Mouse steroid sulfotransferases: substrate specificity and preliminary X-ray crystallographic analysis.
Biochem Pharmacol
; 55(3): 313-7, 1998 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-9484797
ABSTRACT
Three mouse cytosolic sulfotransferases were expressed in Escherichia coli cells in order to study their substrate specificities toward natural as well as synthetic steroid hormones. The Km and Vmax values confirmed the high substrate specificity of estrogen and hydroxysteroid sulfotransferases toward estradiol and dehydroepiandrosterone, respectively. In sharp contrast, the synthetic estrogen diethylstilbestrol was metabolized efficiently by both enzymes to its disulfate ester. These sulfotransferases display highly stereospecific sulfotransferase activity for sulfating only the trans-isomer of diethylstilbestrol. Crystals suitable for high-resolution structure determination of estrogen sulfotransferase were grown with polyethylene glycol. The crystals belong to the orthorhombic space group P2(1)2(1)2, and diffracted to 2.5 A.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Sulfotransferases
Limite:
Animals
Idioma:
En
Ano de publicação:
1998
Tipo de documento:
Article