Reaction: ATP + sulfate = diphosphate + adenylyl sulfate
Glossary: 3'-phosphoadenylyl sulfate = PAPS
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 (PAPSS) 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 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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-39-9
References:
1. Bandurski, R.S., Wilson, L.G. and 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.
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. [PMID: 9668121]