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Details on Person Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase

Class:IdLiteratureReference:176485
_displayNameMutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase
_timestamp2006-03-08 20:43:06
author[Person:176666] Fuda, H
[Person:176541] Lee, YC
[Person:176675] Shimizu, C
[Person:176598] Javitt, NB
[Person:158865] Strott, CA
created[InstanceEdit:176534] D'Eustachio, P, 2006-03-08 20:43:01
journalJ Biol Chem
pages36161-6
pubMedIdentifier12145317
titleMutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase
volume277
year2002
(literatureReference)[Reaction:176517] SULTs transfer (SO4)2- group to PREG [Homo sapiens]
[Reaction:176609] cholesterol + PAPS => cholesterol sulfate + PAP [Homo sapiens]
[Summation:176620] The 3-hydroxyl groups of a number of sterols can undergo sul...
[Summation:176625] The sulfonation of pregnenolone (PREG) is catalyzed by both ...
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No pathways have been reviewed or authored by Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase (176485)