3′-Phosphoadenosine 5′-Phosphosulfate (PAPS) Synthases, Naturally Fragile Enzymes Specifically Stabilized by Nucleotide Binding
نویسندگان
چکیده
منابع مشابه
3′-Phosphoadenosine 5′-Phosphosulfate (PAPS) Synthases, Naturally Fragile Enzymes Specifically Stabilized by Nucleotide Binding*
Activated sulfate in the form of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) is needed for all sulfation reactions in eukaryotes with implications for the build-up of extracellular matrices, retroviral infection, protein modification, and steroid metabolism. In metazoans, PAPS is produced by bifunctional PAPS synthases (PAPSS). A major question in the field is why two human protein isoforms, P...
متن کاملSynthesis of 3'-phosphoadenosine-5'-phosphosulfate (PAPS) increases during corneal development.
متن کامل
Sulfation and sulfotransferases 5: the importance of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) in the regulation of sulfation.
Sulfation is the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to a substrate that is catalyzed by a family of sulfotransferase enzymes. Many different endogenous and xenobiotic molecules are substrates for the sulfotransferases; sulfation affects many different physiological processes, including: 1) deactivation and bioactivation of xenobiotics, 2) inactivation ...
متن کامل3′-Phosphoadenosine 5′-Phosphosulfate Allosterically Regulates Sulfotransferase Turnover
Human cytosolic sulfotransferases (SULTs) regulate the activities of thousands of small molecules-metabolites, drugs, and other xenobiotics-via the transfer of the sulfuryl moiety (-SO3) from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the hydroxyls and primary amines of acceptors. SULT1A1 is the most abundant SULT in liver and has the broadest substrate spectrum of any SULT. Here we presen...
متن کاملDefect in 3'-phosphoadenosine 5'-phosphosulfate formation in brachymorphic mice.
Incorporation of 35SO42- into adenosine 5'-phosphosulfate (APS), 3'-phosphoadenosine 5'-phosphosulfate (PAPS), and chondroitin sulfate was simultaneously assessed with extracts prepared from epiphyseal cartilage of neonatal normal or homozygous brachymorphic mice. Radioactivity measured in APS, PAPS, and chondroitin sulfate of extracts from brachymorphic cartilage was approximately 300%, 9%, an...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2012
ISSN: 0021-9258
DOI: 10.1074/jbc.m111.325498