Molecular genetics of human polymorphic N-acetyltransferase: enzymatic analysis of 15 recombinant wild-type, mutant, and chimeric NAT2 allozymes.

doi:10.1093/hmg/3.5.729

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Article

Molecular genetics of human polymorphic N-acetyltransferase: enzymatic analysis of 15 recombinant wild-type, mutant, and chimeric NAT2 allozymes.

Human molecular genetics - 1 May 1994

Hein D W, Ferguson R J, Doll M A, Rustan T D, Gray K

Abstract excerpt

Human polymorphic N-acetyltransferase (NAT2) catalyzes the N-acetylation of arylamine drugs and carcinogens. Human acetylator phenotype is regulated at the NAT2 locus and has been associated with differential risk to certain drug toxicities or cancer. We examined arylamine substrate and acetyl coenzyme A cofactor affinities, and the N-acetyltransferase catalytic activities of the wild-type and 14 different mutant...

Topics

Acetyl Coenzyme A
Acetylation
Alleles
Aminophenols
Arylamine N-Acetyltransferase
Base Sequence
Cloning, Molecular
Colon
Escherichia coli
Fluorenes
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Molecular Sequence Data

Phenotype

Point Mutation

Polymorphism, Genetic

Protein Denaturation

Recombinant Fusion Proteins

Source

Open in PubMed

Identifiers

PMID: 8081359
DOI: 10.1093/hmg/3.5.729

Genes

NAT2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8081359-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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