Functional effects of single nucleotide polymorphisms in the coding region of human N-acetyltransferase 1

Pharmacogenomics J. 2008 Oct;8(5):339-48. doi: 10.1038/sj.tpj.6500483. Epub 2007 Oct 2.

Abstract

Genetic variants of human N-acetyltransferase 1 (NAT1) are associated with cancer and birth defects. N- and O-acetyltransferase catalytic activities, Michaelis-Menten kinetic constants (K(m) and V(max)) and steady-state expression levels of NAT1-specific mRNA and protein were determined for the reference NAT1*4 and variant human NAT1 haplotypes possessing single nucleotide polymorphisms (SNPs) in the open reading frame. Although none of the SNPs caused a significant effect on steady-state levels of NAT1-specific mRNA, C97T(R33stop), C190T(R64W), C559T (R187stop) and A752T(D251V) each reduced NAT1 protein level and/or N- and O-acetyltransferase catalytic activities to levels below detection. G560A(R187Q) substantially reduced NAT1 protein level and catalytic activities and increased substrate K(m). The G445A(V149I), G459A(synonymous) and T640G(S214A) haplotype present in NAT1*11 significantly (P<0.05) increased NAT1 protein level and catalytic activity. Neither T21G(synonymous), T402C(synonymous), A613G(M205V), T777C(synonymous), G781A(E261K) nor A787G(I263V) significantly affected K(m), catalytic activity, mRNA or protein level. These results suggest heterogeneity among slow NAT1 acetylator phenotypes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Substitution
  • Arylamine N-Acetyltransferase / chemistry
  • Arylamine N-Acetyltransferase / genetics*
  • Arylamine N-Acetyltransferase / metabolism
  • Biocatalysis
  • Haplotypes
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / genetics*
  • Isoenzymes / metabolism
  • Kinetics
  • Polymorphism, Single Nucleotide*
  • RNA, Messenger / genetics

Substances

  • Isoenzymes
  • RNA, Messenger
  • Arylamine N-Acetyltransferase
  • N-acetyltransferase 1