PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10794727-7 2000 Enzyme-kinetic analysis of these mutant proteins with the NAT1-selective and NAT2-selective substrates p-aminosalicylic acid (PAS) and sulphamethazine (SMZ) respectively suggests that residues 125, 127 and 129 are important determinants of NAT1-type and NAT2-type substrate selectivity. Aminosalicylic Acid 103-124 N-acetyltransferase 1 Homo sapiens 58-62 25834322-10 2015 The effect of NAT1 status on TGN seems to be persistent even after one month since the interruption of the aminosalicylate. Aminosalicylic Acid 107-122 N-acetyltransferase 1 Homo sapiens 14-18 25834322-13 2015 CONCLUSION: NAT1 genotype affects TGN levels in patients treated with thiopurines and aminosalicylates and could therefore influence the toxicity and efficacy of these drugs; however the number of patients evaluated is limited and this has to be considered a pilot study. Aminosalicylic Acid 86-102 N-acetyltransferase 1 Homo sapiens 12-16 16003948-7 2005 However, p-aminosalicylic acid (PAS), previously reported to be a human NAT1 and hamster NAT2 selective substrate, exhibits 20-fold higher specificity for hamster rNAT2 (k(cat)/Kmb 3410 microM(-1) s(-1)) than for human rNAT1 (k(cat)/Kmb 169.4 microM(-1) s(-1)). Aminosalicylic Acid 9-30 N-acetyltransferase 1 Homo sapiens 72-76 16003948-7 2005 However, p-aminosalicylic acid (PAS), previously reported to be a human NAT1 and hamster NAT2 selective substrate, exhibits 20-fold higher specificity for hamster rNAT2 (k(cat)/Kmb 3410 microM(-1) s(-1)) than for human rNAT1 (k(cat)/Kmb 169.4 microM(-1) s(-1)). Aminosalicylic Acid 32-35 N-acetyltransferase 1 Homo sapiens 72-76 15545312-4 2004 p-Aminosalicylate, used for antitubercular treatment, is also metabolized by N-acetyltransferase 1 and could potentially inhibit sulfamethoxazole metabolism. Aminosalicylic Acid 0-17 N-acetyltransferase 1 Homo sapiens 77-98 24467436-5 2014 The human gene products NAT1 and NAT2 have distinct substrate specificities: NAT2 acetylates hydralazine and human NAT1 acetylates p-aminosalicylate (p-AS) and the folate catabolite para-aminobenzoylglutamate (p-abaglu). Aminosalicylic Acid 131-148 N-acetyltransferase 1 Homo sapiens 24-28 24467436-5 2014 The human gene products NAT1 and NAT2 have distinct substrate specificities: NAT2 acetylates hydralazine and human NAT1 acetylates p-aminosalicylate (p-AS) and the folate catabolite para-aminobenzoylglutamate (p-abaglu). Aminosalicylic Acid 131-148 N-acetyltransferase 1 Homo sapiens 115-119 24467436-5 2014 The human gene products NAT1 and NAT2 have distinct substrate specificities: NAT2 acetylates hydralazine and human NAT1 acetylates p-aminosalicylate (p-AS) and the folate catabolite para-aminobenzoylglutamate (p-abaglu). Aminosalicylic Acid 150-154 N-acetyltransferase 1 Homo sapiens 24-28 24467436-5 2014 The human gene products NAT1 and NAT2 have distinct substrate specificities: NAT2 acetylates hydralazine and human NAT1 acetylates p-aminosalicylate (p-AS) and the folate catabolite para-aminobenzoylglutamate (p-abaglu). Aminosalicylic Acid 150-154 N-acetyltransferase 1 Homo sapiens 115-119 10794727-7 2000 Enzyme-kinetic analysis of these mutant proteins with the NAT1-selective and NAT2-selective substrates p-aminosalicylic acid (PAS) and sulphamethazine (SMZ) respectively suggests that residues 125, 127 and 129 are important determinants of NAT1-type and NAT2-type substrate selectivity. Aminosalicylic Acid 103-124 N-acetyltransferase 1 Homo sapiens 240-244 10794727-7 2000 Enzyme-kinetic analysis of these mutant proteins with the NAT1-selective and NAT2-selective substrates p-aminosalicylic acid (PAS) and sulphamethazine (SMZ) respectively suggests that residues 125, 127 and 129 are important determinants of NAT1-type and NAT2-type substrate selectivity. Aminosalicylic Acid 126-129 N-acetyltransferase 1 Homo sapiens 58-62 10794727-7 2000 Enzyme-kinetic analysis of these mutant proteins with the NAT1-selective and NAT2-selective substrates p-aminosalicylic acid (PAS) and sulphamethazine (SMZ) respectively suggests that residues 125, 127 and 129 are important determinants of NAT1-type and NAT2-type substrate selectivity. Aminosalicylic Acid 126-129 N-acetyltransferase 1 Homo sapiens 240-244 7598738-4 1995 The Km of the recombinant NAT1 protein for the substrates para-aminobenzoate (p-aba) and 4-aminosalicylate are 14.3 and 11.8 microM, respectively. Aminosalicylic Acid 89-106 N-acetyltransferase 1 Homo sapiens 26-30 9511182-0 1998 Identification and characterization of variant alleles of human acetyltransferase NAT1 with defective function using p-aminosalicylate as an in-vivo and in-vitro probe. Aminosalicylic Acid 117-134 N-acetyltransferase 1 Homo sapiens 82-86 9511182-3 1998 The NAT1-selective substrate p-aminosalicylic acid (PAS) was used as a probe for NAT1 function. Aminosalicylic Acid 29-50 N-acetyltransferase 1 Homo sapiens 4-8 9511182-3 1998 The NAT1-selective substrate p-aminosalicylic acid (PAS) was used as a probe for NAT1 function. Aminosalicylic Acid 29-50 N-acetyltransferase 1 Homo sapiens 81-85 9511182-3 1998 The NAT1-selective substrate p-aminosalicylic acid (PAS) was used as a probe for NAT1 function. Aminosalicylic Acid 52-55 N-acetyltransferase 1 Homo sapiens 4-8 9511182-3 1998 The NAT1-selective substrate p-aminosalicylic acid (PAS) was used as a probe for NAT1 function. Aminosalicylic Acid 52-55 N-acetyltransferase 1 Homo sapiens 81-85 9511182-8 1998 Biochemical investigations in whole blood lysates from case 244 suggested a NAT1 kinetic defect, with a 20-fold increased apparent K(m) for PAS and a 90-fold decreased Vmax for AcPAS formation. Aminosalicylic Acid 140-143 N-acetyltransferase 1 Homo sapiens 76-80 10692486-7 2000 Addition of other NAT1 substrates, such as p-aminosalicylic acid, ethyl-p-aminobenzoate, or p-aminophenol to peripheral blood mononuclear cells in culture also resulted in significant (P <.05) decreases in NAT1 activity. Aminosalicylic Acid 43-64 N-acetyltransferase 1 Homo sapiens 18-22 9342682-0 1997 Determination of p-aminosalicylic acid and its N-acetylated metabolite in human urine by capillary zone electrophoresis as a measure of in vivo N-acetyltransferase 1 activity. Aminosalicylic Acid 17-38 N-acetyltransferase 1 Homo sapiens 144-165 7889851-5 1994 NAT1 codes for a protein with ubiquitous tissue distribution and a high affinity for p-aminobenzoic acid and p-aminosalicylic acid, so-called monomorphic substrates. Aminosalicylic Acid 109-130 N-acetyltransferase 1 Homo sapiens 0-4 1996083-6 1991 Recombinant and human liver NAT1 enzymes showed the same characteristic selectivity (low apparent Km, high Vmax) for the "monomorphic" substrates p-aminosalicylic acid and p-aminobenzoic acid. Aminosalicylic Acid 146-167 N-acetyltransferase 1 Homo sapiens 28-32