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

Eitemau Tebyg

• In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and N(ε)-lysine acetylation
  gan: VanDrisse, Chelsey M., et al.
  Cyhoeddwyd: (2018)
• Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans
  gan: Tucker, Alex C., et al.
  Cyhoeddwyd: (2012)
• The Structure of S. lividans Acetoacetyl-CoA Synthetase Shows a Novel Interaction Between the C-terminal Extension and the N-terminal Domain
  gan: Mitchell, Carter A., et al.
  Cyhoeddwyd: (2015)
• The Acetylation Motif in AMP-Forming Acyl Coenzyme A Synthetases Contains Residues Critical for Acetylation and Recognition by the Protein Acetyltransferase Pat of Rhodopseudomonas palustris
  gan: Crosby, Heidi A., et al.
  Cyhoeddwyd: (2014)
• New AMP-forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation.
  gan: Burckhardt, Rachel M., et al.
  Cyhoeddwyd: (2019)