EC Number   |
Inhibitors |
Structure |
|---|
  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 |
   |
| 2.3.1.192 | KCl |
80 mM KC1, ca. 30% inhibition, inhibition is seen at all concentrations of glutamine up to 150 mM |
|
| 2.3.1.192 | Mg2+ |
1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration |
|
| 2.3.1.192 | more |
human enzyme is insensitive to salts |
|
| 2.3.1.192 | Ni2+ |
2 mM, 28% residual activity |
|
| 2.3.1.192 | p-chloromercuribenzoate |
- |
|
| 2.3.1.192 | Zn2+ |
1 mM, 46% residual activity |
|
