EC Number   |
Reaction |
Reference |
|---|
   2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
a conserved active site loop is involved in substrate recognition, structure analysis, Ser125 in NAT2 is proximal to the catalytic triad and faces a passageway to the catalytic core |
671686 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
Cys69, His108, and Asp125 form the catalytic triad |
-, 674321 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
it is shown that the formation of a thiolate-imidazolium ion pair by Cys68 and His107 is involved in the catylytic mechanism. Asp122 is required for optimal catalysis and structural stability. Enzyme deacetylation step proceeds via nucleophilic attack for acceptor amines with pKa values less than 5.5 and by deprotonation of a tetrahedral intermediate for amines with pKa values greater than 5.5 |
686254 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
mechanism and characterization of active site |
487118, 487128 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
mechanism and inactivation |
487139 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
molecular mechanism of arylamine acetylation by the catalytic triad of NAT1, overview, the catalytic triad is formed by Cys68, His107, and Asp122 |
674029 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
ping pong reaction mechanism, kinetic mechanism, overview |
672795 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
ping pong reaction mechanism, the enzyme contains a strictly conserved a Cys-His-Asp catalytic triad, acetylation of the hamster NAT2 is dependent on a thiolate-imidazolium ion pair, Cys-S--His-ImH+, and not a general acid-base catalysis, a deacetylation mechanism dominated by nucleophilic attack of the thiol ester for arylamines |
671967 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
ping-pong bi-bi mechanism |
-, 487121, 487123, 487133 |
| 2.3.1.5 | acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
residue Y190 is critical for maximizing the acetylation rate of NAT2 and the transacetylation rate of substrate p-aminobenzoic acid. Y190 also plays an important role in determining the pKa of the active site Cys during acetylation, as well as the pH versus the rate profile for transacetylation |
703672 |
