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Information on EC 2.7.7.4 - sulfate adenylyltransferase
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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
-
bottom
- dextran
- sulfite
-
biomolecules
-
sulfotransferase
-
liquid-liquid
-
assimilatory
- chrysogenum
- k2hpo4
- vr
-
vanishing
- selenate
-
e-cigarettes
-
2alpha
- eif2alpha
- phytochelatins
- agriculture
- juncea
- leukoencephalopathy
- chlorate
-
counter-current
-
sults
-
screw
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
atps, atp sulfurylase, papss2, atp-sulfurylase, sulfurylase, atp sulphurylase, atps2, atp-s, atps1, paps synthase 2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphate sulphurylase
-
-
-
-
adenosine 5'-triphosphate-sulfurylase
-
-
-
-
adenosine triphosphate sulfurylase
adenosine triphosphate sulphurylase
-
-
-
-
adenosine-5'-triphosphate sulfurylase
-
-
-
-
adenosinetriphosphate sulfurylase
adenylsulfurylase
adenylylsulfate pyrophosphorylase
-
-
-
-
adenylyltransferase, sulfate
-
-
-
-
APS1
APS2
ATP sulfurylase
ATP sulfurylase-APS kinase
-
; Aquifex aeolicus expresses a gene product that exhibits both ATP sulfurylase and adenosine-5'-phosphosulfate kinase activities
ATP-S
ATP-sulfurylase
ATP: sulfate adenylyl transferase
ATPS
ATPS-B
ATPS1
ATPS2
dissimilatory ATP sulfurylase
MgATP:sulfate adenylyltransferase,
PAPSS1
PAPSs2
SAT
sulfurylase
-
-
-
-
adenosine triphosphate sulfurylase
native enzyme, a dimer with each 71 kDa subunit containing an adenosine triphosphate sulfurylase and an adenosine 5'-hosphosulfate kinase domain, catalyzes the overall formation of PAPS from ATP and inorganic sulfate
adenosinetriphosphate sulfurylase
-
-
-
-
ATP sulfurylase
-
-
-
-
ATP-sulfurylase
-
-
-
-
ATP-sulfurylase
triple fusion protein: APS-kinase, ATP-sulfurylase, and pyrophosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
sequential bi-bi reaction with ATP being the first substrate bound and adenylysulfate the last product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
random sequence for the forward reaction with adenylylsulfate release being partially rate limiting
-
ATP + sulfate = diphosphate + adenylyl sulfate
sequential reaction mechanism in which both substrates bind before any product is released
-
ATP + sulfate = diphosphate + adenylyl sulfate
obligatory ordered kinetic mechanism with MgATP2- adding before MoO42- or SO42- and Mg-diphosphate leaving before AMP + MoO42- or adenosine 5'-phosphosulfate
Brassica capitata
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
analysis of the bi bi substrate kinetic mechanism of GmATPS1. The enzyme shows a kinetic mechanism in which ATP and APS are the first substrates bound in the forward and reverse reactions, respectively
-
ATP + sulfate = diphosphate + adenylyl sulfate
reaction mechanism in which nucleophilic attack by sulfate on the alpha-phosphate of ATP involves transition state stabilization by Arg248, Asn249, His255, and Arg349. ATP sulfurylase overcomes the energetic barrier of APS synthesis by distorting nucleotide structure, identification of critical residues for catalysis, overview
-
ATP + sulfate = diphosphate + adenylyl sulfate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9012-39-9
-
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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
MgATP2- + adenylyl sulfate
MgADP- + 3-phosphoadenylyl sulfate
-
reaction carried out by the APS kinase activity of the bifunctional enzyme
-
-
r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
-
reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
-
-
r
MgATP2- + sulfate
Mg-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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + CrO42-
AMP + adenylyl-chromate
-
-
followed by nonenzymatic reaction of adenylylmolybdate with H2O to AMP and molybdate
?
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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + 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 + MoO42-
AMP + adenylylmolybdate
-
mechanism of molybdolysis is a sequential type in which MgATP2- binds to the enzyme before molybdate
-
-
?
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 + 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 + 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 + 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 + SeO42-
AMP + adenylylselenate
-
20% of the activity with SO42-
reaction is followed by nonenzymatic reaction of adenylylselenate with H2O to AMP and SeO42-
?
ATP + sulfate
diphosphate + adenylyl sulfate
it is shown that AcATPS1 and adenosine-5'-phopshosulfate reductase (AcAPR1) from Allium cepa form protein-protein complexes in vitro, thereby a slight stimulation AcATPS1 activity is detectable
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
reaction is carried out in an anaerobic bioreactor
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
X-ray chrystal structure of a complex between ATPS and its associated regulatory G protein (CysN) is analysed, both proteins are in tight association, with CysD bound to a central cavity formed by the junction of the three domains of CysN
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
catalyzes a reaction in the sulfate assimilation pathway. The chloroplast isoenzyme, representing the more abundant enzyme form, declines in parallel with APS reductase activity during aging of leaf. The cytosolic isoenzyme plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfate reactions
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
adenylylsulfate transgenics are more tolerant than wild-type to As(III), As(V), Cd2+, Cu2+, Hg2+, and Zn2+, but less tolerant to Mo6+ and V6+. The APS seedlings has up to 2.5-fold higher shoot concentrations of As(III), As(V), Hg2+, Mo6+, Pb2+, and V6+, and somewhat lower Cr3+ levels. Mature APS plants contained up to 2.5fold higher shoot concentrations of Cd2+, Cr3+, Cu2+, Mo6+, V6+, and W than wild type. They also contain 1.5fold to 2fold higher levels of the essential elements Fe, Mo, and S in most of the treatments
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
regulation of ATP sulfurylase activity and SO42- uptake by S demand is related to GSH rather than to the GSH/GSSG ratio, and is distinct from the oxidative stress response
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
enzyme plays a crucial role in sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate metabolism
-
-
r
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 + sulfate
diphosphate + adenylylsulfate
-
first enzyme of the two-step sulfate activation sequence
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
key enzyme of sulfate assimilation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes nucleotidyl transfer with inversion of configuration at phosphorus and with a stereoselectivity in excess of 94%
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
-
followed by nonenzymatic reaction of adenylyl-WO42- with H2O to AMP and WO42-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
-
-
-
-
?
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
additional information
?
-
-
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
-
catalyzes the rate-limiting step in the assimilatory pathway for sulfate
-
-
-
additional information
?
-
no binding of diphosphate to enzyme GmATPS1
-
-
-
additional information
?
-
substrate binding structure analysis, overview
-
-
-
additional information
?
-
substrate binding structure analysis, overview
-
-
-
additional information
?
-
the bifunctional PAPS synthases 1 and 2 consist of an N-terminal adenosine-5'-phosphosulphate kinase domain and a C-terminal ATP sulphurylase domain connected by a short irregular linker
-
-
-
additional information
?
-
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
additional information
?
-
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
additional information
?
-
-
enzyme catalyzes ATP-diphosphate exchange reaction. The enzyme does notto catalyze the incorporation of diphosphate into ATP in the absence of SO42-. The enzyme catalyzes SeO42–dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
radioisotopic exchange between the adenosine 5'-sulfatophosphate and SO42- occurs only in the presence of either MgATP2- or diphosphate
-
-
-
additional information
?
-
-
sulfate is the only form of sulfur that catalyzes diphosphate-ATP exchange. The enzyme catalyzes diphosphate-dATP exchange. Selenate catalyzes diphosphate-ATP exchange, but no AMP is formed. Molybdate does not catalyze diphosphate-ATP exchange but AMP is formed
-
-
-
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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 + adenylyl sulfate
O23324, Q43870, Q9LIK9, Q9S7D8
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
Q9LIK9
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
I1LWX5, I1N6H7, I1NGL3, Q8SAG1
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
catalyzes a reaction in the sulfate assimilation pathway. The chloroplast isoenzyme, representing the more abundant enzyme form, declines in parallel with APS reductase activity during aging of leaf. The cytosolic isoenzyme plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfate reactions
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
adenylylsulfate transgenics are more tolerant than wild-type to As(III), As(V), Cd2+, Cu2+, Hg2+, and Zn2+, but less tolerant to Mo6+ and V6+. The APS seedlings has up to 2.5-fold higher shoot concentrations of As(III), As(V), Hg2+, Mo6+, Pb2+, and V6+, and somewhat lower Cr3+ levels. Mature APS plants contained up to 2.5fold higher shoot concentrations of Cd2+, Cr3+, Cu2+, Mo6+, V6+, and W than wild type. They also contain 1.5fold to 2fold higher levels of the essential elements Fe, Mo, and S in most of the treatments
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
regulation of ATP sulfurylase activity and SO42- uptake by S demand is related to GSH rather than to the GSH/GSSG ratio, and is distinct from the oxidative stress response
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
enzyme plays a crucial role in sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate metabolism
-
-
r
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 + sulfate
diphosphate + adenylylsulfate
-
first enzyme of the two-step sulfate activation sequence
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
key enzyme of sulfate assimilation
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
Q9LIK9
-
-
-
r
additional information
?
-
-
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
O67174
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
-
catalyzes the rate-limiting step in the assimilatory pathway for sulfate
-
-
-
additional information
?
-
O43252
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
additional information
?
-
O95340
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cl-
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Co2+
Cobalt
Fe2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Mg2+
Mn2+
Zinc
Zn2+
Ca2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Cobalt
-
contains 1.89 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Cobalt
-
contains 1.53 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Mg2+
required; required; required; required
Mg2+
for APS synthesis assay contains 15 mM MgCl2, for ATP synthesis assay contains 5 mM MgCl2
Mg2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Mg2+
-
formation of ATP from diphosphate and adenylylsulfate is absolutely dependent upon the presence of Mg2+
Mg2+
-
divalent cation required, Mg2+ is optimal for bacteria
Mn2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Zinc
-
contains 0.72 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Zinc
-
contains 1.38 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Zinc
-
zinc ion is tetrahedrally coordinated by Cys294, Cys297, Cys306, and His310, and can not be removed from the protein by treatment with EDTA. The zinc ion binding site is far from the active site. Zinc ion chelation may contribute to the thermal stability of these ATPSs
Zn2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
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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
adenylyl sulfate
APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site; APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site
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
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
adenosine 5'-phosphosulfate
-
potent product inhibition, competitive with both MgATP2- and MoO42- in molybdolysis assay
adenosine 5'-phosphosulfate
-
potent product inhibitor, competitive with respect to MgATP2-, and a mixed type inhibitor with respect to molybdate
ADP
-
linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP
AMP
-
linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP
ATP
-
MgATP2- is the actual substrate, free ATP is an inhibitor of the forward reaction
ATP
-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
ClO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
ClO4-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO4-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
ClO4-
-
linear competitive inhibitor with respect to SO42- and uncompetitive with respect to ATP
FSO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
FSO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate; mixed-type with respect to diphosphate
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
NO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
NO3-
-
linear competitive inhibitor with respect to SO42- and uncompetitive with respect to ATP
S2O32-
-
dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2-
SO42-
-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine-5'-phosphosulfate reductase 1
slight stimulation of ATPS1 activity is noted with the addition of the 5fold volume of full-length adenosine-5'-phosphosulfate reductase 1
-
FSO3-
-
activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
S2O32-
-
activates SO42–dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
-
the enzyme responds to increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea
-
additional information
-
the enzyme responds to sulfate starvation, and increased salinity, but not to increased light irradiation, H2O2, and glutathione level
-
additional information
-
enzyme activity is positively correlated with seed yield and influenced by sulfur assimilation
-
additional information
I1LWX5
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
I1N6H7
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
I1NGL3
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
-
the enzyme responds to increased light irradiation
-
additional information
-
the enzyme in cultured cells responds to sulfate starvation
-
additional information
-
the enzyme responds to increased cadmium level
-
additional information
-
the enzyme responds to increased glutathione level
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
African Swine Fever
The African swine fever virus DP71L protein recruits the protein phosphatase 1 catalytic subunit to dephosphorylate eIF2alpha and inhibits CHOP induction but is dispensable for these activities during virus infection.
Brain Ischemia
PERK is responsible for the increased phosphorylation of eIF2alpha and the severe inhibition of protein synthesis after transient global brain ischemia.
Breast Neoplasms
Enhanced PAPSS2/VCAN sulfation axis is essential for Snail-mediated breast cancer cell migration and metastasis.
Breast Neoplasms
Investigation of the eIF2alpha phosphorylation mechanism in response to proteasome inhibition in melanoma and breast cancer cells.
CADASIL
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
Carcinoma, Hepatocellular
Inactivation of eIF2B and phosphorylation of PHAS-I in heat-shocked rat hepatoma cells.
Chondrosarcoma
Co-purification and characterization of ATP-sulfurylase and adenosine-5'-phosphosulfate kinase from rat chondrosarcoma.
Chondrosarcoma
Intermediate channeling between ATP sulfurylase and adenosine 5'-phosphosulfate kinase from rat chondrosarcoma.
Chondrosarcoma
Rat chondrosarcoma ATP sulfurylase and adenosine 5'-phosphosulfate kinase reside on a single bifunctional protein.
Chondrosarcoma
Sulfate activation and transport in mammals: system components and mechanisms.
Dengue
In situ removal of consensus dengue virus envelope protein domain III fused to hydrophobin in Pichia pastoris cultures.
Dry Eye Syndromes
The Effect of Artificial Tear Preparations with Three Different Ingredients on Contrast Sensitivity in Patients with Dry Eye Syndrome.
Dwarfism
Essential roles of 3'-phosphoadenosine 5'-phosphosulfate synthase in embryonic and larval development of the nematode Caenorhabditis elegans.
Epilepsy
Cellular compartmentalization of phosphorylated eIF2alpha and neuronal NOS in human temporal lobe epilepsy with hippocampal sclerosis.
Epilepsy
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
Epilepsy
Clinical efficacy of gamma knife and surgery treatment of mesial temporal lobe epilepsy and their effects on EF-Tumt and EF-Tsmt expression.
Epilepsy, Temporal Lobe
Cellular compartmentalization of phosphorylated eIF2alpha and neuronal NOS in human temporal lobe epilepsy with hippocampal sclerosis.
Epilepsy, Temporal Lobe
Clinical efficacy of gamma knife and surgery treatment of mesial temporal lobe epilepsy and their effects on EF-Tumt and EF-Tsmt expression.
Glioma
Impairment of stress granule assembly via inhibition of the eIF2alpha phosphorylation sensitizes glioma cells to chemotherapeutic agents.
Head and Neck Neoplasms
Planning comparison of five automated treatment planning solutions for locally advanced head and neck cancer.
Hepatitis C
Cap-dependent and hepatitis C virus internal ribosome entry site-mediated translation are modulated by phosphorylation of eIF2alpha under oxidative stress.
Hepatitis C
The Initiation Factors eIF2, eIF2A, eIF2D, eIF4A, and eIF4G Are Not Involved in Translation Driven by Hepatitis C Virus IRES in Human Cells.
Herpes Simplex
Increased eIF2alpha phosphorylation attenuates replication of herpes simplex virus 2 vhs mutants in mouse embryonic fibroblasts and correlates with reduced accumulation of the PKR antagonist ICP34.5.
Herpes Simplex
Regulation of eIF2alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle.
Infection
The adenovirus E1B 55-kilodalton and E4 open reading frame 6 proteins limit phosphorylation of eIF2alpha during the late phase of infection.
Intellectual Disability
Exclusion of the dymeclin and PAPSS2 genes in a novel form of spondyloepimetaphyseal dysplasia and mental retardation.
Joint Diseases
Degenerative knee joint disease in mice lacking 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (Papss2) activity: a putative model of human PAPSS2 deficiency-associated arthrosis.
Leishmaniasis
Analysis of the Antigenic and Prophylactic Properties of the Leishmania Translation Initiation Factors eIF2 and eIF2B in Natural and Experimental Leishmaniasis.
Leukemia
The induction of G2/M cell-cycle arrest and apoptosis by cucurbitacin E is associated with increased phosphorylation of eIF2alpha in leukemia cells.
Leukoencephalopathies
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
Leukoencephalopathies
Epstein-Barr and other viral mimicry of autoantigens, myelin and vitamin D-related proteins and of EIF2B, the cause of vanishing white matter disease: massive mimicry of multiple sclerosis relevant proteins by the Synechococcus phage.
Leukoencephalopathies
Identification of novel EIF2B mutations in Chinese patients with vanishing white matter disease.
Leukoencephalopathies
Mutant eIF2B leads to impaired mitochondrial oxidative phosphorylation in vanishing white matter disease.
Leukoencephalopathies
Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter.
Leukoencephalopathies
Novel mutation in EIF2B gene in a case of adult-onset leukoencephalopathy with vanishing white matter.
Leukoencephalopathies
Poor cerebral inflammatory response in eIF2B knock-in mice: implications for the aetiology of vanishing white matter disease.
Leukoencephalopathies
Severity of Vanishing White Matter disease does not correlate with deficits in eIF2B activity or the integrity of eIF2B complexes.
Leukoencephalopathies
Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter.
Leukoencephalopathies
The small molecule ISRIB rescues the stability and activity of Vanishing White Matter Disease eIF2B mutant complexes.
Leukoencephalopathies
[Advances in functional study of EIF2B mutations in leukoencephalopathy with vanishing white matter].
Melanoma
Investigation of the eIF2alpha phosphorylation mechanism in response to proteasome inhibition in melanoma and breast cancer cells.
Melanoma, Experimental
ATP6S1 elicits potent humoral responses associated with immune-mediated tumor destruction.
Metabolic Diseases
Human DHEA sulfation requires direct interaction between PAPS synthase 2 and DHEA sulfotransferase SULT2A1.
Migraine Disorders
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
Multiple Myeloma
Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy.
Multiple Sclerosis
Epstein-Barr and other viral mimicry of autoantigens, myelin and vitamin D-related proteins and of EIF2B, the cause of vanishing white matter disease: massive mimicry of multiple sclerosis relevant proteins by the Synechococcus phage.
Myxoma
Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2alpha.
Neoplasms
Engineered Breast Cancer Cell Spheroids Reproduce Biologic Properties of Solid Tumors.
Neoplasms
Extra-low-frequency magnetic fields alter cancer cells through metabolic restriction.
Neoplasms
Sweat but no gain: inhibiting proliferation of multidrug resistant cancer cells with "ersatzdroges".
Neoplasms
Use of the human EF-1alpha promoter for expression can significantly increase success in establishing stable cell lines with consistent expression: a study using the tetracycline-inducible system in human cancer cells.
Onchocerciasis
The elimination of the vector Simulium neavei from the Itwara onchocerciasis focus in Uganda by ground larviciding.
Osteoarthritis, Knee
Identification of sequence polymorphisms in two sulfation-related genes, PAPSS2 and SLC26A2, and an association analysis with knee osteoarthritis.
Osteochondrodysplasias
Human 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase: biochemistry, molecular biology and genetic deficiency.
Osteosarcoma
[In vivo 31P-NMR studies on energy metabolism and the effect of methotrexate in murine implanted osteosarcoma]
Pancreatitis
Caerulein-induced acute pancreatitis inhibits protein synthesis through effects on eIF2B and eIF4F.
Polycystic Ovary Syndrome
PAPSS2 deficiency causes androgen excess via impaired DHEA sulfation - in vitro and in vivo studies in a family harboring two novel PAPSS2 mutations.
Primary Ovarian Insufficiency
Screening for known mutations in EIF2B genes in a large panel of patients with premature ovarian failure.
Prostatic Neoplasms
Aqueous two-phase system to isolate extracellular vesicles from urine for prostate cancer diagnosis.
Prostatic Neoplasms
Exploring Prostate Cancer Genome Reveals Simultaneous Losses of PTEN, FAS and PAPSS2 in Patients with PSA Recurrence after Radical Prostatectomy.
Rift Valley Fever
Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation.
Rotavirus Infections
Protein kinase R is responsible for the phosphorylation of eIF2alpha in rotavirus infection.
Rotavirus Infections
Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules.
Starvation
Catalytic and regulatory properties of sulphur metabolizing enzymes in cyanobacterium Synechococcus elongatus PCC 7942.
Starvation
Coordinated expression of sulfate uptake and components of the sulfate assimilatory pathway in maize.
Starvation
Effect of ATP sulfurylase overexpression in bright yellow 2 tobacco cells. Regulation Of atp sulfurylase and SO4(2-) transport activities.
Starvation
Inter-organ signaling in plants: regulation of ATP sulfurylase and sulfate transporter genes expression in roots mediated by phloem-translocated compound.
Starvation
Regulation of adenosine triphosphate sulfurylase in cultured tobacco cells. Effects of sulfur and nitrogen sources on the formation and decay of the enzyme.
Starvation
Transcriptional and Proteomic Profiling of Aspergillus flavipes in Response to Sulfur Starvation.
Status Epilepticus
Phosphorylation of translation initiation factor eIF2alpha in the brain during pilocarpine-induced status epilepticus in mice.
Stomach Neoplasms
Radiolabeled Anti-Adenosine Triphosphate Synthase Monoclonal Antibody as a Theragnostic Agent Targeting Angiogenesis.
Stroke, Lacunar
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
sulfate adenylyltransferase deficiency
Inactivating PAPSS2 mutations in a patient with premature pubarche.
sulfate adenylyltransferase deficiency
PAPSS2 deficiency causes androgen excess via impaired DHEA sulfation - in vitro and in vivo studies in a family harboring two novel PAPSS2 mutations.
Tuberculosis
Host cell-induced components of the sulfate assimilation pathway are major protective antigens of Mycobacterium tuberculosis.
Tuberculosis
The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex.
Vaccinia
Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2alpha.
Vesicular Stomatitis
The eIF2alpha kinases inhibit vesicular stomatitis virus replication independently of eIF2alpha phosphorylation.
Virus Diseases
The African swine fever virus DP71L protein recruits the protein phosphatase 1 catalytic subunit to dephosphorylate eIF2alpha and inhibits CHOP induction but is dispensable for these activities during virus infection.
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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; pH 8.0, 30°C, molybdolysis, wild-type enzyme
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
0.61
SeO42-
-
pH 7.8, 37°C, SeO42–dependent ATP-diphosphate exchange reaction
additional information
additional information
-
the reaction does not strictly follow Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetic analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michealis-Menten kinetics, overview
-
additional information
additional information
Michealis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, substrate kinetic mechanism of ATP sulfurylase: rapid equilibrium rate equations describe ordered sequential and random sequential kinetic mechanisms, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, substrate kinetic mechanism of ATP sulfurylase: rapid equilibrium rate equations describe ordered sequential and random sequential kinetic mechanisms, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
46.6
adenylylsulfate
-
pH 8.0, 30°C, truncated mutant enzyme del396-573; pH 8.0, 30°C, wild-type enzyme
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; pH 8.0, 30°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000057
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, competitive with MgATP2-, at 0.1 mM MoO42-
0.000063
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, at 0.1 mM MoO42-
0.00007
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, competitive with MoO42-, at 0.05 mM MoO42-
0.00008
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30°C, at 0.05 mM MgATP2-
0.0004
3'-phosphoadenosine-5'-phosphosulfate
-
at 5 mM MgATP2-; pH 8.0, 30°C, at 20 mM MoO42-
0.0047
beta-fluoro-adenosine 5'-phosphosulfate
-
pH 8.0, 30°C, synthesis of ATP
0.0025
beta-methylene-adenosine 5'-phosphosulfate
-
pH 8.0, 30°C, ATP synthesis
0.003
beta-methylene-adenosine 5'-phosphosulfate
-
pH 8.0, 30°C, molybdolysis
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.135
recombinant ATPS1 mutant E169A, pH 8.0, 25°C; recombinant ATPS1 mutant L122V, pH 8.0, 25°C
0.14
recombinant ATPS1 mutant T198A, pH 8.0, 25°C; recombinant ATPS1 mutant V43N, pH 8.0, 25°C
0.145
recombinant wild-type enzyme ATPS1 and mutant A337S, pH 8.0, 25°C
12.96
15.25
ratio AcATPS1-AcAPR1 1:5, five-fold excess of AcAPR1 slightly increases the activity of AcATPS1
additional information
additional information
ATPS activity gradually increases during cold treatment, after 72h at 10°C ATPS activity is 2.2fold higher; ATPS activity in stem and leaf tissue are comparable but lower than in seeds and roots; ATPS activity in young seeds is several-folds higher than in any other tissue
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
7.3