| EC |
2.7.7.4 |
| 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 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., 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] |
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| [EC 2.7.7.4 created 1961, modified 1999] |
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