Molecular characterisation of a human aryl sulfotransferase cDNA.

Article Details

Citation

Zhu X, Veronese ME, Sansom LN, McManus ME

Molecular characterisation of a human aryl sulfotransferase cDNA.

Biochem Biophys Res Commun. 1993 Apr 30;192(2):671-6.

PubMed ID
8484775 [ View in PubMed
]
Abstract

A full-length aryl sulfotransferase cDNA was isolated from a human liver cDNA library. It was 1155 bp long containing a coding region of 885 basepairs encoding a cytosolic protein (M(r) 34178 Da) of 295 amino acids. This human cDNA shared 80% homology to the rat aryl sulfotransferase cDNA, 58% to the bovine and rat oestrogen sulfotransferase cDNAs, 53% to the rat hydroxysteroid sulfotransferase cDNA and 51% to the human liver dehydroepiandrosterone sulfotransferase cDNA over its whole 885 bp coding region. The deduced amino acid sequence of this human cDNA was 79% homologous to that of the rat aryl sulfotransferase cDNA and the putative common-substrate binding site motif GXXGXXK of the sulfotransferases has been conserved in this human amino acid sequence. At least two sizes of this human aryl sulfotransferase mRNA were detected in the human liver and lung.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Sulfotransferase 1A1P50225Details