Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans

Gelijkaardige items

• 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
  door: Tucker, Alex C., et al.
  Gepubliceerd in: (2014)
• The Structure of S. lividans Acetoacetyl-CoA Synthetase Shows a Novel Interaction Between the C-terminal Extension and the N-terminal Domain
  door: Mitchell, Carter A., et al.
  Gepubliceerd in: (2015)
• In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and N(ε)-lysine acetylation
  door: VanDrisse, Chelsey M., et al.
  Gepubliceerd in: (2018)
• New AMP-forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation.
  door: Burckhardt, Rachel M., et al.
  Gepubliceerd in: (2019)
• Stimulation of hepatic cholesterol biosynthesis by fatty acids. Effects of oleate on cytoplasmic acetoacetyl-CoA thiolase, acetoacetyl-CoA synthetase and hydroxymethylglutaryl-CoA synthase.
  door: Salam, W H, et al.
  Gepubliceerd in: (1989)