EC 126.96.36.199 - Adenylyl-sulfate kinase
IntEnz Enzyme Nomenclature
adenosine 5'-phosphosulfate kinase
adenosine phosphosulfate kinase
adenylylsulfate kinase (phosphorylating)
24152 [IUBMB]adenosine 5'-phosphosulfateadenosine 5'-phosphosulfateName origin: UniProt - CHECKED (C)Formula: C10H12N5O10PS
Charge: -2ChEBI compound status: CHECKED (C)ATPATPName origin: UniProt - CHECKED (C)Formula: C10H12N5O13P3
Charge: -4ChEBI compound status: CHECKED (C)<?>3'-phosphoadenylyl sulfate3'-phosphoadenylyl sulfateName origin: UniProt - CHECKED (C)Formula: C10H11N5O13P2S
Charge: -4ChEBI compound status: CHECKED (C)ADPADPName origin: UniProt - CHECKED (C)Formula: C10H12N5O10P2
Charge: -3ChEBI compound status: CHECKED (C)
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 188.8.131.52) and adenylyl-sulfate kinase (EC 184.108.40.206).
Links to other databases
The mechanism of "active sulfate" formation.J. Am. Chem. Soc. 78: 6408-6409 (1956).
Isolation and identification of active sulfate.J. Biol. Chem. 229: 837-851 (1957). [PMID: 13502346]
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 220.127.116.11 created 1961, modified 1999]