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Information on EC 2.7.7.4 - sulfate adenylyltransferase and Organism(s) Penicillium chrysogenum and UniProt Accession Q12650
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2.7.7.4 sulfate adenylyltransferaseIUBMB 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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Word Map
- 2.7.7.4
-
two-phase
- peg
- glycol
-
bottom
- dextran
-
peg-rich
-
liquid-liquid
-
biomolecules
-
assimilatory
- vr
- chrysogenum
- k2hpo4
-
diagram
-
sulfotransferase
- selenate
-
microfluidic
- sulfite
-
counter-current
-
e-cigarettes
- juncea
- o-acetylserine
- na2so4
- phytochelatins
-
ultrasonic-assisted
-
screw
-
immiscible
-
sults
- chlorate
-
cigar
- agriculture
The taxonomic range for the selected organisms is: Penicillium chrysogenum
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphate sulphurylase
-
-
-
-
adenosine 5'-triphosphate-sulfurylase
-
-
-
-
adenosine triphosphate sulphurylase
-
-
-
-
adenosine-5'-triphosphate sulfurylase
-
-
-
-
adenosinetriphosphate sulfurylase
-
-
-
-
adenylylsulfate pyrophosphorylase
-
-
-
-
adenylyltransferase, sulfate
-
-
-
-
ATP sulfurylase
-
-
-
-
ATP-sulfurylase
-
-
-
-
sulfurylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
random sequence for the forward reaction with adenylylsulfate release being partially rate limiting
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
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
9012-39-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
the ATP sulfurylase-adenylylsulfate complex does not serve as a substrate for APS kinase, i.e. there is no substrate chanelling of APS between the two sulfate-activating enzymes
-
-
r
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylylsulfate
-
the ATP sulfurylase-adenylylsulfate complex does not serve as a substrate for APS kinase, i.e. there is no substrate chanelling of APS between the two sulfate-activating enzymes
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-phosphoadenosine 5'-phosphosulfate
allosteric, binding of the inhibitor to the catalytic site as well as to the allosteric site of the wild type enzyme acts to decrease the degree of cooperativity
5,5'-dithiobis(2-nitrobenzoic acid)
0.05 mM, rapid decrease in activity of wild-type enzyme (t1/2: 20 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min
NEM
0.15 mM, rapid decrease in activity of wild-type enzyme (t1/2: 45 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min
Phenylglyoxal
3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
thiosulfate
competitive with molybdate and noncompetitive with MgATP
diacetyl
-
significant inhibition in the presence of borate, protection by adenosine 5'-phosphosulfate, ATP or MgATP2- plus nitrate
methylene blue
-
inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate
N-Acetylimidazole
-
76% of the original activity can be restored by treatment with hydroxylamine
adenosine 5'-phosphosulfate
-
potent product inhibition, competitive with both MgATP2- and MoO42- in molybdolysis assay
ClO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO4-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
FSO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate
S2O32-
-
dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FSO3-
-
activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
S2O32-
-
activates SO42dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
adenylylsulfate
pH 8.0, 30°C, truncated mutant enzyme del396-573
0.027
ATP
pH 8.0, 30°C, molybdolysis, truncated mutant enzyme del396-573
0.21
ATP
pH 8.0, 30°C, synthesis of adenylylsulfate, wild-type enzyme
2.6
ATP
pH 8.0, 30°C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573
0.025
diphosphate
pH 8.0, 30°C, truncated mutant enzyme del396-573
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
46.6
adenylylsulfate
pH 8.0, 30°C, truncated mutant enzyme del396-573
1.8
ATP
pH 8.0, 30°C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573
10.8
ATP
pH 8.0, 30°C, synthesis of adenylylsulfate, wild-type enzyme
13.7
ATP
pH 8.0, 30°C, molybdolysis, truncated mutant enzyme del396-573
73.3
diphosphate
pH 8.0, 30°C, truncated mutant enzyme del396-573
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000063
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, at 0.1 mM MoO42-
0.00008
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, at 0.05 mM MgATP2-
0.0004
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, at 20 mM MoO42-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MET3_PENCH
572
0
63917
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 46000,truncated mutant enzyme del396-573, SDS-PAGE
additional information
additional information
the hexameric enzyme is a dimer of triads in the shape of an ablate ellipsoid 140 A diameter * 70 A. Each subunit is divided into a discrete N-terminal domain, a central catalytic domain, and a C-terminal allosteric domain
additional information
-
the hexameric enzyme is a dimer of triads in the shape of an ablate ellipsoid 140 A diameter * 70 A. Each subunit is divided into a discrete N-terminal domain, a central catalytic domain, and a C-terminal allosteric domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in Escherichia coli, crystals are grown at 22°C by vapor diffusion in hanging drops, crystal structure of the enzyme bound to the allosteric inhibitor 3'-phosphoadenosine-5'-phosphosulfate determined at 2.6 A resolution
recombinant enzyme expressed in Escherichia coli, crystals are grown by hanging drop vapor diffusion at 4°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
del396-573
recombinant ATP sulfurylase lacking the C-terminal allosteric domain is monomeric and noncooperative. Mutant enzyme is less heat stable than wild-type enzyme. Wild-type enzyme behaves cooperative at pH 6.5, truncated enzyme form displays normal hyperbolic behavior
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
641208
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
t1/2 for mutant enzyme del396-573: 0.3 min, wild-type enzyme is stable for more than 2 h
65
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
additional information
additional information
-
the reversible temperature-dependent transitions of the enzyme may play a role in energy conservation at high temperatures where the organism can survive but not grow optimally
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Peck, H.D.
Sulfation linked to ATP cleavage
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
10
651-669
1974
Bacillus subtilis, Desulfotomaculum nigrificans, Desulfovibrio desulfuricans, Escherichia coli, Penicillium sp., Ovis aries, Mus musculus, Nitrobacter winogradskyi, Nitrosomonas europaea, Penicillium chrysogenum, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Spinacia oleracea, Thiobacillus thioparus
-
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
Farley, J.R.; Christie, E.A.; Seubert, P.A.; Segel, I.H.
Adenosine triphosphate sulfurylase from Penicillium chrysogenum. Evidence for essential arginine, histidine, and tyrosine residues
J. Biol. Chem.
254
3537-3542
1979
Penicillium chrysogenum
Seubert, P.A.; Hoang, L.; Renosto, F.; Segel, I.H.
ATP sulfurylase from Penicillium chrysogenum: measurements of the true specific activity of an enzyme subject to potent product inhibition and a reassessment of the kinetic mechanism
Arch. Biochem. Biophys.
225
679-691
1983
Penicillium chrysogenum
Farley, J.R.; Cryns, D.F.; Yang, Y.H.J.; Segel, I.H.
Adenosine triphosphate sulfurylase from penicillium chrysogenum. Steady state kinetics of the forward and reverse reactions
J. Biol. Chem.
251
4389-4397
1976
Penicillium chrysogenum
Seubert, P.A.; Renosto, F.; Knudson, P.; Segel, I.H.
Adenosinetriphosphate sulfurylase from Penicillium chrysogenum: steady-state kinetics of the forward and reverse reactions, alternative substrate kinetics, and equilibrium binding studies
Arch. Biochem. Biophys.
240
509-523
1985
Penicillium chrysogenum
MacRae, I.J.; Segel, I.H.; Fisher, A.J.
Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation
Biochemistry
40
6795-6804
2001
Penicillium chrysogenum (Q12650), Penicillium chrysogenum
Medina, D.C.; Hanna, E.; MacRae, I.J.; Fisher, A.J.; Segel, I.H.
Temperature effects on the allosteric transition of ATP sulfurylase from Penicillium chrysogenum
Arch. Biochem. Biophys.
393
51-60
2001
Penicillium chrysogenum
MacRae, I.J.; Segel, I.H.; Fisher, A.J.
Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum
Nat. Struct. Biol.
9
945-949
2002
Penicillium chrysogenum (Q12650), Penicillium chrysogenum
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