Information on EC 2.7.7.4 - sulfate adenylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.7.7.4
-
RECOMMENDED NAME
GeneOntology No.
sulfate adenylyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
sequential bi-bi reaction with ATP being the first substrate bound and adenylysulfate the last product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
random sequence for the forward reaction with adenylylsulfate release being partially rate limiting
-
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
sequential reaction mechanism in which both substrates bind before any product is released
-
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
obligatory ordered kinetic mechanism with MgATP2- adding before MoO42- or SO42- and Mg-diphosphate leaving before AMP + MoO42- or adenosine 5'-phosphosulfate
Brassica capitata
-
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
selenate reduction
-
-
sulfate activation for sulfonation
-
-
sulfate reduction II (assimilatory)
-
-
sulfate reduction III (assimilatory)
-
-
sulfate reduction IV (dissimilatory)
-
-
sulfate reduction V (dissimilatory)
-
-
sulfite oxidation III
-
-
sulfate reduction
-
-
Purine metabolism
-
-
Monobactam biosynthesis
-
-
Selenocompound metabolism
-
-
Sulfur metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
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).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3'-phospho-adenosine-5'-phosphosulphate synthase
-
AcATPS1
-
-
adenosine 5'-triphosphate sulphurylase
-
-
-
-
adenosine 5'-triphosphate-sulfurylase
-
-
-
-
adenosine triphosphate 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
adenosine triphosphate sulphurylase
-
-
-
-
adenosine triphosphate-sulphurylase
-
-
adenosine-5'-triphosphate sulfurylase
-
-
-
-
adenosinetriphosphate sulfurylase
-
-
-
-
adenosinetriphosphate sulfurylase
-
-
adenylylsulfate pyrophosphorylase
-
-
-
-
adenylyltransferase, sulfate
-
-
-
-
ATP sulfurylase
-
-
-
-
ATP sulfurylase
-
ATP sulfurylase
-
ATP sulfurylase
Candidatus Ruthia magnifica Cm
-
-
ATP sulfurylase
-
-
ATP sulfurylase
-
ATP sulfurylase
-
-
ATP sulfurylase
-
-
ATP sulfurylase
-
-
ATP sulfurylase
-
-
ATP sulfurylase-APS kinase
-
; Aquifex aeolicus expresses a gene product that exhibits both ATP sulfurylase and adenosine-5'-phosphosulfate kinase activities
ATP sulphurylase
-
ATP-sulfurylase
-
-
-
-
ATP-sulfurylase
-
ATP-sulfurylase
triple fusion protein: APS-kinase, ATP-sulfurylase, and pyrophosphatase
ATP: sulfate adenylyl transferase
-
MgATP:sulfate adenylyltransferase
-
-
PAPS synthase
-
PAPS synthase1
-
-
PAPS synthase2
-
-
PAPSS1
isoform
PAPSS1
-
-
PAPSs2
isoform
PAPSs2
-
-
sulfurylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9012-39-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Columbi aecotype
-
-
Manually annotated by BRENDA team
Brassica capitata
-
-
-
Manually annotated by BRENDA team
transgenics overexpressing ATP sulfurylase
-
-
Manually annotated by BRENDA team
Candidatus Ruthia magnifica Cm
strain Cm
SwissProt
Manually annotated by BRENDA team
strain ATCC 27774
-
-
Manually annotated by BRENDA team
mixed SRB (sulfate reducing bacteria)-containing consortium consisting mainly of the Desulfovibrio genus
-
-
Manually annotated by BRENDA team
Klebs var. bacillaris Cori, aplastidic mutant W10BSmL
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus NCA 1503
strain NCA 1503
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
SwissProt
Manually annotated by BRENDA team
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
-
-
Manually annotated by BRENDA team
recombinant
SwissProt
Manually annotated by BRENDA team
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
-
-
Manually annotated by BRENDA team
Penicillium duponti
-
-
-
Manually annotated by BRENDA team
Sacardo, strongly sulfite producing strain
-
-
Manually annotated by BRENDA team
Saccharomyces bayanus Sacardo
Sacardo, strongly sulfite producing strain
-
-
Manually annotated by BRENDA team
var. ellipsoideus Hansen, non-sulfite producing strain
-
-
Manually annotated by BRENDA team
Synechococcus sp. 6301
6301
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + CrO42-
AMP + adenylyl-chromate
show the reaction diagram
-
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
show the reaction diagram
-
-
followed by nonenzymatic reaction of adenylylmolybdate with H2O to AMP and molybdate
?
ATP + CrO42-
AMP + adenylyl-chromate
show the reaction diagram
-
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 + FPO32-
?
show the reaction diagram
-
-
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
r
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
Penicillium duponti
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
Brassica capitata
-
-
-
-
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
-
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
show the reaction diagram
-
mechanism of molybdolysis is a sequential type in which MgATP2- binds to the enzyme before molybdate
-
?
ATP + SeO42-
AMP + adenylylselenate
show the reaction diagram
-
-
-
-
ATP + SeO42-
AMP + adenylylselenate
show the reaction diagram
-
-
-
?
ATP + SeO42-
AMP + adenylylselenate
show the reaction diagram
-
-
-
?
ATP + SeO42-
AMP + adenylylselenate
show the reaction diagram
-
20% of the activity with SO42-
reaction is followed by nonenzymatic reaction of adenylylselenate with H2O to AMP and SeO42-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Penicillium duponti
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Penicillium duponti
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Brassica capitata
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
the enzyme catalyzes nucleotidyl transfer with inversion of configuration at phosphorus and with a stereoselectivity in excess of 94%
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
constitutive enzyme
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
the enzyme catalyzes the first step of sulfate metabolism
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
key enzyme of sulfate assimilation
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
enzyme plays a crucial role in sulfate activation
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
the enzyme catalyzes the first step of sulfate activation
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
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
show the reaction diagram
-
first enzyme of the two-step sulfate activation sequence
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Saccharomyces bayanus Sacardo
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Synechococcus sp. 6301
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
the enzyme catalyzes the first step of sulfate activation
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
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
show the reaction diagram
-
reaction is carried out in an anaerobic bioreactor
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
-
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
adenylyl sulfate + diphosphate
show the reaction diagram
-
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
show the reaction diagram
-
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
show the reaction diagram
-
-
followed by nonenzymatic reaction of adenylyl-WO42- with H2O to AMP and WO42-
?
ATP + WO42-
AMP + adenylyl-wolframate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
show the reaction diagram
-
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
show the reaction diagram
-
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
-
-
?
MgATP2- + adenylyl sulfate
MgADP- + 3-phosphoadenylyl sulfate
show the reaction diagram
-
reaction carried out by the APS kinase activity of the bifunctional enzyme
-
r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
show the reaction diagram
-
reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
-
r
MgATP2- + sulfate
Mg-diphosphate + adenylyl sulfate
show the reaction diagram
-
-
r
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
-
-
-
additional information
?
-
-
radioisotopic exchange between the adenosine 5'-sulfatophosphate and SO42- occurs only in the presence of either MgATP2- or diphosphate
-
-
-
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
?
-
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
?
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
constitutive enzyme
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
the enzyme catalyzes the first step of sulfate metabolism
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
key enzyme of sulfate assimilation
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
enzyme plays a crucial role in sulfate activation
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
the enzyme catalyzes the first step of sulfate activation
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
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
show the reaction diagram
-
first enzyme of the two-step sulfate activation sequence
-
r
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
?
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
the enzyme catalyzes the first step of sulfate activation
-
r
additional information
?
-
O67174
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
-
catalyzes the rate-limiting step in the assimilatory pathway for sulfate
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
50-60% of the activity with Mg2+
Ca2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Cl-
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Co2+
-
50-60% of the activity with Mg2+
Co2+
-
Mg2+ or Co2+ required
Co2+
-
divalent cation required: Mg2+, Mn2+ or Co2+
Co2+
-
contains cobalt
Cobalt
-
contains 1.89 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Cobalt
-
contains 1.53 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Fe2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Mg2+
-
or an other divalent cation required
Mg2+
-
divalent cation required, Mg2+ is optimal for bacteria
Mg2+
-
-
Mg2+
-
divalent cation required, Mg2+ is optimal for bacteria
Mg2+
-
divalent cation required, Mg2+ is optimal for bacteria
Mg2+
-
divalent cation required, Mg2+ is optimal for bacteria
Mg2+
-
Mg2+-ATP complex is the actual substrate
Mg2+
-
activates
Mg2+
-
formation of ATP from diphosphate and adenylylsulfate is absolutely dependent upon the presence of Mg2+
Mg2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Mg2+
-
Mg2+ is the most efficient divalent cation, Km: 0.122 mM
Mg2+
-
optimal concentration is 1.5 mM
Mg2+
-
optimal concentration is 3 mM
Mg2+
-
Mg2+ or Co2+ required
Mg2+
-
divalent cation required: Mg2+, Mn2+ or Co2+
Mg2+
for APS synthesis assay contains 15 mM MgCl2, for ATP synthesis assay contains 5 mM MgCl2
Mg2+
-
required for activity
Mg2+
-
assay with 2 mM Mg2+
Mn2+
-
divalent cation required, Mn2+ is optimal for mammals
Mn2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Mn2+
-
84% of the activity with Mg2+
Mn2+
-
divalent cation required: Mg2+, Mn2+ or Co2+
SO42-
-
stimulatory to ATPS
Zinc
-
contains 0.72 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Zinc
-
contains 1.38 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Zinc
-
zinc ion is tetrahedrally coordinated by Cys294, Cys297, Cys306, and His310, and can not be removed from the protein by treatment with EDTA. The zinc ion binding site is far from the active site. Zinc ion chelation may contribute to the thermal stability of these ATPSs
Zn2+
-
-
Zn2+
-
divalent cation required, Zn2+ is optimal
Zn2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Zn2+
-
50-60% of the activity with Mg2+
Zn2+
-
contains zinc
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3',5'-adenosine diphosphate
-
-
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'-phosphoadenosine-5'-phosphate
-
strong
3'-phosphoadenosine-5'-phosphate
-
-
3'-phosphoadenosine-5'-phosphate
-
-
3'-phosphoadenosine-5'-phosphate
-
allosteric
3'-phosphoadenosine-5'-phosphosulfate
-
-
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
adenosine 5'-monosulfate
-
-
adenosine 5'-phosphoramidate
-
-
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
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
1 mM, 30% inhibition
adenosine 5'-phosphosulfate
-
1 mM, 90% inhibition
adenosine 5'-phosphosulfate
Brassica capitata
-
-
adenosine 5'-phosphosulfate
-
inhibits molybdolysis
adenosine 5'-phosphosulfate
competitive with ATP and molybdate
adenosine 5'-phosphosulfate
-
competitive with both substrates
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
AMP
-
competitive with MgATP2- and mixed-type with respect to SO42-
ATP
-
MgATP2- is the actual substrate, free ATP is an inhibitor of the forward reaction
ATP
-
free ATP
ATP
-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
Ba2+
-
2 mM
beta-fluoro-adenosine 5'-phosphosulfate
-
-
beta-methylene-adenosine 5'-phosphosulfate
-
-
Ca2+
-
2 mM
ClO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
ClO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO3-
Brassica capitata
-
-
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
ClO4-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO4-
competitive with sulfate and adenylyl sulfate
deoxyadenylylsulfate
-
1 mM, in presence of about 20% inhibition
diacetyl
-
significant inhibition in the presence of borate, protection by adenosine 5'-phosphosulfate, ATP or MgATP2- plus nitrate
diphosphate
-
mixed-type inhibitor with respect to both MgATP2- and MoO42-
diphosphate
-
noncompetitive with respect to MgATP and sulfate
EDTA
-
inhibits due to chelation of Mg2+
EDTA
-
inhibition is reversed by mn2+, Mg2+, Cu2+, Co2+
FSO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
FSO3-
-
inhibition in absence of 3'-phosphoadenosine-5'-phosphate
FSO3-
Penicillium duponti
-
-
FSO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
FSO3-
-
0.03 mM, 50% inhibition
guanylylsulfate
-
1 mM, in presence of adenylylsulfate about 20% inhibition
inosylylsulfate
-
1 mM, in presence of adenylylsulfate about 20% inhibition
methylene blue
-
inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate; mixed-type with respect to diphosphate
MgATP2-
Brassica capitata
-
-
molybdate
-
N-Acetylimidazole
-
76% of the original activity can be restored by treatment with hydroxylamine
NEM
-
10 mM, inhibits reaction with diphosphate and adenylylsulfate
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
Ni2+
-
2 mM
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
NO3-
-
dead-end inhibitor, competitive with SO42-
NO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
PCMB
-
5 mM, inhibits reaction with diphosphate and adenylylsulfate
Phenylglyoxal
-
3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
phosphate
-
inhibition is enhanced by increasing concentrations of Mg2+
S2O32-
-
noncompetitive mixed-type inhibition with respect to MgATP2-
S2O32-
-
1 mM, 62% inhibition
S2O32-
Penicillium duponti
-
-
S2O32-
-
dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2-
SeO42-
-
competitive inhibition at and above 0.075 mM
SO32-
-
1 mM, 10-25% inhibition
SO42-
-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
SO42-
-
competitive with respect to MoO42-
Sulfide
-
no inhibition
Sulfide
-
4 mM, 65% inhibition
Sulfide
-
inhibitory effect
Tetranitromethane
-
partial
thiosulfate
-
competitive with molybdate and noncompetitive with MgATP
Zn2+
-
inhibitory effect even at concentrations as low as 40 mg/l
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
-
AMP
-
activates
dithiothreitol
activates
S2O32-
-
activates SO42dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
FSO3-
-
activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
additional information
-
enzyme activity is positively correlated with seed yield and influenced by sulfur assimilation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
adenosine 5'-phosphosulfate
Penicillium duponti
-
pH 8.0, 30C
0.0003
adenosine 5'-phosphosulfate
-
pH 8.0, 30C
0.00053
adenosine 5'-phosphosulfate
-
pH 8.0, 30C, cytosolic enzyme
0.001
adenosine 5'-phosphosulfate
-
less than
0.001
adenosine 5'-phosphosulfate
Brassica capitata
-
pH 8.0, 30C
0.00135
adenosine 5'-phosphosulfate
-
-
0.00162
adenosine 5'-phosphosulfate
-
-
0.0037
adenosine 5'-phosphosulfate
-
pH 8.0, 30C, chloroplastic enzyme
0.005
adenosine 5'-phosphosulfate
-
30C
0.0051
adenosine 5'-phosphosulfate
pH 8.0, 37C
0.17
adenosine 5'-phosphosulfate
-
pH 7.5, 85C
0.17
adenosine 5'-phosphosulfate
-
-
0.0045
adenylyl sulfate
ATP synthesis
0.0245
adenylyl sulfate
reverse reaction, ATP synthesis
0.0004
adenylylsulfate
-
pH 8.0, 30C, wild-type enzyme
0.0005
adenylylsulfate
-
pH 8.0, 30C, truncated mutant enzyme del396-573
0.0048
adenylylsulfate
pH 8.0, 30C
0.025
adenylylsulfate
-
pH 7.8, 37C
0.027
ATP
-
pH 8.0, 30C, molybdolysis, truncated mutant enzyme del396-573; pH 8.0, 30C, molybdolysis, wild-type enzyme
0.045
ATP
-
pH 6.0, 40C
0.1
ATP
pH 8.0, 30C, reaction with molybdate
0.15
ATP
pH 8.0, 30C, reaction with sulfate
0.195
ATP
forward reaction, APS synthesis
0.21
ATP
-
pH 8.0, 30C, synthesis of adenylylsulfate, wild-type enzyme
0.26
ATP
-
pH 8.0, 30C
0.35
ATP
-
pH 7.8, 35C
0.38
ATP
-
pH 7.8, 37C
2.6
ATP
-
pH 8.0, 30C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573
0.12
CrO42-
-
30C, pH 8.0
0.16
dATP
-
pH 6.0, 40C
0.84
dATP
-
pH 7.8, 35C
0.00071
diphosphate
Brassica capitata
-
pH 8.0, 30C
0.001
diphosphate
-
pH 8.8, enzyme form ATPSm
0.004
diphosphate
-
pH 8.0, 30C
0.0065
diphosphate
-
pH 8.0, 30C
0.007
diphosphate
-
-
0.0083
diphosphate
-
pH 8.0, 30C
0.0092
diphosphate
-
pH 8.0, 30C, wild-type enzyme
0.017
diphosphate
-
pH 8.0, 30C, cytosolic enzyme
0.018
diphosphate
-
pH 7.8, 37C
0.025
diphosphate
-
pH 8.0, 30C, truncated mutant enzyme del396-573
0.029
diphosphate
ATP synthesis
0.033
diphosphate
-
-
0.0346
diphosphate
pH 8.0, 30C
0.0389
diphosphate
-
pH 7.8, 37C
0.0389
diphosphate
-
30C
0.057
diphosphate
pH 8.0, 30C
0.1
diphosphate
-
pH 8.0, 30C, chloroplastic enzyme
0.13
diphosphate
-
pH 7.5, 85C
0.13
diphosphate
-
-
1
diphosphate
-
pH 8.8, enzyme form ATPSc
1.3
FPO32-
-
pH 8.0, 30C, chloroplastic enzyme
0.0191
magnesium diphosphate
reverse reaction, ATP synthesis
0.0077
MgATP2-
-
pH 8.0, 30C, reaction with CrO42-
0.012
MgATP2-
-
30C, pH 8.0, reaction with CrO42-
0.019
MgATP2-
-
30C, pH 8.0, reaction with SeO42-
0.023
MgATP2-
-
pH 8.0, 30C, reaction with MoO42-
0.03
MgATP2-
Penicillium duponti
-
pH 8.0, 30C, at saturating concentrations of MoO42-
0.031
MgATP2-
-
pH 8.0, 30C, reaction with SeO42-
0.0374
MgATP2-
-
pH 8.0, 30C, reaction with MoO42-
0.045
MgATP2-
-
pH 8.0, 30C, chloroplastic enzyme, reaction with MoO42-
0.046
MgATP2-
-
pH 8.0, 30C, chloroplastic enzyme, reaction with SO42-
0.05
MgATP2-
-
pH 8.0, 30C, at saturating concentrations of MoO42-
0.059
MgATP2-
-
pH 8.0, 30C, reaction with WO42-
0.07
MgATP2-
-
pH 8.0, 30C
0.13
MgATP2-
-
30C, pH 8.0, reaction with MoO42-
0.13
MgATP2-
-
pH 8.0, 30C
0.15
MgATP2-
-
pH 8.0, 30C
0.15
MgATP2-
-
pH 8.0, 30C, cytosolic enzyme, reaction with MoO42-
0.18
MgATP2-
-
pH 8.0, 30C, at saturating concentrations of SO42-
0.19
MgATP2-
Penicillium duponti
-
pH 8.0, 30C, at saturating concentrations of SO42-
0.21
MgATP2-
-
30C, pH 8.0, reaction with SO42-
0.23
MgATP2-
pH 8.0, 30C, reaction with MoO42-
0.24
MgATP2-
-
pH 8.0, 30C, cytosolic enzyme
0.27
MgATP2-
-
30C, pH 8.0, reaction with WO42-
0.31
MgATP2-
Brassica capitata
-
pH 8.0, 30C, SO42- as substrate
0.33
MgATP2-
Brassica capitata
-
pH 8.0, 30C, MoO42- as substrate
0.38
MgATP2-
-
pH 8.0, 30C
0.5
MgATP2-
-
pH 8.0, 30C, chloroplastic enzym, reaction with FPO32-
0.67
MgATP2-
-
-
0.78
MgATP2-
adenylyl sulfate synthesis
1.1
MgATP2-
pH 8.0, 30C, reaction with SO42-
1.3
molybdate
pH 8.0, 30C
0.076
MoO42-
-
pH 8.0, 30C, wild-type enzyme
0.08
MoO42-
Penicillium duponti
-
pH 8.0, 30C
0.093
MoO42-
-
pH 8.0, 30C
0.11
MoO42-
-
pH 8.0, 30C
0.15
MoO42-
pH 8.0, 30C
0.17
MoO42-
-
pH 8.0, 30C
0.24
MoO42-
-
30C, pH 8.0
0.32
MoO42-
-
pH 8.0, 30C, chloroplastic enzyme
0.36
MoO42-
-
pH 8.0, 30C, cytosolic enzyme
0.53
MoO42-
-
pH 8.0, 30C, truncated mutant enzyme del396-573
0.1
SeO42-
-
30C, pH 8.0
0.61
SeO42-
-
pH 7.8, 37C, SeO42dependent ATP-diphosphate exchange reaction
1
SeO42-
-
pH 7.8, 35C
0.18
SO42-
-
30C, pH 8.0
0.2
SO42-
-
pH 6.0, 40C
0.25
SO42-
-
pH 8.0, 30C, chloroplastic enzyme, reaction with SO42-
0.33
SO42-
-
pH 8.0, 30C
0.36
SO42-
-
pH 8.0, 30C
0.5
SO42-
-
pH 8.0, 30C
0.55
SO42-
Penicillium duponti
-
pH 8.0, 30C
0.55
SO42-
-
pH 8.0, 30C
0.87
SO42-
Brassica capitata
-
pH 8.0, 30C
0.87
SO42-
-
cytosolic enzyme; pH 8.0, 30C
2.5
SO42-
-
pH 7.8, 37C, exchange reaction
2.8
SO42-
-
pH 9.0
3.1
SO42-
-
pH 7.8, 35C
3.1
SO42-
-
pH 9.0
3.2
SO42-
-
pH 7.8, 37C, formation of adenylylsulfate
3.3
SO42-
pH 8.0, 30C
0.00211
sulfate
forward reaction, APS synthesis
0.16
sulfate
pH 8.0, 30C
0.29
sulfate
-
pH 8.0, 30C, wild-type enzyme
3.6
sulfate
-
pH 8.0, 30C, truncated mutant enzyme del396-573
17
sulfate
adenylyl sulfate synthesis
0.47
WO42-
-
30C, pH 8.0
0.64
MoO42-
Brassica capitata
-
pH 8.0, 30C
additional information
additional information
-
-
-
additional information
additional information
-
the reaction does not strictly follow Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
36
adenosine 5'-phosphosulfate
Brassica capitata
-
pH 8.0, 30C, synthesis of ATP
24.5
adenylyl sulfate
Glycine max
Q8SAG1
reverse reaction, ATP synthesis
260
adenylyl sulfate
Thiobacillus denitrificans ATCC 25259
Q3SEZ6
ATP synthesis
46.6
adenylylsulfate
Penicillium chrysogenum
-
pH 8.0, 30C, truncated mutant enzyme del396-573; pH 8.0, 30C, wild-type enzyme
1.49
ATP
Glycine max
Q8SAG1
forward reaction, APS synthesis
1.8
ATP
Penicillium chrysogenum
-
pH 8.0, 30C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573
3.13
ATP
Brassica capitata
-
pH 8.0, 30C, synthesis of adenosine 5'-phosphosulfate
10.8
ATP
Penicillium chrysogenum
-
pH 8.0, 30C, synthesis of adenylylsulfate, wild-type enzyme
13.7
ATP
Penicillium chrysogenum
-
pH 8.0, 30C, molybdolysis, truncated mutant enzyme del396-573
24.4
ATP
Penicillium chrysogenum
-
pH 8.0, 30C, molybdolysis, wild-type enzyme
36
ATP
Brassica capitata
-
pH 8.0, 30C, molybdolysis
36
diphosphate
Brassica capitata
-
pH 8.0, 30C, synthesis of ATP
73.3
diphosphate
Penicillium chrysogenum
-
pH 8.0, 30C, truncated mutant enzyme del396-573; pH 8.0, 30C, wild-type enzyme
19.1
magnesium diphosphate
Glycine max
Q8SAG1
reverse reaction, ATP synthesis
13.7
MoO42-
Penicillium chrysogenum
-
pH 8.0, 30C,truncated mutant enzyme del396-573
24.4
MoO42-
Penicillium chrysogenum
-
pH 8.0, 30C, wild-type enzyme
3.13
SO42-
Brassica capitata
-
pH 8.0, 30C, synthesis of adenosine 5'-phosphosulfate
1.8
sulfate
Penicillium chrysogenum
-
pH 8.0, 30C, truncated mutant enzyme del396-573
2.11
sulfate
Glycine max
Q8SAG1
forward reaction, APS synthesis
10.8
sulfate
Penicillium chrysogenum
-
pH 8.0, 30C, wild-type enzyme
23.2
sulfate
Thiobacillus denitrificans ATCC 25259
Q3SEZ6
adenylyl sulfate synthesis
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
3',5'-adenosine diphosphate
-
pH 8.0, 30C, synthesis of ATP
1.3
3',5'-adenosine diphosphate
-
pH 8.0, 30C, molybdolysis
0.0008
3'-phosphoadenosine-5'-phosphate
-
pH 8.0, 30C
0.000057
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30C, competitive with MgATP2-, at 0.1 mM MoO42-
0.000063
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30C, at 0.1 mM MoO42-
0.00007
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30C, competitive with MoO42-, at 0.05 mM MoO42-
0.00008
3'-phosphoadenosine-5'-phosphosulfate
-
pH 8.0, 30C, at 0.05 mM MgATP2-
0.0004
3'-phosphoadenosine-5'-phosphosulfate
-
at 5 mM MgATP2-; pH 8.0, 30C, at 20 mM MoO42-
0.25
adenosine 5'-monosulfate
-
pH 8.0, 30C, molybdolysis
0.42
adenosine 5'-monosulfate
-
pH 8.0, 30C, synthesis of ATP
0.24
adenosine 5'-phosphoramidate
-
pH 8.0, 30C, synthesis of AMP
0.000018
adenosine 5'-phosphosulfate
pH 8.0, 30C
0.00007
adenosine 5'-phosphosulfate
-
pH 8.0, 30C, molybdolysis
0.0015
adenosine 5'-phosphosulfate
Brassica capitata
-
pH 8.0, 30C, product inhibitor
0.04
adenosine 5'-phosphosulfate
-
pH 8.0, 30C
0.3
adenosine 5'-phosphosulfate
-
pH 8.0, 30C
0.06
ADP
-
pH 7.8, 37C
0.087
ADP
-
pH 8.0, 30C, synthesis of ATP
1.15
ADP
-
pH 8.0, 30C
0.165
AMP
-
pH 8.0, 30C, synthesis of AMP
0.55
AMP
-
pH 8.0, 30C
0.6
AMP
-
pH 7.8, 37C
1.6
AMP
-
pH 7.5, 30C
2.1
AMP
-
pH 8.0, 30C
1
ATP
pH 8.0, 30C, reaction with molybdate
1.1
ATP
pH 8.0, 30C, reaction with sulfate
0.0047
beta-fluoro-adenosine 5'-phosphosulfate
-
pH 8.0, 30C, synthesis of ATP
0.005
beta-fluoro-adenosine 5'-phosphosulfate
-
pH 8.0, 30C, molybdolysis
0.0025
beta-methylene-adenosine 5'-phosphosulfate
-
pH 8.0, 30C, ATP synthesis
0.003
beta-methylene-adenosine 5'-phosphosulfate
-
pH 8.0, 30C, molybdolysis
0.033
ClO3-
-
pH 8.0, 30C
0.15
ClO3-
-
pH 8.0, 30C
0.25
ClO3-
-
pH 7.8, 37C
0.3
ClO3-
Brassica capitata
-
pH 8.0, 30C
0.28
ClO4-
-
pH 8.0, 30C
0.001
diphosphate
-
pH 8.0, 30C, at 20 mM SO42- and 5 mM excess Mg2+
0.0034
FSO3-
-
pH 8.0, 30C
0.004
FSO3-
Penicillium duponti
-
pH 8.0, 30C
0.5
FSO3-
-
pH 8.0, 30C
0.33
MgATP2-
-
pH 8.0, 30C
0.385
MgATP2-
-
pH 8.0, 30C, reaction with SeO42- or CrO42-
0.41
MgATP2-
-
pH 8.0, 30C, reaction with SO42-
0.417
MgATP2-
-
pH 8.0, 30C, reaction with MoO42-
0.5
MgATP2-
-
pH 8.0, 30C
0.606
MgATP2-
-
pH 8.0, 30C, reaction with WO42-
0.71
MgATP2-
-
pH 8.0, 30C
0.75 - 1.3
MgATP2-
Brassica capitata
-
pH 8.0, 30C
14.3
molybdate
pH 8.0, 30C
2.02
MoO42-
-
pH 8.0, 30C
0.9
NAD+
-
pH 8.0, 30C, synthesis of ATP
2.5
NAD+
-
pH 8.0, 30C, molybdolysis
0.25
NO3-
-
pH 8.0, 30C
1.2
NO3-
-
pH 8.0, 30C
2.2
NO3-
-
pH 7.8, 37C
0.36
S2O32-
-
pH 8.0, 30C
0.4
S2O32-
Penicillium duponti
-
pH 8.0, 30C
0.4
S2O32-
-
pH 8.0, 30C
1.13
S2O32-
-
pH 8.0, 30C
0.5
SeO42-
-
pH 7.8, 37C
2
SO42-
-
pH 8.0, 30C
1.7
sulfate
pH 8.0, 30C
0.66
Sulfide
-
pH 8.0, 30C
3.4
Sulfide
-
pH 8.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000066
-
formation of adenosine 5'-phosphosulfate
0.000246
-
formation of ATP
0.013
-
purified enzyme has an activity of 0.013-0.016 micromol/min/mg
1.1
-
cell extract
2.9
specific activity for APS synthesis
3.3
Brassica capitata
-
synthesis of adenosine 5'-phosphosulfate
4.3
Brassica capitata
-
Mg-diphosphate-MgATP2-exchange
11.98
ratio AcATPS1-AcAPR1 1:1
12.96
ratio AcATPS1-AcAPR1 1:0; recombinant enzyme, at 25C
15.25
ratio AcATPS1-AcAPR1 1:5, five-fold excess of AcAPR1 slightly increases the activity of AcATPS1
30
Brassica capitata
-
-
31.5
adenylyl sulfate synthesis
38
Brassica capitata
-
molybdolysis, and synthesis of MgATP2-
48.7
specific activity for ATP synthesis
205.2
-
enzyme form ATPSc
237.7
-
enzyme form ATPSm
247
-
cytosolic enzyme
267
-
chloroplastic enzyme
additional information
ATPS activity gradually increases during cold treatment, after 72h at 10C ATPS activity is 2.2fold higher; ATPS activity in stem and leaf tissue are comparable but lower than in seeds and roots; ATPS activity in young seeds is several-folds higher than in any other tissue
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
Tris-MES buffer
7.3
-
enzyme form ATPSc, incorporation of SO42-
7.8 - 8
-
0.1 M phosphate buffer
8
Brassica capitata
-
-
8.8
-
synthesis of ATP, enzyme form ATPSm and ATPSc
8.8
-
and a second but lower optimum at pH 7.3, enzyme form ATPSm, incorporation of SO42-
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 - 8.5
-
about 90% of maximal activity at pH 7.2 and pH 8.5
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
Penicillium chrysogenum, Penicillium duponti
-
in a 20 min assay
30
-
incubation of the bioreactor
46
-
bimodal temperature optima: 46C and 52-54C
90
-
wild-type enzyme
100
-
recombinant enzyme
additional information
-
assay performed at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
-
full activity up to 40C, completely inactive at 55C
30 - 50
-
30C: about 35% of maximal activity, 50C: about 75% of maximal activity
35 - 60
-
35C: about 40% of maximal activity, 60C: about 35% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3 - 4.4
-
isoelectric focusing
5.8
-
isoelectric focusing, enzyme form ATPSm
7.3
predicted from cDNA sequence
7.9
-
isoelectric focusing, enzyme form ATPSc
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
maximal activity in 10-day old culture
Manually annotated by BRENDA team
-
highest activity at the third day after inoculation, declining afterwards to a level found in resting cells
Manually annotated by BRENDA team
Synechococcus sp. 6301
-
highest activity at the third day after inoculation, declining afterwards to a level found in resting cells
-
Manually annotated by BRENDA team
-
PAPSs2 mRNA is highly expressed in duodenum
Manually annotated by BRENDA team
-
PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus; PAPSs2mRNA is expressed in kidney, expression is higher in female than in male mice
Manually annotated by BRENDA team
-
of seedling
Manually annotated by BRENDA team
Brassica capitata
-
-
Manually annotated by BRENDA team
-
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; PAPSs2mRNA is expressed in liver
Manually annotated by BRENDA team
-
PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus; PAPSs2mRNA is expressed in lung
Manually annotated by BRENDA team
-
of seedling
Manually annotated by BRENDA team
ATPS mRNA is most abundant in root tissue, cold treatment induces RNA accumulation and enhances the specific activity of ATPS in root tissue
Manually annotated by BRENDA team
-
root and leaf
Manually annotated by BRENDA team
-
PAPSs2 mRNA is highly expressed in small intestine
Manually annotated by BRENDA team
-
PAPSs2mRNA is expressed in stomach
Manually annotated by BRENDA team
-
PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus
Manually annotated by BRENDA team
additional information
by northern blot analysis a decline in the ATPS transcript level during seed development can be found
Manually annotated by BRENDA team
additional information
-
PAPSs2 mRNA is not detectable in brain, gonads, placenta or uterus
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
stroma, ATP sulfurylase isoenzymes exist in chloroplast and in cytosol
Manually annotated by BRENDA team
isoform PAPSS2 is localised mainly within the cytoplasm
Manually annotated by BRENDA team
-
ATP sulfurylase isoenzymes exist in chloroplast and in cytosol
Manually annotated by BRENDA team
-
enzyme form ATPSm is mainly associated with mitochondrial membrane
Manually annotated by BRENDA team
isoform PAPSS1 is predominantly nuclear
Manually annotated by BRENDA team
-
enzyme form ATPSc
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Human immunodeficiency virus type 1 group M subtype B
Pseudomonas syringae pv. tomato (strain DC3000)
Riftia pachyptila sulfur-oxidizing endosymbiont
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40540
isozyme APS1, calculated from sequence of cDNA
694749
42000
-
gel filtration
643279
47000
-
-
690263
50000
SDS-PAGE; SDS-PAGE and gel filtration
673697
51780
isozyme APS2, calculated from sequence of cDNA
694749
51810
calculated from sequence of cDNA
673697
52000
predicted from cDNA sequence, enzyme functions as a 100 kDa homodimer
671601
61100
recombinant isozyme APS1, SDS-PAGE
694749
66000
-
enzyme ATPSm and ATPSc, gel filtration
643278
70200
recombinant isozyme APS2, SDS-PAGE
694749
85000
-
gel filtration
643274
100000
-
gel filtration
643292
108000
Brassica capitata
-
glycerol density gradient centrifugation
643280
122000
-
gel filtration
641204
133000
isoform PAPSS1, gel filtration
723546
138000
-
gel filtration
643294
150000
-
gel filtration
643275, 643291
151000
-
gel filtration
643294
160000
-
non-denaturing PAGE
643263
170000
-
gel filtration
643282
260000
-
gel filtration
643263
260000
gel filtration
643286
290000
-
gel filtration
643276
410000
-
gel filtration
643259
420000 - 440000
-
-
643252
440000
Penicillium chrysogenum, Penicillium duponti
-
gel filtration
641208
470000
-
recombinant enzyme, gel filtration
643290
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
643293
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
671601
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 65000, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
-
x * 67000, SDS-PAGE
?
Penicillium duponti
-
x * 66000, SDS-PAGE
?
-
x * 62000, SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 35000-37000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
dimer
-
2 * 41000-44000, two bands of 41000 Da and of 44000 Da, SDS-PAGE
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
-
2 * 57000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
Geobacillus stearothermophilus NCA 1503
-
2 * 44000, SDS-PAGE
-
dimer
Synechococcus sp. 6301
-
2 * 41000-44000, two bands of 41000 Da and of 44000 Da, SDS-PAGE
-
hexamer
-
6 * 69000, SDS-PAGE
hexamer
-
wild-type enzyme
homodimer
enzyme functions as a 2 * 50000 Da homodimer
homodimer
-
x-ray crystallography
monomer
-
1 * 52300, enzyme form ATPSc, SDS-PAGE; 1 * 55000, enzyme form ATPSm, SDS-PAGE
monomer
-
1 * 46000,truncated mutant enzyme del396-573, SDS-PAGE
monomer
-
1 * 47000
octamer
-
8 * 56000
octamer
-
8 * 59300, SDS-PAGE
tetramer
-
4 * 49000, chloroplastic enzyme, SDS-PAGE; 4 * 50000, cytosolic enzyme, SDS-PAGE
tetramer
4 * 62800, calculation from amino acid sequence
trimer
-
alpha2beta, 2 * 50000 + 1 * 53000, SDS-PAGE
trimer
-
3 * 47100, electrospray mass spectrometry
trimer
-
3 * 48000-50000, electrospray mass spectrometry
monomer
-
1 * 60490, calculated from amino acid sequence; 1 * 64500, recombinant enzyme, SDS-PAGE
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
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
-
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop vapor diffusion at 25C 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
-
recombinant enzyme expressed in Escherichia coli, crystals are grown at 22C 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 4C
-
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
crystal structure of the enzyme in complex with adenosine 5'-phosphate is determined at 2.5 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4
Penicillium chrysogenum, Penicillium duponti
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
641208
7.8
-
unstable in Tris, diethylbarbiturate, glycine, triethanolamine and bicarbonate buffer, but stable in phosphate buffers of the same pH
643259
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
2 h, wild-type enzyme and individually expressed ATP sulfurylase domain of the bifunctional are stable
641225
37
-
2 h, wild-type enzyme is stable, individually expressed ATP sulfurylase domain of the bifunctional enzyme loses 98% of its activity
641225
45
-
t1/2 for mutant enzyme del396-573: 1.5 min
662282
50
-
stable for 5 min
643252
50
-
rapid inactivation
643255
50
-
t1/2 for mutant enzyme del396-573: 0.3 min, wild-type enzyme is stable for more than 2 h
662282
55
-
5 min, 50% loss of activity
643252
60
-
stable for 10 min
643252
62
-
t1/2 for wild-type enzyme: 1.5 min
662282
65
Penicillium chrysogenum, Penicillium duponti
-
enzyme of Penicillium chrysogenum denaturates with a rate constant nearly 100fold greater than that of the Penicillium duponti enzyme
641208
70
-
15 min, stable below. 20% loss of activity after 1 h
643292
75
-
1 min, complete loss of activity
643281
90
half-life: more than 1 h
643286
100
-
2 min, complete inactivation
643273
100
-
1 min, complete inactivation
643279
additional information
-
Q10 is 1.85 between 30C and 40C
643252
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
643288
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
675422
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing inactivates the purified enzyme
-
5C, enzyme solution with 5-10 mg/ml, stable for several months
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
not stable to freezing and thawing
-
643259
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-6C, enzyme is stable for over 21 days
-
4C, 50 mM MOPS buffer, pH 7.4, 0.2 mM CoCl2, 0.2 mM ZnCl2, stable for 48 h
-
0-4C, purified enzyme solution, 1 mg protein per ml, 15% loss of activity after 5 weeks
-
-15C, stable for at least 4 months
-
-15C, 80% loss of activity within 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed enzyme is purified by affinity chromatography using glutathione-Sepharose and subsequent ion-exchange chromatography; glutathione-Sepharose column chromatography and Mono Q column chromatography
hydroxyapatite column chromatography, DEAE cellulose column chromatography, and gel filtration; protein is purified by sequential chromatographies on hydroxyapatite, DEAE cellulose and gel filtration
-
recombinant enzyme
-
-
Brassica capitata
-
DEAE-52 cellulose column chromatography, Source 15Q column chromatography, Superdex 200 gel filtration, and hydroxyapatite column chromatography
-
enzyme form ATPSm and ATPSc
-
N-terminal His-tagged protein is passed over a Ni2+-NTA column
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
-
glutathione Sepharose column chromatography and Superdex 200 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
-
recombinant enzyme
-
a chloroplastic and a cytosolic enzyme form
-
immobilized metal ion affinity chromatography
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21Star (DE3) cells
-
cloned in Escherichia coli; expressed in Escherichia coli BL21 cells
Aquifex aeolicus ATP-sulfurylase-APS kinase is expressed in an Escherichia coli pET vector expression system; expressed in Escherichia coli
-
expression in Escherichia coli BL-21
overexpression in Eacherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells; expressed in Escherichia coli BL21 (DE3) cells; expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli
-
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; 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
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed
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isoform PAPS synthase 1 wild type and mutant proteins are expressed in Escherichia coli
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
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truncated enzyme form
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expressed in Escherichia coli BL21-DE3
cloned in Escherichia coli BL-21
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ATP sulfurylase cDNA from MET3 on chromosome X is amplified and expressed in Escherichia coli XL1-Blue. The synthesis of the enzyme is directed by an expression system that employs the regulatory genes of Vibrio fischeri
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His-tag version expressed in Escherichia coli BL21-DE3
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C53A
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mutation has no effect on activity
C77A
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mutation has no effect on activity
C84A
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mutation has no effect on activity
D523A
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no sulfurylase activity, reduced PAPS kinase activity
G59A
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significant effect on ATP sulfurylase activity, no effect on adenosine 5'-phosphosulfate kinase activity
G62A
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mutation has no effect on activity
G64A
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diminished adenosine 5'-phosphosulfate kinase activity
H425A
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no sulfurylase activity
H428A
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no sulfurylase activity
H506A
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mutant enzyme shows 91% of the sulfurylase activity compared to that of the wild-type enzyme, reduced PAPS kinase activity
K65A
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mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
K65R
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mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
R421A
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no sulfurylase activity
R421K
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mutant enzyme shows 8% of the sulfurylase activity compared to that of the wild-type enzyme
R468A
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no sulfurylase activity
R510A
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mutant enzyme shows 90% of the sulfurylase activity compared to that of the wild-type enzyme
R522A
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no sulfurylase activity
R522K
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no sulfurylase activity
T66A
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mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact
del396-573
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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
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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overexpression of ATP sulfurylase may be a promising approach to create plants with enhanced phytoextraction capacity for mixtures of metals
agriculture
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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