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Information on EC 2.7.7.4 - sulfate adenylyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P08536

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.4 sulfate adenylyltransferase
IUBMB 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).
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P08536
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
atps, atp sulfurylase, papss2, atp-sulfurylase, sulfurylase, atp sulphurylase, sulfate adenylyltransferase, atps2, atps1, atp-s, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine 5'-triphosphate sulphurylase
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-
-
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adenosine 5'-triphosphate-sulfurylase
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-
-
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adenosine triphosphate sulphurylase
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-
-
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adenosine-5'-triphosphate sulfurylase
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-
-
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adenosinetriphosphate sulfurylase
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-
-
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adenylylsulfate pyrophosphorylase
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-
-
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adenylyltransferase, sulfate
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-
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ATP sulfurylase
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-
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ATP-sulfurylase
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-
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sulfurylase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
sequential reaction mechanism in which both substrates bind before any product is released
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:sulfate adenylyltransferase
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).
CAS REGISTRY NUMBER
COMMENTARY hide
9012-39-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
r
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
-
-
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r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
additional information
?
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radioisotopic exchange between the adenosine 5'-sulfatophosphate and SO42- occurs only in the presence of either MgATP2- or diphosphate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 5'-phosphosulfate
Cys
-
2 mM, slight
Met
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2 mM, slight
SO42-
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competitive with respect to MoO42-
Sulfide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
ATP
0.17
MoO42-
-
pH 8.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
SO42-
-
pH 8.0, 30°C
3.4
Sulfide
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pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7 - 9
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pH 7.7: about 75% of maximal activity, pH 9.0: about 70% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
470000
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recombinant enzyme, gel filtration
59300
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8 * 59300, SDS-PAGE
60000
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x * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 60000, SDS-PAGE
octamer
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8 * 59300, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of ATP sulfurylase with thiosulfate, ADP and chlorate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATP sulfurylase cDNA from MET3 on chromosome X is amplified and expressed in Escherichia coli XL1-Blue. The synthesis of the enzyme is directed by an expression system that employs the regulatory genes of Vibrio fischeri
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robbins, P.W.; Lipmann, F.
The enzymatic sequence in the biosynthesis of active sulfate
J. Am. Chem. Soc.
78
6409-6410
1956
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Renosto, F.; Martin, R.L.; Wailes, L.M.; Daley, L.A.; Segel, I.H.
Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3-phosphoadenosine-5-phosphosulfate
J. Biol. Chem.
265
10300-10308
1990
Aspergillus nidulans, Saccharomyces cerevisiae, Neurospora crassa, Penicillium chrysogenum, Penicillium duponti, Rattus norvegicus, Spinacia oleracea
Manually annotated by BRENDA team
Hawes, C.S.; Nicholas, D.J.D.
Adenosine 5-triphosphate sulphurylase from Saccharomyces cerevisiae
Biochem. J.
133
541-550
1973
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bicknell, R.; Cullis, P.M.; Jarvest, R.L.; Lowe, G.
The stereochemical course of nucleotidyl transfer catalyzed by ATP sulfurylase
J. Biol. Chem.
257
8922-8927
1982
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Heinzel, M.; Trper, H.G.
Sulfite formation by wine yeasts II. Properties of ATP-sulfurylase.
Arch. Microbiol.
107
293-297
1976
Saccharomyces cerevisiae, Saccharomyces bayanus, Saccharomyces bayanus Sacardo
-
Manually annotated by BRENDA team
Karamohamed, S.; Nilsson, J.; Nourizad, K.; Ronaghi, M.; Pettersson, B.; Nyren, P.
Production, Purification, and Luminometric Analysis of Recombinant Saccharomyces cerevisiae MET3 Adenosine Triphosphate Sulfurylase Expressed in Escherichia coli
Protein Expr. Purif.
15
381-388
1999
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ullrich, T.C.; Huber, R.
The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle
J. Mol. Biol.
313
1117-1125
2001
Saccharomyces cerevisiae (P08536), Saccharomyces cerevisiae
Manually annotated by BRENDA team