Genotyping test of Arylamine N-acetyltransferase (NAT) Genes for oral mucosa as samples.

NAT 2 ( N - acetyltransferase 2 ( arylamine N - acetyltransferase ) )

NAT 1 ( N - acetyltransferase 1 ( arylamine N - acetyltransferase ) )

The human NAT1 gene has nine exons. The coding region is located in exon 9 and spans 870 bp. Diverse NAT1 transcripts have been reported and two promoters exist. The first promoter, designated as P1 is located in the 5' flanking region of exon 1 and controls two major (a1 and a2) transcripts. The second promoter is located upstream of exon 4 and give rise to at least five (b1 to b5) different t...

Arylamine N-acetyltransferase.

304 3.5. Namboodiri. kl. A. A,. Nakai. C‘. k Klein, 1). C. (1070) J. Ncurochem. 33. 807-810 30. Klein. 1). C’. k Namboodiri, M. A. A. (1082) Trends Biochem. Sci. 7, OXI02 37. Namboodiri, M. A. A,, Weller, J. I , . Kc Klein, I). C’. (1080) J. l k l . Cheni. 255. 6032-0035 38. Namboodiri, M. A. A,. Weller, J. I, . K: Klein, I). C’. ( 1080) Hiochem. Hiophys. Kes. C’ommun. 96, 1 8%1 05 30 . Niimboo...

A long-lived luminescent probe to sensitively detect arylamine N-acetyltransferase (NAT) activity of cells.

Arylamine N-acetyltransferase (NAT) is an important phase II metabolizing enzyme that influences drug efficacy and adverse effects. Here, we report a long-lived luminescent lanthanide complex as a probe for NAT, employing an intraligand photoinduced electron transfer strategy. The probe shows approximately 100-fold increase of luminescence upon N-acetylation catalyzed by NAT, with relatively hi...

Evidence for arylamine N-acetyltransferase activity in Klebsiella pneumoniae.

Arylamine N-acetyltransferase (NAT) enzymes have been found in laboratory animals, humans, microorganisms (fungi, bacteria and parasites), and in plants. But the characteristics of NAT from Klebsiella pneumoniae are not clear. NAT activities with p-aminobenzoic acid (PABA) and 2-aminofluorene (AF) as substrates were examined in the cytosol of K. pneumoniae. NAT activity (N-acetylation of substr...