Structural highlights
Function
PAT_MYCS2 Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.[1] [2]
References
- ↑ Nambi S, Basu N, Visweswariah SS. cAMP-regulated protein lysine acetylases in mycobacteria. J Biol Chem. 2010 Aug 6;285(32):24313-23. doi: 10.1074/jbc.M110.118398. Epub 2010, May 27. PMID:20507997 doi:http://dx.doi.org/10.1074/jbc.M110.118398
- ↑ Xu H, Hegde SS, Blanchard JS. Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP. Biochemistry. 2011 Jul 5;50(26):5883-92. doi: 10.1021/bi200156t. Epub 2011 Jun, 10. PMID:21627103 doi:http://dx.doi.org/10.1021/bi200156t