2.4.2.30	3-amino-1-methyl-5H-pyrido[4,3-b]indole	i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM	675627	
2.4.2.30	4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N,N-dimethylpiperidine-1-carboxamide	activates in presence of Mg2+, inhibits in absence of Mg2+	637997	
2.4.2.30	ATP	5-10 mM, 20-30% stimulation	637995	
2.4.2.30	Bmh1p	a yeast homologue of the human FAS, acts as an activating ExoS cofactor, overview	694800	
2.4.2.30	DNA	absolute requirement	637991, 637993	
2.4.2.30	DNA	enzyme has an N-terminal binding domain	638000	
2.4.2.30	DNA	required	637998	
2.4.2.30	DNA	slightly increases activity	725600	
2.4.2.30	DNA	the enzyme is completely dependent on the presence of DNA containing single or double stranded breaks. Activation results in a decondensation of chromatin superstructure in vitro, which is caused mainly by hyper(ADP-ribosyl)ation of histone H1	637999	
2.4.2.30	FAS	exoenzyme S absolutely requires a soluble eukaryotic protein, named FAS (Factor Activating exoenzyme E), in order to ADP-ribosylate all substrates. In the presence of FAS, exoenzyme S ADP-ribosylates several proteins in lysates of Pseudomonas aeruginosa. Purification and characterization of FAS	662089