The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: sulfate adenylyltransferase
Reaction: ATP + sulfate = diphosphate + adenylyl sulfate
Other name(s): ATP-sulfurylase; adenosine-5′-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; ATP-sulfurylase; sulfurylase
Systematic name: ATP:sulfate adenylyltransferase
Comments: The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5′-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC and adenylyl-sulfate kinase (EC
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-39-9
1.  Bandurski, R.S., Wilson, L.G., Squires, C.L. The mechanism of "active sulfate" formation. J. Am. Chem. Soc. 78 (1956) 6408–6409.
2.  Hilz, H. and Lipmann, F. The enzymatic activation of sulfate. Proc. Natl. Acad. Sci. USA 41 (1955) 880–890. [DOI] [PMID: 16589765]
3.  Venkatachalam, K.V., Akita, H., Strott, C. Molecular cloning, expression and characterization of human bifunctional 3′-phosphoadenosine-5′-phosphosulfate synthase and its functional domains. J. Biol. Chem. 273 (1998) 19311–19320. [DOI] [PMID: 9668121]
[EC created 1961, modified 1999]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald