Literature DB >> 2924904

Evidence for two closely related isozymes of arylamine N-acetyltransferase in human liver.

D M Grant1, F Lottspeich, U A Meyer.   

Abstract

Acetyl CoA-dependent arylamine N-acetyltransferase (EC 2.3.1.5) is the target of a genetic polymorphism in the metabolism of drugs and carcinogens. N-Acetyltransferase was purified 1000-fold from cytosol of human liver and its identity was verified by amino acid sequence homology of two of its tryptic peptides with published rabbit and chicken N-acetyltransferase sequences. Enzyme activity correlated with the presence of two proteins, NAT-1 and NAT-2, with indistinguishable molecular masses (31 kDa). NAT-1 and NAT-2 could be separated by anion-exchange chromatography and were functionally distinguished by their different apparent affinities for the acceptor amine sulfamethazine (SMZ). Antibodies raised against NAT-1 were able to recognize both isozymes on Western blots.

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Year:  1989        PMID： 2924904     DOI： 10.1016/0014-5793(89)81193-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  11 in total

Review 1.  Detoxification pathways in the liver.

Authors:  D M Grant
Journal:  J Inherit Metab Dis       Date:  1991       Impact factor: 4.982

2.  N-acetyltransferase 2 genotype in colorectal cancer and selective gene retention in cancers with chromosome 8p deletions.

Authors:  A L Hubbard; D J Harrison; C Moyes; A H Wyllie; C Cunningham; E Mannion; C A Smith
Journal:  Gut       Date:  1997-08       Impact factor: 23.059

3.  Acetylation pharmacogenetics. The slow acetylator phenotype is caused by decreased or absent arylamine N-acetyltransferase in human liver.

Authors:  D M Grant; K Mörike; M Eichelbaum; U A Meyer
Journal:  J Clin Invest       Date:  1990-03       Impact factor: 14.808

4.  Nucleotide sequence of an intronless gene for a human arylamine N-acetyltransferase related to polymorphic drug acetylation.

Authors:  D M Grant; M Blum; A Demierre; U A Meyer
Journal:  Nucleic Acids Res       Date:  1989-05-25       Impact factor: 16.971

5.  Identification of amino acids imparting acceptor substrate selectivity to human arylamine acetyltransferases NAT1 and NAT2.

Authors:  G H Goodfellow; J M Dupret; D M Grant
Journal:  Biochem J       Date:  2000-05-15       Impact factor: 3.857

6.  Molecular mechanism of slow acetylation of drugs and carcinogens in humans.

Authors:  M Blum; A Demierre; D M Grant; M Heim; U A Meyer
Journal:  Proc Natl Acad Sci U S A       Date:  1991-06-15       Impact factor: 11.205

7.  N-acetylation pharmacogenetics: a gene deletion causes absence of arylamine N-acetyltransferase in liver of slow acetylator rabbits.

Authors:  M Blum; D M Grant; A Demierre; U A Meyer
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

8.  Polymorphic acetylation: lack of influence of rheumatic disease activity and concomitant drug administration.

Authors:  C Astbury; C Beyeler; H A Bird
Journal:  Rheumatol Int       Date:  1995       Impact factor: 2.631

9.  Metabolic activation of aromatic and heterocyclic N-hydroxyarylamines by wild-type and mutant recombinant human NAT1 and NAT2 acetyltransferases.

Authors:  D W Hein; T D Rustan; R J Ferguson; M A Doll; K Gray
Journal:  Arch Toxicol       Date:  1994       Impact factor: 5.153

10.  Arylamine N-acetyltransferase activity in human cultured cell lines.

Authors:  E Coroneos; E Sim
Journal:  Biochem J       Date:  1993-09-01       Impact factor: 3.857
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