Linked Life Data

8033246

Source:http://linkedlifedata.com/resource/pubmed/id/8033246

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1994-8-12
pubmed:abstractText
In the present study, four new forms of aryl sulfotransferase cDNAs have been isolated and their structures determined. A compilation of primary structures of 16 different sulfotransferases, including enzymes metabolizing endogenous chemicals and xenobiotics, showed a considerable extent of similarity among bacterial, plant and mammalian species, and indicates that these enzymes constitute a supergene family. Aryl sulfotransferase and estrogen sulfotransferase are shown to belong to a single gene family (ST1) which consists of at least four subfamilies, whereas, based on the sequence similarity, hydroxysteroid sulfotransferases constitute a distinct family (ST2). Little or no clear similarity was observed between the primary structures of enzymes N-sulfating aminosugars and those sulfating hydrophobic chemicals such as phenols, alcohols or amines, indicating that both types of enzymes diverged early in their evolutionary history. Two regions in the C-terminal parts are, however, conserved among all enzymes examined, which suggests a possibly essential role of these sites for the binding of a PAPS cofactor or for sulfate transfer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0009-2797
pubmed:author
pubmed:issnType
Print
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Structural similarity and diversity of sulfotransferases.
pubmed:affiliation
Department of Pharmacology, School of Medicine, Keio University, Tokyo, Japan.
pubmed:publicationType
Journal Article