| First Author | Tamura H | Year | 1999 |
| Journal | Biol Pharm Bull | Volume | 22 |
| Issue | 3 | Pages | 234-9 |
| PubMed ID | 10220276 | Mgi Jnum | J:54249 |
| Mgi Id | MGI:1334850 | Doi | 10.1248/bpb.22.234 |
| Citation | Tamura H, et al. (1999) Molecular cloning, expression and characterization of a phenol sulfotransferase cDNA from mouse intestine. Biol Pharm Bull 22(3):234-9 |
| abstractText | A sulfotransferase (ST) cDNA was isolated from a mouse intestinal cDNA library using a probe which was generated by reverse transcription (RT)-PCR based on the conserved amino acid sequences of the ST molecules. The isolated cDNA (1.1 kb) contained an 858 bp open reading frame encoding a 286 amino acid polypeptide with molecular weight of 33439. The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively. RT-PCR analyses showed abundant expression of the P-ST mRNA in the intestine as well as in the liver in the mouse tissues examined (brain, heart, intestine, kidney, liver and lung) of both sexes. E. coli-expressed enzyme is capable of catalyzing the sulfation of 2-naphthol at Km = 3.3 microM and Vmax = 3.33 nmol/min/mg protein and also showed sulfation activity for L-3,4-dihydroxyphenylalanine (L-DOPA) and dopamine. Among food constituents tested, tannic acid and epigallocatechin gallate strongly inhibited the P-ST activity in vitro. |
