica, OatA (Formerly YjgM) Uses O-Acetyl-Serine and Acetyl-CoA to Synthesize N,O-Diacetylserine, Which Upregulates Cysteine Biosynthesis
  af: VanDrisse, Chelsey M., et al.
  Udgivet: (2018)
• Determinants within the C-Terminal Domain of Streptomyces lividans Acetyl-CoA Synthetase that Block Acetylation of Its Active Site Lysine In Vitro by the Protein Acetyltransferase (Pat) Enzyme
  af: Tucker, Alex C., et al.
  Udgivet: (2014)
• Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans
  af: Tucker, Alex C., et al.
  Udgivet: (2012)
• Reversible N(ε)-Lysine Acetylation Regulates the Activity of Acyl-CoA Synthetases Involved in Anaerobic Benzoate Catabolism in Rhodopseudomonas palustris
  af: Crosby, Heidi A., et al.
  Udgivet: (2010)