2.3.1.192	2,4,5-trichlorophenoxyacetyl-CoA	competitive	159684	
2.3.1.192	2,4-dichlorophenoxyacetyl-CoA	competitive	80357	
2.3.1.192	5,5'-dithiobis(2-nitrobenzoate)	phenylacetyl-CoA partially protects phenylacetyltransferase against 5,5'-dithiobis(2-nitrobenzoate) inactivation	303	
2.3.1.192	acylglycine	noncompetitive	159685	
2.3.1.192	benzoyl-CoA	-	394	
2.3.1.192	butyryl-CoA	-	270	
2.3.1.192	citrate	40 mM, 22% residual activity	131	
2.3.1.192	CoA	noncompetitve	18	
2.3.1.192	CoA	at physiologic concentrations of substrate, the arylacetyl transferase is extensively inhibited by CoA, inhibition is greatly reduced by ions. The 3-phosphate group on CoA is important for binding to the salt-free enzyme but in the presence of ions its importance is diminished	18	
2.3.1.192	K2SO4	55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration	2560	
2.3.1.192	KCl	110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration. Inhibition results in a large decrease in the affinity of the enzyme for phenylacetyl-CoA. In the presence of KCl the KD values for phenylacetyl-CoA and naphthylacetyl-CoA are similar, but the KD for glycine is extremely high for 1-naphthylacetyl-CoA conjugation	79	
2.3.1.192	KCl	80 mM KC1, ca. 30% inhibition, inhibition is seen at all concentrations of glutamine up to 150 mM	79	
2.3.1.192	Mg2+	1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration	6	
2.3.1.192	additional information	human enzyme is insensitive to salts	2	
2.3.1.192	Ni2+	2 mM, 28% residual activity	38	
2.3.1.192	p-chloromercuribenzoate	-	43	
2.3.1.192	Zn2+	1 mM, 46% residual activity	14