A fragment consisting of the first 204 amino-terminal amino acids of human arylamine N-acetyltransferase one (NAT1) and the first transacetylation step of catalysis.
Human arylamine N-acetyltransferase 1 (NAT1) has 290 amino acids and acetylates arylamines from acetyl coenzyme A. The acetyl group forms a thiolester with Cys 68 in the enzyme, and the acetyl group is then transferred to the arylamine. When NAT1 is expressed using the pGEX vector, the glutathione S-transferase (GST)-NAT1 fusion protein catalyses the acetylation of the NAT1 substrate p-aminobenzoic acid from acetyl CoA. Neither GST alone, nor a fusion protein of GST with the N-terminal 204 amino acids of NAT, catalyses the acetylation of p-aminobenzoic acid from acetyl CoA. Using [3H]acetyl CoA as substrate, it is shown that the full-length NAT1 and the N-terminal 204 amino acids of NAT1 each form an acetylated intermediate on reaction with acetyl CoA.
Sinclair
J
J
Department of Pharmacology, University of Oxford, U.K.
Sim
E
E
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000107:Acetylation; D001191:Arylamine N-Acetyltransferase / Q000378:metabolism*; D003001:Cloning, Molecular; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D013329:Structure-Activity Relationship
D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D000105:Acetyl Coenzyme A; D001191:Arylamine N-Acetyltransferase; D005982:Glutathione Transferase