On the nature of rat hepatic and mouse olfactory sulfotransferases

Michio Matsui, Hiro omi Tamura, Fusako Nagai, Hiroshi Homma, Atsushi Miyawaki, Katsuhiko Mikoshiba

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


Rat hydroxysteroid sulfotransferase (HS-SULT) cDNAs, ST-40 and ST-20 are 90% identical in amino acid sequences and show different substrate specificities toward dehydroepiandrosterone (DHEA), androsterone (AD) and cortisol (CS). ST-40 enzyme is active toward the three substrates, whereas ST-20 enzyme is preferentially active for CS. First we prepared mutants of well conserved histidine, lysine and asparagine by site-directed mutagenesis. Secondly we constructed 20 chimeric HS-SULTs by reciprocal exchange of five protein domains between ST-20 and ST-40 enzymes. The studies on the expressed mutant and chimetic enzymes indicate the importance of the C-terminal region for the substrate specificity and the involvement of multiple regions for the enzyme activities. Next we determined the genetic loci of ST-40 and ST-20 by fluorescence in situ hybridization. Biotinylated ST-20 and ST-40 probes gave a pair of fluorescent spots on the same region of rat chromosome 1 and the loci of these genes were localized to the same chromosomal region of 1q21.3→q22.1. Finally we studied mouse olfactory phenol SULT (P-SULT). It was immunolocalized in the cytoplasm of mouse olfactory sustentacular cells and mouse nasal cytosols show high SULT activities toward phenolic aromatic odorants. We subsequently isolated a mouse P-SULT cDNA from mouse olfactory cDNA library. It encodes 304 amino acid polypeptide and is 94% identical with rat STlC1 in amino acid sequences.

Original languageEnglish
Pages (from-to)69-80
Number of pages12
JournalChemico-Biological Interactions
Issue number1-3
Publication statusPublished - 1998 Feb 20


  • Dehydroepiandrosterone
  • Enzymes
  • Sulfotransferase

ASJC Scopus subject areas

  • Toxicology


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