A Nucleotide-Gated Molecular Pore Selects Sulfotransferase Substrates

Human SULT2A1 is one of two predominant sulfotransferases in liver and catalyzes transfer of the sulfuryl moiety (−SO3) from activated sulfate (PAPS, 3′-phosphoadenosine 5-phosphosulfate) to hundreds of acceptors (metabolites and xenobiotics). Sulfation recodes the biologic activity of acceptors by...

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Veröffentlicht in:	Biochemistry (Easton) 2012-07, Vol.51 (28), p.5674-5683
Hauptverfasser:	Cook, Ian, Wang, Ting, Falany, Charles N, Leyh, Thomas S
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites bioactive properties Bone Density Conservation Agents - chemistry Computer Simulation crystal structure Dehydroepiandrosterone - chemistry humans isomerization Kinetics liver metabolites Molecular Docking Simulation molecular models osteoporosis Phosphoadenosine Phosphosulfate - chemistry prasterone prediction Protein Binding Raloxifene Hydrochloride - chemistry Recombinant Proteins - chemistry sieves sieving Substrate Specificity sulfates sulfotransferases Sulfotransferases - chemistry xenobiotics
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