The Enzyme Database

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Accepted name: adenylyl-sulfate kinase
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 (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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-38-8
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. [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 (1998) 19311–19320. [PMID: 9668121]
[EC created 1961, modified 1999]

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