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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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- 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 enzyme appears in viruses and cellular organisms
Synonyms
atps, atp sulfurylase, papss2, atp-sulfurylase, sulfurylase, atp sulphurylase, sulfate adenylyltransferase, atps2, atps1, atp-s, 
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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
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-
-
-
adenosinetriphosphate sulfurylase
adenylsulfurylase
adenylylsulfate pyrophosphorylase
-
-
-
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adenylyltransferase, sulfate
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-
-
-
APS1
APS2
ATP sulfurylase
ATP sulfurylase-APS kinase
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
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-
-
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ATP sulfurylase
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-
-
-
ATP sulfurylase-APS kinase
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Aquifex aeolicus expresses a gene product that exhibits both ATP sulfurylase and adenosine-5'-phosphosulfate kinase activities
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
obligatory ordered kinetic mechanism with MgATP2- adding before MoO42- or SO42- and Mg-diphosphate leaving before AMP + MoO42- or adenosine 5'-phosphosulfate
Brassica capitata
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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
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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
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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
sequential reaction mechanism in which both substrates bind before any product is released
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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
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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-
-
-
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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
-
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 + 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 + 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
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-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
reaction is carried out in an anaerobic bioreactor
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-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
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r
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
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-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
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-
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
-
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
Megalodesulfovibrio gigas
-
enzyme plays a crucial role in 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
diphosphate + adenylyl sulfate
ATP + sulfate
diphosphate in form of magnesium diphosphate
-
-
r
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
?
-
-
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
?
-
-
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
?
-
-
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 SeO42dependent 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
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
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
-
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
Megalodesulfovibrio gigas
-
enzyme plays a crucial role in 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
-
-
-
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
?
-
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
?
-
-
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
-
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
Megalodesulfovibrio gigas
-
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+
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
-
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
Megalodesulfovibrio gigas
-
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
3-tert-butyl-4-hydroxyanisole
ligand diffuses through the gate formed by residues Glu332, Thr312 and His290 to the outside of enzyme. When the gate opens, the ligand is expelled from active site of enzyme, thereafter the ligand returns when the gate closes and binds itself in another region of active site nearby the zinc atom
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 inhibitor, competitive with respect to MgATP2-, and a mixed type inhibitor with respect to molybdate
adenosine 5'-phosphosulfate
-
potent product inhibition, competitive with both MgATP2- and MoO42- in molybdolysis assay
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 SO42dependent 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
-
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
-
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
-
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
-
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
-
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
Alcohol-Related Disorders
Rate of alcoholism diagnoses in community mental health centers: the effect of the presence of an alcoholism treatment program.
Breast Neoplasms
Enhanced PAPSS2/VCAN sulfation axis is essential for Snail-mediated breast cancer cell migration and metastasis.
Breast Neoplasms
Zr-89 Immuno-PET Targeting Ectopic ATP Synthase Enables In-Vivo Imaging of Tumor Angiogenesis.
CADASIL
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
Carcinogenesis
Intestinal Sulfation Is Essential to Protect Against Colitis and Colonic Carcinogenesis.
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.
Colitis
Intestinal Sulfation Is Essential to Protect Against Colitis and Colonic Carcinogenesis.
Colonic Neoplasms
Intestinal Sulfation Is Essential to Protect Against Colitis and Colonic Carcinogenesis.
Dengue
In situ removal of consensus dengue virus envelope protein domain III fused to hydrophobin in Pichia pastoris cultures.
Dry Eye Syndromes
A Decade of Effective Dry Eye Disease Management with Systane Ultra (Polyethylene Glycol/Propylene Glycol with Hydroxypropyl Guar) Lubricant Eye Drops.
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
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
Gallstones
Hypothyroidism Increases Cholesterol Gallstone Prevalence in Mice by Elevated Hydrophobicity of Primary Bile Acids.
Head and Neck Neoplasms
Planning comparison of five automated treatment planning solutions for locally advanced head and neck cancer.
Hyperandrogenism
Low DHEAS Concentration in a Girl Presenting with Short Stature and Premature Pubarche: A Novel PAPSS2 Gene Mutation.
Inflammatory Bowel Diseases
Intestinal Sulfation Is Essential to Protect Against Colitis and Colonic Carcinogenesis.
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.
Leukoencephalopathies
Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy without Anterior Temporal Pole Involvement: A Case Report.
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.
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
Zr-89 Immuno-PET Targeting Ectopic ATP Synthase Enables In-Vivo Imaging of Tumor Angiogenesis.
Onchocerciasis
The elimination of the vector Simulium neavei from the Itwara onchocerciasis focus in Uganda by ground larviciding.
Osteoarthritis
Degenerative knee joint disease in mice lacking 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (Papss2) activity: a putative model of human PAPSS2 deficiency-associated arthrosis.
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]
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.
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.
Prostatic Neoplasms
Zr-89 Immuno-PET Targeting Ectopic ATP Synthase Enables In-Vivo Imaging of Tumor Angiogenesis.
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.
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
Low DHEAS Concentration in a Girl Presenting with Short Stature and Premature Pubarche: A Novel PAPSS2 Gene Mutation.
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.
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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
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
0.61
SeO42-
-
pH 7.8, 37°C, SeO42dependent 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
-
steady-state kinetic analysis of wild-type and mutant enzymes, 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
-
additional information
additional information
Michealis-Menten kinetics, overview
-
additional information
additional information
-
Michealis-Menten kinetics, 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
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
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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
-
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
0.14
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
-
the specific activity in sulfate-reducing bacteria for corrosive and intestinal strains is 0.98-1.56 and 0.98-2.26 U per mg protein, respectively, pH 8.0, 27°C
additional information
ATPS activity gradually increases during cold treatment, after 72h at 10°C ATPS activity is 2.2fold higher
additional information
-
ATPS activity gradually increases during cold treatment, after 72h at 10°C ATPS activity is 2.2fold higher
additional information
ATPS activity in stem and leaf tissue are comparable but lower than in seeds and roots
additional information
-
ATPS activity in stem and leaf tissue are comparable but lower than in seeds and roots
additional information
ATPS activity in young seeds is several-folds higher than in any other tissue
additional information
-
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
8 - 8.5
8.8
8.8
-
and a second but lower optimum at pH 7.3, enzyme form ATPSm, incorporation of SO42-
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
in Tris-malate and Tris-HCl buffer active between pH 5.5 and pH 9.0
6 - 9
-
pH 6.0: about 65% of maximal activity, pH 9.0: about 65% of maximal activity
6.8 - 9.4
-
the enzyme is active in Tris-buffer between pH 6.8 and 9.4
7 - 7.9
-
pH 7.0: about 70% of maximal activity, pH 7.0: about 65% of maximal activity, enzyme form ATPSc, incorporation of SO42-
7.2 - 9.1
-
pH 7.2: about 45% of maximal activity, pH 9.1: about 50% of maximal activity
7.7 - 9
-
pH 7.7: about 75% of maximal activity, pH 9.0: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
30
35
37
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
30 - 50
-
30°C: about 35% of maximal activity, 50°C: about 75% of maximal activity
35 - 60
-
35°C: about 40% of maximal activity, 60°C: about 35% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
ATPS contains a chloroplast/plastid transit peptide sequence in its N-terminal region, processing of the transit peptide releases a mature protein of 46.4 kDa an a pI of 6.26
additional information
-
ATPS contains a chloroplast/plastid transit peptide sequence in its N-terminal region, processing of the transit peptide releases a mature protein of 46.4 kDa an a pI of 6.26
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sulfate-reducing bacteria isolated from various ecotopes such as soils, corrosion products and human large intestine
-
-
brenda
mixed SRB (sulfate reducing bacteria)-containing consortium consisting mainly of the Desulfovibrio genus
-
-
brenda
bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
SwissProt
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bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus
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additional information
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highest activity at the third day after inoculation, declining afterwards to a level found in resting cells
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highest activity at the third day after inoculation, declining afterwards to a level found in resting cells
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PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus
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PAPSs2mRNA is expressed in kidney, expression is higher in female than in male mice
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PAPSs2mRNA expression in liver is higher in female than in male mice, hepatic expression gradually increases from birth until 3 weeks of age and then declines
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PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus
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ATPS mRNA is most abundant in root tissue, cold treatment induces RNA accumulation and enhances the specific activity of ATPS in root tissue
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additional information
by northern blot analysis a decline in the ATPS transcript level during seed development can be found
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additional information
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by northern blot analysis a decline in the ATPS transcript level during seed development can be found
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additional information
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PAPSs2 mRNA is not detectable in brain, gonads, placenta or uterus
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform PAPSS2 is localised mainly within the cytoplasm
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enzyme form ATPSm is mainly associated with mitochondrial membrane
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additional information
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stroma, ATP sulfurylase isoenzymes exist in chloroplast and in cytosol
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Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
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Arabidopsis thaliana has isozymes with N-terminal extensions typical of plastid-transit-peptides
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isozyme ATPS2 is dually encoded in plastidic and cytosolic forms, where translational initiation at AUGMet1 and AUGMet52 or AUGMet58 produce ATPS2 in plastid and cytosol, respectively
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the enzyme has a plastid localization sequence (residues 1-48)
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ATP sulfurylase isoenzymes exist in chloroplast and in cytosol
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isozyme ATPS2 is dually encoded in plastidic and cytosolic forms, where translational initiation at AUGMet1 and AUGMet52 or AUGMet58 produce ATPS2 in plastid and cytosol, respectively
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additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
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additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
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additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
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additional information
Arabidopsis thaliana has isozymes with N'-terminal extensions typical of plastid-transit-peptides
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additional information
isozyme ATPS2 is alternatively translated into two different isoforms that dually localize in plastids and cytosol in Arabidopsis thaliana. Molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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additional information
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isozyme ATPS2 is alternatively translated into two different isoforms that dually localize in plastids and cytosol in Arabidopsis thaliana. Molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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additional information
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isozyme ATPS2 is alternatively translated into two different isoforms that dually localize in plastids and cytosol in Arabidopsis thaliana. Molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-B belongs to the oceanic cyanobacteria of the genera Synechococcus and Prochlorococcus and to all eukaryotic algae except dinoflagellates, sequence alignment of ATPS from the algal species, overview
evolution
an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. The absence of this residue in the ATPS-A of the freshwater cyanobacterium Synechocystis sp. is consistent with its lack of regulation. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-A is typical of all freshwater cyanobacteria and marine-coastal cyanobacteria that do not belong to the genera Synechococcus and Prochlorococcus, sequence alignment of ATPS from the algal species, overview
evolution
despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes. The sat-aprMBA gene locus in Allochromatium vinosum and other phototrophic members of the family Chromatiaceae, overview
evolution
in plants, gene families encode multiple isoforms of ATP sulfurylase with varied expression patterns and organelle localization
evolution
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despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes. The sat-aprMBA gene locus in Allochromatium vinosum and other phototrophic members of the family Chromatiaceae, overview
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evolution
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an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-B belongs to the oceanic cyanobacteria of the genera Synechococcus and Prochlorococcus and to all eukaryotic algae except dinoflagellates, sequence alignment of ATPS from the algal species, overview
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malfunction
plants with the Bay allele of ATPS1 accumulate lower steady-state levels of ATPS1 transcript than those with the Sha allele, which leads to lower enzyme activity and, ultimately, the accumulation of sulfate. Examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher. The contents of glutathione are not affected by the disruption of ATPS1 in Col-0 but are lower in Shahdara and both HIF004 lines compared with Bay-0 and the Col-0 genotypes
malfunction
the suppression of PAPSS1 and 2 decreases the levels of obligate cofactor and sulfate donor PAPS and reduce cellular sulfotransferase activity. Endogenous SULT2A1 is not upregulated in PAPSS1/2 double knockdown HepG2 cells, whereas the amount of UGT2B4 mRNA is significantly increased. Mechanism(s) responsible for the PAPSS1/2 knockdown-mediated upregulation of human UGT2B4, overview
malfunction
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plants with the Bay allele of ATPS1 accumulate lower steady-state levels of ATPS1 transcript than those with the Sha allele, which leads to lower enzyme activity and, ultimately, the accumulation of sulfate. Examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher. The contents of glutathione are not affected by the disruption of ATPS1 in Col-0 but are lower in Shahdara and both HIF004 lines compared with Bay-0 and the Col-0 genotypes
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metabolism
all sulfation reactions rely on active sulfate in the form of 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate is converted to the sulfonucleotide adenylyl sulfate, APS, by the ubiquitous ATP sulfurylase. APS represents a metabolic branchpoint in bacteria and plants, where it is reduced by APS reductase to sulfite, and finally incorporated into primary metabolites after further reduction. Alternatively, APS is phosphorylated by APS kinase to the universal sulfate donor PAPS. In metazoans and humans, ATP sulfurylase and APS kinase reside on one polypeptide, the bifunctional PAPS synthase. All eukaryotic sulfotransferases depend on the provision of active sulfate inthe form of 3'-phospho-adenosine-5'-phosphosulfate (PAPS) for their proper action. The importance of PAPS for sulfation can rival that of ATP for phosphorylation processes. Various regulatory roles of APS in the overall process of PAPS biosynthesis
metabolism
all sulfation reactions rely on active sulfate in the form of 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate is converted to the sulfonucleotide adenylyl sulfate, APS, by the ubiquitous ATP sulfurylase. APS represents a metabolic branchpoint in bacteria and plants, where it is reduced by APS reductase to sulfite, and finally incorporated into primary metabolites after further reduction. Alternatively, APS is phosphorylated by APS kinase to the universal sulfate donor PAPS. In metazoans and humans, ATP sulfurylase and APS kinase reside on one polypeptide, the bifunctional PAPS synthase. All eukaryotic sulfotransferases depend on the provision of active sulfate inthe form of 3?-phospho-adenosine-5'-phosphosulfate (PAPS) for their proper action. The importance of PAPS for sulfation can rival that of ATP for phosphorylation processes. Various regulatory roles of APS in the overall process of PAPS biosynthesis
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
metabolism
ATP sulfurylase precedes adenosine 5'-phosphosulfate reductase in the sulfate assimilation pathway. The ATPS1 transcript variation is controlled in cis
metabolism
molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
metabolism
sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase
metabolism
the first enzymatic reaction in the sulfur assimilation pathway of plants is the non-reductive adenylation of sulfate catalysed by ATP sulfurylase to yield adenylyl sulfate, APS, and diphosphate. The enzyme also catalyzes the next step, producing ADP and 3'-phosphoadenylyl sulfate from ATP and adenylyl sulfate, cf. EC 2.7.1.25
metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
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metabolism
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sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase
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metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
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metabolism
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molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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metabolism
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ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
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metabolism
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ATP sulfurylase precedes adenosine 5'-phosphosulfate reductase in the sulfate assimilation pathway. The ATPS1 transcript variation is controlled in cis
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physiological function
ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-A of the freshwater cyanobacterium Synechocystis sp. shows that the lack of residue Cys247 causes a lack of regulation
physiological function
ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-B from the marine diatom Thalassiosira pseudonana shows that the residue Cys247 is presumably involved in the redox regulation
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
sulfate content in Arabidopsis thaliana is controlled by two genes encoding subsequent enzymes in the sulfate assimilation pathway but using different mechanisms, variation in amino acid sequence and variation in expression levels
physiological function
the enzyme is dispensible for growth on reduced sulfur compounds due to the presence of an alternate sulfite-oxidizing pathway in Allochromatium vinosum
physiological function
the sulfur assimilation pathway provides sulfide for a range of biosynthetic pathways that supply methionine, glutathione, ironsulfur clusters, vitamin cofactors such as biotin and thiamin, and multiple specialized metabolites such as glucosinolates
physiological function
-
comparative analysis of both enzyme characteristics and growth parameters of sulfate-reducing bacteria isolated from various ecotopes such as soils, corrosion products and human large intestine
physiological function
transgenic soybean seeds overexpressing ATP sulfurylase without the transit peptide show predominant localization in the cytoplasm. Transgenic plants accumulate very low levels of the beta-subunit of beta-conglycinin. The accumulation of the cysteine-rich Bowman-Birk protease inhibitor is several fold higher in transgenic soybean plants. Their overall protein content is lowered by about 3%. 84 out of 124 seed metabolites are present in higher amounts and 40 are present in lower amounts in ATP sulfurylase overexpressing seeds compared to the wild-type seeds. ATP sulfurylase overexpressing seeds contain significantly higher amounts of phospholipids, lysophospholipids, diacylglycerols, sterols, and sulfolipids. Overexpression of ATP sulfurylase results in 37-52% and 15-19% increases in the protein-bound cysteine and methionine content of transgenic seeds, respectively
physiological function
upon expression in Medicago sativa, transgenic plants grow more efficiently compared with their non-transgenic counterparts under heavy metal stress conditions, with significant increase in shoot and root dry weight. Transgenic lines show higher levels of heavy metal accumulation in shoot and root tissues. The transgenic lines are fertile and do not exhibit any apparent morphological abnormality
physiological function
-
the enzyme is dispensible for growth on reduced sulfur compounds due to the presence of an alternate sulfite-oxidizing pathway in Allochromatium vinosum
-
physiological function
-
ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-B from the marine diatom Thalassiosira pseudonana shows that the residue Cys247 is presumably involved in the redox regulation
-
physiological function
-
sulfate content in Arabidopsis thaliana is controlled by two genes encoding subsequent enzymes in the sulfate assimilation pathway but using different mechanisms, variation in amino acid sequence and variation in expression levels
-
additional information
sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, overview
additional information
the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase
additional information
the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase
additional information
-
the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase
additional information
the enzyme has several highly conserved substrate binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but is similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Residues involved in catalysis and substrate binding, overview
additional information
-
the enzyme has several highly conserved substrate binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but is similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Residues involved in catalysis and substrate binding, overview
additional information
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
-
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
-
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
-
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
-
additional information
-
sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, overview
-
Show AA Sequence and Transmembrane Helices (51884 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
260000
440000
50000
52000
predicted from cDNA sequence, enzyme functions as a 100 kDa homodimer
62000
66000
additional information
additional information
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed. MW is determined by SDS-PAGE for the recombinant full-length enzyme 70000 Da, for the ATP sulfurylase domain 50000 Da, and for the adenosine 5'-phosphosulfate kinase domain 22000 Da
additional information
ATPS contains a chloroplast/plastid transit peptide sequence in its N-terminal region, processing of the transit peptide releases a mature protein of 46.4 kDa an a pI of 6.26
additional information
-
ATPS contains a chloroplast/plastid transit peptide sequence in its N-terminal region, processing of the transit peptide releases a mature protein of 46.4 kDa an a pI of 6.26
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
monomer
octamer
tetramer
trimer
additional information
dimer
Brassica capitata
-
2 * 56000-57000, 2 band of 56000 Da and of 57000 Da, the 56000 Da protein perhaps is a partially proteolyzed subunit, SDS-PAGE
dimer
the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker
homodimer
each subunit subdivided into three domains, the N-terminal domain I (residues 1-172) is basically built up of a beta-barrel with five antiparallel strands surrounded by alpha-helices, the catalytic domain II (residues 173-331) of a typical Rossmann-like alpha/beta structure and the small C-terminal domain III (residues 332-396) of a small three-strand beta-sheet and two alpha-helices
homodimer
-
each subunit subdivided into three domains, the N-terminal domain I (residues 1-172) is basically built up of a beta-barrel with five antiparallel strands surrounded by alpha-helices, the catalytic domain II (residues 173-331) of a typical Rossmann-like alpha/beta structure and the small C-terminal domain III (residues 332-396) of a small three-strand beta-sheet and two alpha-helices
-
monomer
1 * 46000,truncated mutant enzyme del396-573, SDS-PAGE
additional information
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed. MW is determined by SDS-PAGE for the recombinant full-length enzyme 70000 Da, for the ATP sulfurylase domain 50000 Da, and for the adenosine 5'-phosphosulfate kinase domain 22000 Da
additional information
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
additional information
-
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
additional information
-
the enzyme consists of a COOH-terminal ATP sulfurylase domain covalently linked through a nonhomologous intervening sequence to an NH2-terminal adenosine 5'-phosphosulfate kinase domain forming a bifunctional fused protein
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
ATPS contains a chloroplast/plastid transit peptide sequence in its N-terminal region, processing of the transit peptide releases a mature protein of 46.4 kDa an a pI of 6.26
additional information
-
ATPS contains a chloroplast/plastid transit peptide sequence in its N-terminal region, processing of the transit peptide releases a mature protein of 46.4 kDa an a pI of 6.26
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified native enzyme in open state with a ligand-free active site, vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 1.5 M potassium sodium tartrate and 100 mM MES, pH 6.5, at 18°C, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution
crystals are grown by hanging drop vapor diffusion at 25°C in 40% (v/v) ethanol, 1% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM MgATP, X-ray crystal structure analysis shows that the protein dimerizes through its APS kinase domain and contains ADP bound in all four active sites
-
hanging drop vapour diffusion method, at 25 °C, in 40% (v/v) ethanol, 1.0% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM Mg-ATP
-
hanging drop vapour diffusion method, using 3 M ammonium sulfate, 100 mM Tris-HCl pH 7.5 with 10% (v/v) MPD
-
ATP sulfurylase isoform 1 in complex with APS, X-ray diffraction structure determination and analysis
PAPSS1 crystal structures analysis, PDB IDs 2GIF, 2OFW, 1XNJ, and 2PEY
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
X-ray crystal structure analysis of complex between Pseudomonas syringae ATPS (CysD) and its associated regulatory G protein (CysN)
-
crystal structures of ATP sulfurylase with thiosulfate, ADP and chlorate
molecular dynamics simulations for free enzyme and in presence of inhibitors
crystal structure of the enzyme in complex with adenosine 5'-phosphate is determined at 2.5 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A337S
site-directed mutagenesis, shows activity unaltered to the wild-type enzyme
E169A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
G342D
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
G56S
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
L122V
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
M1L/M4L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M52L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M52L/M58
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M4L/M58L
site-directed mutagenesis, cytosolic localization of the mutant
M1L/M52L/M58L
site-directed mutagenesis, cytosolic localization of the mutant
M4L/M52L/M58L
site-directed mutagenesis, chloroplastidic localization of the mutant
M52L/M58L
site-directed mutagenesis, chloroplastidic localization of the mutant
S9R
site-directed mutagenesis, a transit peptide mutant, inactive mutant
T198A
site-directed mutagenesis, shows activity similar to the wild-type enzyme
V316F
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
V43N
site-directed mutagenesis, a transit peptide mutant, shows activity similar to the wild-type enzyme
E169A
-
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
-
G56S
-
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
-
L122V
-
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
-
M1L/M4L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M4L/M52L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M4L/M52L/M58
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M4L/M58L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
M1L/M52L/M58L
-
site-directed mutagenesis, cytosolic localization of the mutant
-
S9R
-
site-directed mutagenesis, a transit peptide mutant, inactive mutant
-
T198A
-
site-directed mutagenesis, shows activity similar to the wild-type enzyme
-
DELTA48
a truncated version of soybean ATPS lacking the first 48 amino acids is generated for protein expression and purification, removal of the putative localisation sequence improves the yield of N-terminally His-tagged protein in Escherichia coli
F245A
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
F245L
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
H252N
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
H255A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
H255Q
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
H333Q
site-directed mutagenesis, shows highly increased activity compared to the wild-type enzyme
L258A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
L258V
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
N249A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
N249D
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
Q246A
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Q246E
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Q246N
site-directed mutagenesis, shows very highly increased activity compared to the wild-type enzyme
R248K
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
R349K
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
G59A
-
significant effect on ATP sulfurylase activity, no effect on adenosine 5'-phosphosulfate kinase activity
H506A
-
mutant enzyme shows 91% of the sulfurylase activity compared to that of the wild-type enzyme, reduced PAPS kinase activity
K65A
-
mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
K65R
-
mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
R421K
-
mutant enzyme shows 8% of the sulfurylase activity compared to that of the wild-type enzyme
R510A
-
mutant enzyme shows 90% of the sulfurylase activity compared to that of the wild-type enzyme
T66A
-
mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
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
additional information
additional information
the plant enzymes only contain ATP sulfurylase domain, unlike the human and yeast enzymes which include an APS kinase domain, located at the N- or C-terminal regions, respectively
additional information
-
the plant enzymes only contain ATP sulfurylase domain, unlike the human and yeast enzymes which include an APS kinase domain, located at the N- or C-terminal regions, respectively
additional information
enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants
additional information
-
enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4
7.8
-
unstable in Tris, diethylbarbiturate, glycine, triethanolamine and bicarbonate buffer, but stable in phosphate buffers of the same pH
643259
4.4
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
641208
4.4
Penicillium duponti
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
641208
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
25
-
2 h, wild-type enzyme and individually expressed ATP sulfurylase domain of the bifunctional are stable
37
-
2 h, wild-type enzyme is stable, individually expressed ATP sulfurylase domain of the bifunctional enzyme loses 98% of its activity
50
65
additional information
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
65
Penicillium duponti
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
additional information
-
the thermal stability of the Aquifex aeolicus ATP-sulfurylase-APS kinase can be explained by the 43% decreased cavity volume found within the protein core
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, purified enzyme solution, 1 mg protein per ml, 15% loss of activity after 5 weeks
-
4C, 50 mM MOPS buffer, pH 7.4, 0.2 mM CoCl2, 0.2 mM ZnCl2, stable for 48 h
4C, 50 mM MOPS buffer, pH 7.4, 0.2 mM CoCl2, 0.2 mM ZnCl2, stable for 48 h
-
4C, 50 mM MOPS buffer, pH 7.4, 0.2 mM CoCl2, 0.2 mM ZnCl2, stable for 48 h
Megalodesulfovibrio gigas
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified
DEAE-52 cellulose column chromatography, Source 15Q column chromatography, Superdex 200 gel filtration, and hydroxyapatite column chromatography
-
expressed enzyme is purified by affinity chromatography using glutathione-Sepharose and subsequent ion-exchange chromatography
glutathione Sepharose column chromatography and Superdex 200 gel filtration
glutathione-Sepharose column chromatography and Mono Q column chromatography
hydroxyapatite column chromatography, DEAE cellulose column chromatography, and gel filtration
-
partial
protein is purified by sequential chromatographies on hydroxyapatite, DEAE cellulose and gel filtration
-
recombinant enzyme
recombinant His-tagged enzyme from Escherichia coli BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration, native enzyme by hydrophobic interaction chromatography, ultrafiltration, dialysis, anion exchange chromatography, ultracentrifugation, and gel filtration
recombinant wild-type and mutant N-terminally truncated and His6-tagged enzymes from Escherichia coli strain Rosetta (DE3) by nicke affinity chromatography and gel filtration
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Aquifex aeolicus ATP-sulfurylase-APS kinase is expressed in an Escherichia coli pET vector expression system
-
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
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified. Expressed protein generated from the ATP-sulfurylase domain alone is fully active in both the forward and the reverse assays. APS kinase-only recombinants exhibit no kinase activity
-
cloned in Escherichia coli as a truncated version of soybean ATPS lacking the first 48 amino acids, removal of the putative localisation sequence improves the yield of N-terminally His-tagged protein in Escherichia coli
expressed in Escherichia coli
gene APS2 or At1g19920, Arabidopsis thaliana APS isozyme sequence comparisons, protoplast isolation and transfection of APS2, expression of GFP(S65T)-tagged enzyme under control of CaMV 35S promoter, the binary plasmids are transferred to Agrobacteriumtume faciens C58C1 GV3101 that are transformed by floral dip method into plants. Translationof ATPS2 mRNA starts at multiple sites, AUGMet1 and eitherAUGMet52 or AUGMet58, to produce the plastidic and the cytosolic ATPS2 isoforms, respectively, in Arabidopsis thaliana. The alternative translational initiation sites of ATPS2 are determined by expression of dual-luciferase-tagged fusion constructs of wild-type and mutant isozyme ATPS2 in Arabidopsis protoplasts. The translation of chloroplastic ATPS2 pre-protein can only be initiated from the AUGMet1 start codon
gene atps1 or At3g22890, examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher
gene sat, sequence comparisons, the sat gene is located in one operon and co-transcribed with the aprMBA genes for membrane-bound APS reductase, recombinant expression of His-tagged enzyme in Escherichia coli
His-tag version expressed in Escherichia coli BL21-DE3
isoform PAPS synthase 1 wild type and mutant proteins are expressed in Escherichia coli
sequence comparisons and phylogenetic tree, recombinant expression of wild-type and mutant N-terminally truncated and His6-tagged enzymes in Escherichia coli strain Rosetta (DE3)
the four ATP-S genes ATPS1,-2,-3, and -4 have N-terminal extensions typ ical of plastid-transit peptides, and are located on different chromosomes
the four ATP-S genes ATPS1,-2,-3, and -4 have N-terminal extensions typical of plastid-transit peptides, and are located on different chromosomes
the protein is insoluble when the full-length cDNA of soybean ATPS, including the chloroplast/plastid localisation sequence, is used for expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ATP-S activity/expression can also be controlled/modulated by S-limitation1 (SLIM1), a transcription factor identical to ethylene-insensitive3-like (EIL3) transcription factor in Arabidopsis and the regulator of many S-deficiency responsive genes
growth on Se enriched soil, induces APS2 expression levels in young (or mature) leaves and roots in Camellia sinensis
growth on Se enriched soil, suppresses APS1 expression levels in young (or mature) leaves and roots in Camellia sinensis
the enzyme responds to increased cadmium level
the enzyme responds to increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea
-
the enzyme responds to increased glutathione level
the enzyme responds to increased light irradiation
the enzyme responds to sulfate starvation, and increased salinity, but not to increased light irradiation, H2O2, and glutathione level
-
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthora infestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion mediates regulation of ATP-S activity/expression. ATP-S isoforms can be differentially expressed by S-depletion, e.g. isozyme APS3, while isozyme APS2 is insensitive to S-depletion. Arabidopsis thaliana overexpressing or disruption in MYB51-gene shows alterations in ATP-S-transcript levels and activity. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthora infestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion mediates regulation of ATP-S activity/expression. ATP-S isoforms can be differentially expressed by S-depletion, e.g. isozyme APS3, while isozyme APS2 is insentivie to S depletion. Expression of both ATPS1 and ATPS3 isoforms is controlled by all six GSs-related MYBTFs, namely MYB28, MYB29, and MYB76, MYB51, MYB34, and MYB122. Isozymes ATPS1 and ATPS3 are strongly associated with the control of synthesis of aliphatic and indolic GSs, respectively. Arabidopsis thaliana overexpressing or disruption in MYB51-gene shows alterations in ATP-S-transcript levels and activity. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthora infestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion mediates regulation of ATP-S activity/expression. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation. S-depletion-mediates regulation of ATP-S activity/expression. Expression of both ATPS1 and ATPS3 isoforms is controlled by all six GSs-related MYBTFs, namely MYB28, MYB29, and MYB76, MYB51, MYB34, and MYB122. Isozymes ATPS1 and ATPS3 are strongly associated with the control of synthesis of aliphatic and indolic GSs, respectively. Arabidopsis thaliana overexpressing or disruption in MYB51-gene shows alterations in ATP-S-transcript levels and activity. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
the enzyme responds to sulfate starvation, increased light irradiation, and chilling o cold stress
-
under Se-exposure and S-deficiency, Stanleya pinnata hyperaccumulates and tolerates selenium due to its ability to convert SeO24- to non-toxic organic-seleno-compounds by downregulating isozymes APS1, APS2, and APS4. Under S-sufficient and Se-exposure, adoption of different types of regulatory mechanisms and subcellular localization are revealed in Stanleya pinnata, where Se upregulates APS1 and APS4 but is not able to affect APS2 in Stanleya pinnata
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
-
overexpression of ATP sulfurylase may be a promising approach to create plants with enhanced phytoextraction capacity for mixtures of metals
agriculture
-
ATPS may potentially be used as an enzymatic marker for biological sulfate reduction in sulfate-rich wastewaters and natural environments consisting of anaerobic systems such as soils and sediments found in freshwater and marine systems
agriculture
increasing the expression level of this key enzyme during soybean seed development could lead to an increase in the availability of sulfur amino acids, thereby enhancing the nutritional value of the crop
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ORGANISM (UNIPROT)
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1985
Blastochloris viridis, Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodovulum sulfidophilum, Rubrivivax gelatinosus, Rhodopseudomonas palustris, Rhodospirillum rubrum
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Mus musculus
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Purification and properties of two forms of ATP sulfurylase from Euglena
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1991
Euglena gracilis
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Zea mays
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Brassica capitata
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Spinacia oleracea
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Spinacia oleracea
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Astragalus bisulcatus, Astragalus hamosus, Astragalus racemosus, Astragalus sinicus
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Oryza sativa
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Mus musculus
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Penicillium chrysogenum (Q12650), Penicillium chrysogenum
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Saccharomyces cerevisiae
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Archaeoglobus fulgidus
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Geobacillus stearothermophilus, Geobacillus stearothermophilus NCA 1503
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Homo sapiens
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Desulfovibrio desulfuricans, Megalodesulfovibrio gigas
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Thermus thermophilus HB8
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Homo sapiens (O43252), Homo sapiens
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Brassica juncea
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Glycine max (Q8SAG1), Glycine max
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Allium cepa, Allium cepa (Q9SDP4)
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Desulfovibrio desulfuricans
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Sedum alfredii
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Acidithiobacillus ferrooxidans
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Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm
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Homo sapiens (O43252), Homo sapiens
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Redox regulation of ATP sulfurylase in microalgae
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Glycine max (Q8SAG1)
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Upregulation of UGT2B4 expression by 3-phosphoadenosine-5-phosphosulfate synthase knockdown: implications for coordinated control of bile acid conjugation
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Homo sapiens (O43252), Homo sapiens
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Alternative translational initiation of ATP sulfurylase underlying dual localization of sulfate assimilation pathways in plastids and cytosol in Arabidopsis thaliana
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Arabidopsis thaliana (Q43870), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q43870)
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ATP-sulfurylase, sulfur-compounds, and plant stress tolerance
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Avena sativa, Brassica juncea, Brassica napus, Hordeum vulgare, Lemna gibba, Lepidium sativum, Nicotiana tabacum, Oryza sativa, Triticum aestivum, Zea mays, Noccaea caerulescens, Sedum alfredii, Stanleya pinnata, Salvinia minima, Glycine max (I1LWX5), Glycine max (I1N6H7), Glycine max (I1NGL3), Glycine max (Q8SAG1), Arabidopsis thaliana (O23324), Arabidopsis thaliana (Q43870), Arabidopsis thaliana (Q9LIK9), Arabidopsis thaliana (Q9S7D8), Camellia sinensis (Q1HL01), Camellia sinensis (Q1HL02)
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Glycine max (Q8SAG1), Glycine max, Arabidopsis thaliana (Q9LIK9), Arabidopsis thaliana Col-0 (Q9LIK9)
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Allochromatium vinosum (O66036), Allochromatium vinosum, Allochromatium vinosum DSM 180 (O66036)
brenda
Kushkevych, I.V.; Antonyak, H.L.; Bartos, M.
Kinetic properties of adenosine triphosphate sulfurylase of intestinal sulfate-reducing bacteria
Ukr. Biochem. J.
86
129-138
2015
Desulfovibrio piger, Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger Vib-7
brenda
Abdulina, D.; Kovvac, J.; Iutynska, G.; Kushkevych, I.
ATP sulfurylase activity of sulfate-reducing bacteria from various ecotopes
3 Biotech
10
55
2020
bacterium
brenda
Kumar, V.; AlMomin, S.; Al-Shatti, A.; Al-Aqeel, H.; Al-Salameen, F.; Shajan, A.B.; Nair, S.M.
Enhancement of heavy metal tolerance and accumulation efficiency by expressing Arabidopsis ATP sulfurylase gene in alfalfa
Int. J. Phytoremediation
21
1112-1121
2019
Arabidopsis thaliana (Q9LIK9)
brenda
Dos Santos, E.; Gritta, D.; De Almeida, J.
Analysis of interactions between potent inhibitors of ATP sulfurylase via molecular dynamics
Mol. Simul.
42
605-610
2016
Thermus thermophilus (Q5SKH7)
-
brenda
Kim, W.; Sun-Hyung, J.; Oehrle, N.; Jez, J.; Krishnan, H.
Overexpression of ATP sulfurylase improves the sulfur amino acid content, enhances the accumulation of Bowman-Birk protease inhibitor and suppresses the accumulation of the beta-subunit of beta-conglycinin in soybean seeds
Sci. Rep.
10
14989
2020
Glycine max (Q8SAG1), Glycine max
brenda
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Release 2023.1 (January 2023)
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