TY - JOUR
T1 - Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794
T2 - A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa
AU - Majorek, Karolina A.
AU - Kuhn, Misty L.
AU - Chruszcz, Maksymilian
AU - Anderson, Wayne F.
AU - Minor, Wladek
PY - 2013/10/18
Y1 - 2013/10/18
N2 - Background: Gcn5-related N-acetyltransferases (GNATs) are involved in small molecule and protein acetylation in all organisms. Results: Crystallographic and biochemical characterization of PA4794 is shown, including identification of substrates and inhibitors. Conclusion: PA4794 is a new bacterial C-terminal lysine protein acetyltransferase inhibited by cephalosporins. Significance: PA4794 is the first identified acetyltransferase specific for C-terminal lysine; identified interactions with cephalosporins may be of clinical relevance.
AB - Background: Gcn5-related N-acetyltransferases (GNATs) are involved in small molecule and protein acetylation in all organisms. Results: Crystallographic and biochemical characterization of PA4794 is shown, including identification of substrates and inhibitors. Conclusion: PA4794 is a new bacterial C-terminal lysine protein acetyltransferase inhibited by cephalosporins. Significance: PA4794 is the first identified acetyltransferase specific for C-terminal lysine; identified interactions with cephalosporins may be of clinical relevance.
UR - http://www.scopus.com/inward/record.url?scp=84886928360&partnerID=8YFLogxK
U2 - 10.1074/jbc.M113.501353
DO - 10.1074/jbc.M113.501353
M3 - Article
C2 - 24003232
AN - SCOPUS:84886928360
SN - 0021-9258
VL - 288
SP - 30223
EP - 30235
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 42
ER -