Reaction: ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
Glossary: 3'-phosphoadenylyl sulfate = PAPS
Other name(s): adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5'-phosphosulfate-3'-phosphokinase; APS kinase
Systematic name: ATP:adenylyl-sulfate 3'-phosphotransferase
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, KEGG, Metacyc, PDB, CAS registry number: 9012-38-8
References:
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. Robbins, P.W., Lipmann, F. Isolation and identification of active sulfate. J. Biol. Chem. 229 (1957) 837-851.
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]