Xenobiotic microsomal epoxide hydrolase: 5′ sequence of the human gene

Neil M. Wilson, Curtis John Omiecinski

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

A cDNA for human microsomal epoxide hydrolase (mEH) was used to isolate genomic clones representing the 5′ portion of the corresponding human gene. A total of 1034 bases of mEH gene sequence were obtained that included exon 1 and 5′ flanking information. In contrast to the structure reported for the rat mEH gene (Falany et al. (1987) J. Biol. Chem. 262, 5924-5930), the human mEH gene lacked at CAAT box, but did contain a high-affinity CTF binding site at position -278 and an SV40 core enhancer element at position -525. TATA boxes were identified at positions -32 and -29 for the human and rat genes, respectively. Sequence comparisons between 5′ flanking regions of the human and rat mEH genes demonstrated 47% homology, considerably less than the 83% conservation observed in the cDNA coding areas. Primer extension experiments localized the transcription initiation site of the human gene to a position 116 bases 5′ from the analogous site in the rat mEH gene.

Original languageEnglish (US)
Pages (from-to)357-358
Number of pages2
JournalBBA - Gene Structure and Expression
Volume1008
Issue number3
DOIs
StatePublished - Aug 14 1989

Fingerprint

Epoxide Hydrolases
Xenobiotics
Genes
Rats
Complementary DNA
TATA Box
5' Flanking Region
Transcription Initiation Site
Exons
Conservation
Clone Cells
Binding Sites

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

Cite this

Wilson, Neil M. ; Omiecinski, Curtis John. / Xenobiotic microsomal epoxide hydrolase : 5′ sequence of the human gene. In: BBA - Gene Structure and Expression. 1989 ; Vol. 1008, No. 3. pp. 357-358.
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Xenobiotic microsomal epoxide hydrolase : 5′ sequence of the human gene. / Wilson, Neil M.; Omiecinski, Curtis John.

In: BBA - Gene Structure and Expression, Vol. 1008, No. 3, 14.08.1989, p. 357-358.

Research output: Contribution to journalArticle

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