EC 2.7.7.4 - Sulfate adenylyltransferase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 2.7.7.4

Names

Accepted name:
sulfate adenylyltransferase
Other names:
ATP sulfurylase
ATP-sulfurylase
adenosine-5'-triphosphate sulfurylase
adenosinetriphosphate sulfurylase
adenylylsulfate pyrophosphorylase
sulfurylase
sulfate adenylate transferase
Systematic name:
ATP:sulfate adenylyltransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004781
CAS Registry Number: 9012-39-9
UniProtKB/Swiss-Prot: (457) [show] [UniProt]

References

  1. Bandurski, R.S., Wilson, L.G. and Squires, C.L.
    The mechanism of "active sulfate" formation.
    J. Am. Chem. Soc. 78: 6408-6409 (1956).
  2. Hilz, H. and Lipmann, F.
    The enzymatic activation of sulfate.
    Proc. Natl. Acad. Sci. USA 41: 880-890 (1955). [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: 19311-19320 (1998). [PMID: 9668121]

[EC 2.7.7.4 created 1961, modified 1999]