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System-wide Studies of N-Lysine Acetylation in Rhodopseudomonas palustris Reveals Substrate Specificity of Protein Acetyltran...

by Heidi Crosby, Dale A Pelletier, Gregory B Hurst, Jorge Escalante-semerena
Publication Type
Journal
Journal Name
Journal of Biological Chemistry
Publication Date
Page Numbers
15590 to 15601
Volume
287
Issue
19

Background: Protein acetylation is widespread in
prokaryotes.
Results: Six new acyl-CoA synthetases whose
activities are controlled by acetylation were
identified, and their substrate preference
established. A new protein acetyltransferase was
also identified and its substrate specificity
determined.
Conclusion: Protein acetyltransferases acetylate a
conserved lysine residue in protein substrates.
Significance: The R. palustris Pat enzyme
specifically acetylates AMP-forming acyl-CoA
synthetases and regulates fatty acid metabolism.