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.

@article{Crosby2014TheAM,
  title={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.},
  author={Heidi A. Crosby and Jorge C Escalante-Semerena},
  journal={Journal of bacteriology},
  year={2014},
  volume={196 8},
  pages={
          1496-504
        }
}

• Heidi A. Crosby, Jorge C Escalante-Semerena
• Published 2014 in Journal of bacteriology
• DOI:10.1128/JB.00004-14

The AMP-forming acyl coenzyme A (acyl-CoA) synthetases are a large class of enzymes found in both anabolic and catabolic pathways that activate fatty acids to acyl-CoA molecules. The protein acetyltransferase (Pat) from Rhodopseudomonas palustris (RpPat) inactivates AMP-forming acyl-CoA synthetases by acetylating the ε-amino group of a conserved, catalytic lysine residue. In all of the previously described RpPat substrates, this lysine residue is located within a PX4GK motif that has been… CONTINUE READING

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