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EC Tree
IUBMB 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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
The taxonomic range for the selected organisms is: Penicillium chrysogenum The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aps kinase, papss1, aps-kinase, paps synthetase, papss, paps synthase, adenosine-5'-phosphosulfate kinase, mxan3487, adenosine 5'-phosphosulfate kinase, adenylylsulfate kinase,
more
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3'-phosphoadenosine-5'-phosphosulfate synthetase
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5'-phosphoadenosine sulfate kinase
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adenosine 5'-phosphosulfate kinase
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adenosine phosphosulfate kinase
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adenosine phosphosulfokinase
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adenosine-5'-phosphosulfate 3'-phosphotransferase
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adenosine-5'-phosphosulfate-3'-phosphokinase
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adenosine-5'phosphosulfate kinase
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adenylylsulfate 3'-phosphotransferase
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adenylylsulfate kinase
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ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
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kinase, adenylylsulfate (phosphorylating)
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ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
enzyme follows a compulsory ordered mechanism in which MgATP2- binds before APS, and PAPS leaves before MgADP-
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
mechanism
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phospho group transfer
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ATP:adenylyl-sulfate 3'-phosphotransferase
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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
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ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
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r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
ATP + adenylyl sulfate
ADP + 3'-phosphoadenylyl sulfate
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r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
?
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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no substrate-chanelling of adenosine 5'-phosphosulfate between ATP-sulfurylase, EC 2.7.7.4, and APS-kinase, i.e. ATP-sulfurylase-APS-complex is no substrate for the kinase
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
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ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
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ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
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ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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i.e. adenylylsulfate or APS
i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate
r
ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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second step in pathway of assimilation of inorganic sulfate
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ATP + adenosine 5-phosphosulfate
ADP + 3'-phosphoadenosine 5'-phosphosulfate
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second step in pathway of assimilation of inorganic sulfate
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Co2+
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5 mM, 58% of activation with Mg2+ or Mn2+
Mn2+
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5 mM yield the same reaction velocity as 5 mM Mg2+, excess inhibits slightly
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adenosine 5'-phosphosulfate
adenosine 5'-phosphosulfate can bind to E-MgADP forming a catalytically inactive E-MgADP-APS ternary complex
ammonium sulfate
high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations
2'-Phosphoadenosine 5'-phosphosulfate
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2,4,6-Trinitrobenzene sulfonate
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in the presence or absence of ATP-sulfurylase
3'-phosphoadenosine 5'-phosphosulfate
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product inhibition
adenosine 5'-phosphosulfate
ATP
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inhibition by free ATP, i.e. in excess of total Mg2+
diethyldicarbonate
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in the presence or absence of ATP-sulfurylase
adenosine 5'-phosphosulfate
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adenosine 5'-phosphosulfate
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kinetics
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ammonium sulfate
high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations
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0.003 - 0.039
3'-phosphoadenosine 5'-phosphosulfate
0.001 - 0.012
adenosine 5'-phosphosulfate
0.008
3'-phosphoadenosine 5'-phosphosulfate
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pH 8.0, 30°C
0.0008 - 0.0014
adenosine 5'-phosphosulfate
additional information
additional information
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kinetic study
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0.003
3'-phosphoadenosine 5'-phosphosulfate
pH 8.1, 30°C, wild-type enzyme
0.039
3'-phosphoadenosine 5'-phosphosulfate
pH 8.1, 30°C, S107A mutant enzyme
0.001
adenosine 5'-phosphosulfate
pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate
0.012
adenosine 5'-phosphosulfate
pH 8.1, 30°C, S107A mutant enzyme at 100 mM ammonium sulfate
0.8
ATP
pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate
0.8
ATP
ATP in form of MgATP2-
2.4
ATP
pH 8.1, 30°C, S107A mutant enzyme
2.4
ATP
ATP in form of MgATP2-
0.0008
adenosine 5'-phosphosulfate
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pH 8.1, 30°C
0.0014
adenosine 5'-phosphosulfate
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0.0014
adenosine 5'-phosphosulfate
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pH 8.0, 30°C
0.8
ATP
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pH 8.1, 30°C
0.8
ATP
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ATP in form of MgATP2-
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0.013
adenosine 5'-phosphosulfate
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pH 8.1, 30°C
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8
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90% of maximal activity at pH 7.5 and pH 8.5
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SwissProt
brenda
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brenda
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KAPS_PENCH
211
0
23770
Swiss-Prot
Mitochondrion (Reliability: 5 )
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30000
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2 * 30000, SDS-PAGE
33000
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2 * 33000, gel filtration at 46°C, the enzyme dissociates into two inactive monomers by heating above 42°C
57000
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gel filtration at 22°C
59000 - 60000
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gel filtration
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dimer
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2 * 30000, SDS-PAGE
dimer
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2 * 33000, gel filtration at 46°C, the enzyme dissociates into two inactive monomers by heating above 42°C
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crystals are grown in 1.7 M NaH2PO4, 300 mM K2HPO4 and 100 mM Na-succinate, pH 4.0 by hanging drop vapor diffusion at room temperature, crystal structure of E-ADP-APS ternary complex at 1.43 A, crystal structure of E-ADP binary complex at 2.0 A
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S104A
similar properties as wild-type
S107A
similar properties as wild-type enzyme
S107C
similar properties as wild-type, suggesting that S107 is not essential for activity but may be located in the substrate binding pocket
S97A
similar properties as wild-type
S99A
similar properties as wild-type
T103A
similar properties as wild-type
Y109F
similar properties as wild-type, velocity curve is shifted to the far right
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6
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below, reversible inactivation at 30°C, reactivation rate increases with increasing pH
641209
7
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reversible inactivation at 42°C
641209
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35
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inactivation above, reversible by cooling to 0-30°C
36
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equilibrium between active and inactive enzyme form
40
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reversible inactivation above by subunit dissociation, kinetics, MgATP2- or MgADP- stimulate reactivation
43
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reversible inactivation, t1/2: 1 min
60 - 100
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1 min, 85% reversible inactivation
80
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irreversible inactivation, t1/2: 47 min, pH 8, 0.023 mg protein/ml
50
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1 min, 80% reversible inactivation
50
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rapid loss of activity, approx. 80% of activity is recovered upon cooling at 0°C, presence of MgATP2- accelerates the recovery process
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slow inactivation in dilute solutions, even at low temperatures
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ammonium sulfate, Affi-gel blue, Matrix-gel green, Agarose A
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expression of wild-type and S107A mutant enzyme in Escherichia coli
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Renosto, F.; Seubert, P.A.; Segel, I.H.
Adenosine 5-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization
J. Biol. Chem.
259
2113-2123
1984
Penicillium chrysogenum
brenda
Renosto, F.; Schultz, T.; Re, E.; Mazer, J.; Chandler, C.J.; Barron, A.; Segel, I.H.
Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile)
J. Bacteriol.
164
674-683
1985
Penicillium chrysogenum, Penicillium duponti
brenda
Renosto, F.; Seubert, P.A.; Knudson, P.; Segel, I.H.
APS kinase from Penicillium chrysogenum. Dissociation and reassociation of subunits as the basis of the reversible heat inactivation
J. Biol. Chem.
260
1535-1544
1985
Penicillium chrysogenum
brenda
Renosto, F.; Martin, R.L.; Segel, I.H.
Sulfate-activating enzymes of Penicillium chrysogenum. The ATP sulfurylase.adenosine 5-phosphosulfate complex does not serve as a substrate for adenosine 5-phosphosulfate kinase
J. Biol. Chem.
264
9433-9437
1989
Penicillium chrysogenum
brenda
MacRae, I.J.; Rose, A.B.; Segel, I.H.
Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues
J. Biol. Chem.
273
28583-28589
1998
Escherichia coli (P23846), Escherichia coli, Penicillium chrysogenum (Q12657), Penicillium chrysogenum
brenda
MacRae, I.J.; Segel, I.H.
Adenosine 5'-phosphosulfate (APS) kinase: diagnosing the mechanism of substrate inhibition
Arch. Biochem. Biophys.
361
277-282
1999
Penicillium chrysogenum
brenda
Lansdon, E.B.; Segel, I.H.; Fisher, A.J.
Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum
Biochemistry
41
13672-13680
2002
Penicillium chrysogenum (Q12657), Penicillium chrysogenum
brenda