EC - Adenylyl-sulfate kinase

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IntEnz Enzyme Nomenclature


Accepted name:
adenylyl-sulfate kinase
Other names:
5'-phosphoadenosine sulfate kinase
APS kinase
adenosine 5'-phosphosulfate kinase
adenosine phosphosulfate kinase
adenosine phosphosulfokinase
adenylylsulfate kinase (phosphorylating)
Systematic name:
ATP:adenylyl-sulfate 3'-phosphotransferase



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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004020
CAS Registry Number: 9012-38-8
UniProtKB/Swiss-Prot: (155) [show] [UniProt]


  1. Bandurski, R.S., Wilson, L.G., Squires, C.L.
    The mechanism of "active sulfate" formation.
    J. Am. Chem. Soc. 78 : 6408-6409 (1956).
  2. Robbins, P.W., Lipmann, F.
    Isolation and identification of active sulfate.
    J. Biol. Chem. 229 : 837-851 (1957). [PMID: 13502346]
  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 created 1961, modified 1999]