Reversible Lysine Acetylation Regulates Activity of Human Glycine N-Acyltransferase-like 2 (hGLYATL2): Implications for Production of Glycine-conjugated Signaling Molecules

Authors

Dominick P. Waluk, Stockholm University
Filip Sucharski, AGH University of Science & Technology Poland
Laszlo Sipos, Stockholm University
Jerzy Silberring, AGH University of Science & Technology, Poland
Mary Hunt, Technological University DublinFollow

Document Type

Article

Rights

Available under a Creative Commons Attribution Non-Commercial Share Alike 4.0 International Licence

Disciplines

1.6 BIOLOGICAL SCIENCES

Publication Details

Journal of Biological Chemistry

Abstract

Background: Lysine acetylation is a major post-translational modification of proteins.

Results: Human glycine N-acyltransferase-like 2 is regulated by acetylation/deacetylation of lysine 19.

Conclusion: Reversible lysine acetylation is important in regulating the activity and function of human glycine N-acyltransferases.

Significance: Our study links post-translational modification of proteins with the production of lipid signaling molecules, the N-acyl glycines.

DOI

https:doi.org/10.1074/jbc.M112.347260

Recommended Citation

Waluk, D., Sucharski, F., Sipos, L., Silberring, J. & Hunt, M. (2012). Reversible Lysine Acetylation Regulates Activity of Human Glycine N-Acyltransferase-like 2 (hGLYATL2): Implications for Production of Glycine-conjugated Signaling Molecules. The Journal of Biological Chemistry, 287(20), pp.16158-16167. doi:10.1074/jbc.M112.347260