PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19932120-9 2010 SIGNIFICANCE: Since increasing NAT1 activity decreases folate in at least one tissue, the detrimental effect of expression of human NAT1 in combination with endogenous mouse Nat2 may be a consequence of increased catabolism of folate. Folic Acid 55-61 N-acetyltransferase 1 Homo sapiens 31-35 20870783-1 2011 Arylamine N-acetyltransferase-1 (NAT1) has been associated with disorders involving folate metabolism, such as spina bifida, as well as numerous human cancers. Folic Acid 84-90 N-acetyltransferase 1 Homo sapiens 0-31 20870783-1 2011 Arylamine N-acetyltransferase-1 (NAT1) has been associated with disorders involving folate metabolism, such as spina bifida, as well as numerous human cancers. Folic Acid 84-90 N-acetyltransferase 1 Homo sapiens 33-37 20026257-2 2010 Both human NAT1 and its murine equivalent NAT2 have previously been shown to play roles in the catabolism of folate, which is required for the synthesis of S-adenosylmethionine, the methyl donor for cellular methylation reactions. Folic Acid 109-115 N-acetyltransferase 1 Homo sapiens 11-15 19932120-9 2010 SIGNIFICANCE: Since increasing NAT1 activity decreases folate in at least one tissue, the detrimental effect of expression of human NAT1 in combination with endogenous mouse Nat2 may be a consequence of increased catabolism of folate. Folic Acid 227-233 N-acetyltransferase 1 Homo sapiens 132-136 19842618-2 2009 NAT1 also catalyzes the N-acetylation of 4-aminobenzoylglutamic acid, a product of folic acid degradation, and is associated with endogenous functions in embryonic development. Folic Acid 83-93 N-acetyltransferase 1 Homo sapiens 0-4 17392017-6 2007 Recent links between NAT1 genotypes and susceptibility to spina bifida suggests that the enzyme has an important role in folate homeostasis. Folic Acid 121-127 N-acetyltransferase 1 Homo sapiens 21-25 18642144-8 2008 The mammalian NAT enzymes are involved in metabolism of drugs and carcinogens but there is growing evidence, including from transgenic mice, that human NAT1 has an endogenous role in folate degradation. Folic Acid 183-189 N-acetyltransferase 1 Homo sapiens 152-156 17961509-6 2007 These results support an in vivo role for mouse Nat2/human NAT1 in folate metabolism. Folic Acid 67-73 N-acetyltransferase 1 Homo sapiens 59-63 19664055-6 2009 In addition to its role in xenobiotic metabolism, several studies have suggested that NAT1 is involved in other physiological and/or pathological processes, such as folate metabolism or cancer progression. Folic Acid 165-171 N-acetyltransferase 1 Homo sapiens 86-90 16680433-2 2006 N-acetyltransferase 1 (NAT1) participates in the catabolism of folates and the acetylation of aromatic and heterocyclic amines. Folic Acid 63-70 N-acetyltransferase 1 Homo sapiens 0-21 16680433-2 2006 N-acetyltransferase 1 (NAT1) participates in the catabolism of folates and the acetylation of aromatic and heterocyclic amines. Folic Acid 63-70 N-acetyltransferase 1 Homo sapiens 23-27 16680433-3 2006 Hence, functional polymorphisms in NAT1, the gene encoding NAT1, could influence the risk of spina bifida via either folate catabolism or acetylation of exogenous agents. Folic Acid 117-123 N-acetyltransferase 1 Homo sapiens 35-39 16680433-3 2006 Hence, functional polymorphisms in NAT1, the gene encoding NAT1, could influence the risk of spina bifida via either folate catabolism or acetylation of exogenous agents. Folic Acid 117-123 N-acetyltransferase 1 Homo sapiens 59-63 16680433-10 2006 These associations may be attributable to a decrease in either folate catabolism or the conversion of exogenous agents to teratogenic derivatives in women and/or developing embryos with a NAT1 genotype that includes a loss of function allele relative to those who do not. Folic Acid 63-69 N-acetyltransferase 1 Homo sapiens 188-192 15523664-2 2004 We investigated whether polymorphic variants of fetal acetyl-N-transferase 1 (NAT1), an enzyme involved in the catabolism of folates, differentially interacted with maternal multivitamin use during early pregnancy to alter the risk of delivering an infant with an orofacial cleft malformation. Folic Acid 125-132 N-acetyltransferase 1 Homo sapiens 78-82 15959877-2 2005 N-acetyltransferase 1 is involved in acetylation of aromatic and heterocyclic amines and the catabolism of folates. Folic Acid 107-114 N-acetyltransferase 1 Homo sapiens 0-21 15142281-3 2004 In addition to its xenobiotic-metabolising capacity, human arylamine N-acetyltransferase type-1 (NAT1) acetylates the folate catabolite para-aminobenzoylglutamate and is implicated in folate metabolism. Folic Acid 118-124 N-acetyltransferase 1 Homo sapiens 97-101 15142281-3 2004 In addition to its xenobiotic-metabolising capacity, human arylamine N-acetyltransferase type-1 (NAT1) acetylates the folate catabolite para-aminobenzoylglutamate and is implicated in folate metabolism. Folic Acid 184-190 N-acetyltransferase 1 Homo sapiens 97-101 11005799-11 2000 Human NAT1 and its murine equivalent specifically acetylate the folate catabolite p-aminobenzoylglutamate. Folic Acid 64-70 N-acetyltransferase 1 Homo sapiens 6-10 12946272-1 2003 Human N -acetyltransferase Type I (NAT1) catalyses the acetylation of many aromatic amine and hydrazine compounds and it has been implicated in the catabolism of folic acid. Folic Acid 162-172 N-acetyltransferase 1 Homo sapiens 35-39 7598738-0 1995 Purification of recombinant human N-acetyltransferase type 1 (NAT1) expressed in E. coli and characterization of its potential role in folate metabolism. Folic Acid 135-141 N-acetyltransferase 1 Homo sapiens 34-60 10449187-4 1999 Mouse NAT2 and human NAT1 have a widespread tissue distribution and the folate catabolite p-aminobenzoylglutamate (pAB-Glu) has been proposed as a candidate endogenous substrate. Folic Acid 72-78 N-acetyltransferase 1 Homo sapiens 21-25 10767335-8 2000 In view of the role of folate in protecting against neural tube defects, we propose that NAT1 is a candidate risk factor for susceptibility to neural tube defects. Folic Acid 23-29 N-acetyltransferase 1 Homo sapiens 89-93 9839355-2 1998 The discovery that human NAT1 acts upon p-aminobenzoylgluatamate (p-ABG) to generate p-acetamidobenzoylglutamate (p-AABG), a major urinary metabolite of folic acid, suggests that human NAT1 may play a role in folic acid metabolism and hence in the normal development of the neural tube. Folic Acid 153-163 N-acetyltransferase 1 Homo sapiens 25-29 9839355-2 1998 The discovery that human NAT1 acts upon p-aminobenzoylgluatamate (p-ABG) to generate p-acetamidobenzoylglutamate (p-AABG), a major urinary metabolite of folic acid, suggests that human NAT1 may play a role in folic acid metabolism and hence in the normal development of the neural tube. Folic Acid 153-163 N-acetyltransferase 1 Homo sapiens 185-189 9839355-2 1998 The discovery that human NAT1 acts upon p-aminobenzoylgluatamate (p-ABG) to generate p-acetamidobenzoylglutamate (p-AABG), a major urinary metabolite of folic acid, suggests that human NAT1 may play a role in folic acid metabolism and hence in the normal development of the neural tube. Folic Acid 209-219 N-acetyltransferase 1 Homo sapiens 25-29 7598738-0 1995 Purification of recombinant human N-acetyltransferase type 1 (NAT1) expressed in E. coli and characterization of its potential role in folate metabolism. Folic Acid 135-141 N-acetyltransferase 1 Homo sapiens 62-66 7598738-6 1995 The pteroate moiety of folate, in contrast is a poor inhibitor, with 100 microM pteroate inhibiting only 40% of NAT1 activity. Folic Acid 23-29 N-acetyltransferase 1 Homo sapiens 112-116 7598738-7 1995 A catabolite of folate para-aminobenzoly-L-glutamate has also been shown to be a NAT1 substrate with a Km value of 263 microM. Folic Acid 16-22 N-acetyltransferase 1 Homo sapiens 81-85 24823794-0 2014 From arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN)NAT1 and its homologue (MOUSE)NAT2. Folic Acid 87-97 N-acetyltransferase 1 Homo sapiens 124-128 26309907-2 2015 Recently, studies report that human NAT1 and mouse Nat2 hydrolyze acetyl-coenzyme A (AcCoA) into acetate and coenzyme A in a folate-dependent fashion, a previously unknown function. Folic Acid 125-131 N-acetyltransferase 1 Homo sapiens 36-40 26309907-3 2015 In this study, our goal was to confirm these findings and determine the apparent Michaelis-Menten kinetic constants (Vmax and Km) of the folate-dependent AcCoA hydrolysis for human NAT1/NAT2, and the rodent analogs rat Nat1/Nat2, mouse Nat1/Nat2, and hamster Nat1/Nat2. Folic Acid 137-143 N-acetyltransferase 1 Homo sapiens 181-185 26309907-3 2015 In this study, our goal was to confirm these findings and determine the apparent Michaelis-Menten kinetic constants (Vmax and Km) of the folate-dependent AcCoA hydrolysis for human NAT1/NAT2, and the rodent analogs rat Nat1/Nat2, mouse Nat1/Nat2, and hamster Nat1/Nat2. Folic Acid 137-143 N-acetyltransferase 1 Homo sapiens 236-240 26309907-5 2015 Human NAT1 and its rodent analogs rat Nat2, mouse Nat2 and hamster Nat2 catalyzed AcCoA hydrolysis in a folate-dependent manner. Folic Acid 104-110 N-acetyltransferase 1 Homo sapiens 6-10 24467436-8 2014 Human NAT1 is strongly expressed in oestrogen receptor-positive breast cancer and may contribute to folate and acetyl CoA homeostasis. Folic Acid 100-106 N-acetyltransferase 1 Homo sapiens 6-10 32555504-1 2020 Human arylamine N-acetyltransferase 1 (NAT1), present in all tissues, is classically described as a phase-II xenobiotic metabolizing enzyme but can also catalyze the hydrolysis of acetyl-Coenzyme A (acetyl-CoA) in the absence of an arylamine substrate using folate as a cofactor. Folic Acid 258-264 N-acetyltransferase 1 Homo sapiens 6-37 32555504-1 2020 Human arylamine N-acetyltransferase 1 (NAT1), present in all tissues, is classically described as a phase-II xenobiotic metabolizing enzyme but can also catalyze the hydrolysis of acetyl-Coenzyme A (acetyl-CoA) in the absence of an arylamine substrate using folate as a cofactor. Folic Acid 258-264 N-acetyltransferase 1 Homo sapiens 39-43