Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1gene.[1][2][3]
Three-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS) is the sulfate donor cosubstrate for all sulfotransferase (SULT) enzymes (Xu et al., 2000). SULTs catalyze the sulfate conjugation of many endogenous and exogenous compounds, including drugs and other xenobiotics. In humans, PAPS is synthesized from adenosine 5-prime triphosphate (ATP) and inorganic sulfate by 2 isoforms, PAPSS1 and PAPSS2 (MIM 603005).[supplied by OMIM][3]
References
↑Girard JP, Baekkevold ES, Amalric F (May 1998). "Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase". FASEB J. 12 (7): 603–12. PMID9576487.
↑ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH (Oct 1998). "Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse". Nat Genet. 20 (2): 157–62. doi:10.1038/2458. PMID9771708.
Yanagisawa K, Sakakibara Y, Suiko M, et al. (1998). "cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme". Biosci. Biotechnol. Biochem. 62 (5): 1037–40. doi:10.1271/bbb.62.1037. PMID9648242.
Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. doi:10.1074/jbc.273.30.19311. PMID9668121.
Venkatachalam KV, Fuda H, Koonin EV, Strott CA (1999). "Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase". J. Biol. Chem. 274 (5): 2601–4. doi:10.1074/jbc.274.5.2601. PMID9915785.
Besset S, Vincourt JB, Amalric F, Girard JP (2000). "Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells". FASEB J. 14 (2): 345–54. PMID10657990.
Harjes S, Scheidig A, Bayer P (2004). "Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1". Acta Crystallogr. D. 60 (Pt 2): 350–2. doi:10.1107/S0907444903027628. PMID14747722.
Lansdon EB, Fisher AJ, Segel IH (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains". Biochemistry. 43 (14): 4356–65. doi:10.1021/bi049827m. PMID15065880.
Harjes S, Bayer P, Scheidig AJ (2005). "The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding". J. Mol. Biol. 347 (3): 623–35. doi:10.1016/j.jmb.2005.01.005. PMID15755455.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID16169070.
Sekulic N, Konrad M, Lavie A (2007). "Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 and its ramifications for enzyme regulation". J. Biol. Chem. 282 (30): 22112–21. doi:10.1074/jbc.M701713200. PMID17540769.