Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Computational and experimental analyses of mammalian arylamine N-acetyltransferase structure and function.

Drug metabolism and disposition: the biological fate of chemicals - 1 Jun 2007

Walraven Jason M, Trent John O, Hein David W

Abstract excerpt

Arylamine N-acetyltransferases (NATs) play an important role in the metabolism of arylamine and hydrazine drugs and many arylamine procarcinogens. The two human N-acetyltransferases, NAT1 and NAT2, are widely distributed in human tissues and are highly polymorphic. Although many xenobiotic procarcinogens and drugs are known mammalian NAT substrates, it is unclear what physiological roles these enzymes might play,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alphaproteobacteria
Share to Arylamine N-Acetyltransferase

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Protein Structure, Secondary

Share to Pseudomonas aeruginosa

Share to Salmonella typhi

Share to Sequence Homology, Amino Acid

Share to Sulfamethazine

Source

Open in PubMed Open full text

Identifiers

PMID: 17371801
DOI: 10.1124/dmd.107.015040
PMCID: PMC2085365

Genes

NAT2
NAT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computational and experimental analyses of mammalian arylamine N-acetyltransferase structure and function.PMID 17371801Read ↗

Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2.Semantic proximity Read ↗

Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases.Semantic proximity Read ↗

Arylamine N-acetyltransferases: From Structure to FunctionSemantic proximity Read ↗

ArylamineN-acetyltransferasesSemantic proximity Read ↗

Screening and characterizing human NAT2 variants.Semantic proximity Read ↗

Pharmacogenomics of Arylamine N-acetyltransferase.Semantic proximity Read ↗

Human acetyl CoA:arylamine N-acetyltransferase variants generated by random mutagenesis.Semantic proximity Read ↗

Structural Analysis of the Genes for Human Arylamine N-Acetyltransferases and Characterisation of Alternative TranscriptsSemantic proximity Read ↗

Structure-function analyses of single nucleotide polymorphisms in human N-acetyltransferase 1.Semantic proximity Read ↗

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

Functional characterization of human N-acetyltransferase 2 (NAT2) single nucleotide polymorphisms.Semantic proximity Read ↗

Polymorphism of human acetyltransferases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.