Molecular Characterization of a Human Aryl Sulfotransferase cDNA

• Published in: Biochemical and biophysical research communications Vol. 192; no. 2; pp. 671 - 676
• Main Authors: Zhu, X.Y., Veronese, M.E., Sansom, L.N., Mcmanus, M.E.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 30.04.1993; Elsevier
• Subjects: Amino Acid Sequence; Animals; Arylsulfotransferase - genetics; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA - chemistry; DNA - genetics; Fundamental and applied biological sciences. Psychology; Genes. Genome; Humans; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; RNA, Messenger - metabolism; Sequence Homology, Amino Acid; Human; Arylsulfotransferase; Complementary DNA; Nucleotide sequence; Enzyme; Liver
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1993.1467

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 (Mr 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.