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ATP + chromate
diphosphate + adenylyl chromate
ATP + CrO42-
AMP + adenylyl-chromate
ATP + fluorophosphate
diphosphate + adenylyl fluorophosphate
-
-
-
-
r
ATP + molybdate
diphosphate + adenylyl molybdate
ATP + MoO42-
AMP + adenylylmolybdate
ATP + selenate
diphosphate + adenylyl selenate
ATP + SeO42-
AMP + adenylylselenate
ATP + sulfate
adenylyl sulfate + diphosphate
-
-
-
-
?
ATP + sulfate
ADP + adenylyl sulfate
ATP + sulfate
diphosphate + adenylyl sulfate
ATP + sulfate
diphosphate + adenylylsulfate
ATP + tungstate
diphosphate + adenylyl tungstate
ATP + WO42-
AMP + adenylyl-wolframate
dATP + SO42-
diphosphate + deoxyadenylylsulfate
diphosphate + adenylyl sulfate
ATP + sulfate
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
additional information
?
-
ATP + chromate

diphosphate + adenylyl chromate
-
-
-
-
r
ATP + chromate
diphosphate + adenylyl chromate
-
-
-
-
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
-
-
-
-
?
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 + molybdate

diphosphate + adenylyl molybdate
Brassica capitata
-
-
-
-
r
ATP + molybdate
diphosphate + adenylyl molybdate
-
-
-
-
r
ATP + molybdate
diphosphate + adenylyl molybdate
Penicillium duponti
-
-
-
-
r
ATP + molybdate
diphosphate + adenylyl molybdate
-
-
-
-
r
ATP + molybdate
diphosphate + adenylyl molybdate
-
-
-
-
r
ATP + MoO42-

AMP + adenylylmolybdate
-
-
-
?
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
Brassica capitata
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
-
-
r
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
Penicillium duponti
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 + selenate

diphosphate + adenylyl selenate
-
-
-
-
r
ATP + selenate
diphosphate + adenylyl selenate
-
-
-
-
r
ATP + SeO42-

AMP + adenylylselenate
-
-
-
-
?
ATP + SeO42-
AMP + adenylylselenate
-
-
-
-
?
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 + SeO42-
AMP + adenylylselenate
-
-
-
-
?
ATP + sulfate

ADP + adenylyl sulfate
-
-
-
r
ATP + sulfate
ADP + adenylyl sulfate
-
-
-
?
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
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
Brassica capitata
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
reaction is carried out in an anaerobic bioreactor
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
Penicillium duponti
-
-
-
-
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 + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate

diphosphate + adenylylsulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
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
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
Brassica capitata
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
?
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
-
-
-
-
r
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
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
enzyme plays a crucial role in sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
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
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate metabolism
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
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
Penicillium duponti
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
Penicillium duponti
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
first enzyme of the two-step sulfate activation sequence
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
key enzyme of sulfate assimilation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
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 + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + tungstate

diphosphate + adenylyl tungstate
-
-
-
-
r
ATP + tungstate
diphosphate + adenylyl tungstate
-
-
-
-
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
-
-
-
-
?
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
-
-
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
-
-
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
-
-
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
-
-
-
-
?
diphosphate + adenylyl sulfate

ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
diphosphate in form of magnesium diphosphate
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
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 SeO42âdependent 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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + sulfate
ADP + adenylyl sulfate
ATP + sulfate
diphosphate + adenylyl sulfate
ATP + sulfate
diphosphate + adenylylsulfate
diphosphate + adenylyl sulfate
ATP + sulfate
additional information
?
-
ATP + sulfate

ADP + adenylyl sulfate
-
-
-
r
ATP + sulfate
ADP + adenylyl sulfate
-
-
-
?
ATP + sulfate

diphosphate + adenylyl sulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
r
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
-
?
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
-
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
enzyme plays a crucial role in sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate metabolism
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the ATP sulfurylase-adenylylsulfate complex does not serve as a substrate for APS kinase, i.e. there is no substrate chanelling of APS between the two sulfate-activating enzymes
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
first enzyme of the two-step sulfate activation sequence
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
key enzyme of sulfate assimilation
-
-
r
diphosphate + adenylyl sulfate

ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid
-
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
3'-phosphoadenosine-5'-phosphosulfate
3,5-di-tert-butyl-4-hydroxytoluene
-
-
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
adenosine 5'-monosulfate
-
-
adenosine 5'-phosphoramidate
-
-
adenosine 5'-phosphosulfate
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
beta-fluoro-adenosine 5'-phosphosulfate
-
-
beta-methylene-adenosine 5'-phosphosulfate
-
-
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
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
N-Acetylimidazole
-
76% of the original activity can be restored by treatment with hydroxylamine
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+
SO32-
-
1 mM, 10-25% inhibition
Tetranitromethane
-
partial
thiosulfate
competitive with molybdate and noncompetitive with MgATP
Tris-malic acid-KOH buffer
-
Zn2+
-
inhibitory effect even at concentrations as low as 40 mg/l
3'-phosphoadenosine-5'-phosphate

-
strong
3'-phosphoadenosine-5'-phosphate
-
strong
3'-phosphoadenosine-5'-phosphate
-
strong
3'-phosphoadenosine-5'-phosphate
allosteric
3'-phosphoadenosine-5'-phosphate
Penicillium duponti
-
strong
3'-phosphoadenosine-5'-phosphate
-
-
3'-phosphoadenosine-5'-phosphate
-
-
3'-phosphoadenosine-5'-phosphosulfate

-
-
3'-phosphoadenosine-5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate

Brassica capitata
-
-
adenosine 5'-phosphosulfate
competitive with ATP and molybdate
adenosine 5'-phosphosulfate
-
potent product inhibition, competitive with both MgATP2- and MoO42- in molybdolysis assay
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
competitive with both substrates
adenosine 5'-phosphosulfate
-
potent product inhibitor, competitive with respect to MgATP2-, and a mixed type inhibitor with respect to molybdate
adenosine 5'-phosphosulfate
-
1 mM, 30% inhibition
adenosine 5'-phosphosulfate
-
-
adenosine 5'-phosphosulfate
-
1 mM, 90% inhibition
adenosine 5'-phosphosulfate
-
inhibits molybdolysis
ADP

-
-
ADP
-
linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP
AMP

-
-
AMP
-
competitive with MgATP2- and mixed-type with respect to SO42-
AMP
-
linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP
ATP

-
free 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
Ca2+

-
-
ClO3-

-
ClO3-
Brassica capitata
-
-
ClO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
ClO4-

competitive with sulfate and adenylyl sulfate
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
Cys

-
2 mM, slight
diphosphate

noncompetitive with respect to MgATP and sulfate
diphosphate
-
mixed-type inhibitor with respect to both MgATP2- and MoO42-
EDTA

-
inhibition is reversed by mn2+, Mg2+, Cu2+, Co2+
EDTA
-
inhibits due to chelation of Mg2+
FSO3-

-
FSO3-
-
inhibition in absence of 3'-phosphoadenosine-5'-phosphate
FSO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
FSO3-
0.03 mM, 50% inhibition
FSO3-
Penicillium duponti
-
-
FSO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
iodoacetic acid

-
Met

-
2 mM, slight
MgATP2-

Brassica capitata
-
-
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate; mixed-type with respect to diphosphate
N-ethylmaleimide

-
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
NEM
-
10 mM, inhibits reaction with diphosphate and adenylylsulfate
NO3-

-
NO3-
-
dead-end inhibitor, competitive with SO42-
NO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
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-

-
-
S2O32-
-
1 mM, 62% inhibition
S2O32-
-
dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2-
S2O32-
Penicillium duponti
-
-
S2O32-
-
noncompetitive mixed-type inhibition with respect to MgATP2-
SeO42-

-
-
SeO42-
-
competitive inhibition at and above 0.075 mM
SO42-

-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
SO42-
-
competitive with respect to MoO42-
Sulfide

-
inhibitory effect
Sulfide
-
4 mM, 65% inhibition
Tris-malic acid-KOH buffer

-
pH 6-8.5
-
Tris-malic acid-KOH buffer
-
pH 6-8.5
-
Tris-malic acid-KOH buffer
-
pH 6-8.5
-
Tris-malic acid-KOH buffer
-
pH 6-8.5
-
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Alcohol-Related Disorders
Rate of alcoholism diagnoses in community mental health centers: the effect of the presence of an alcoholism treatment program.
Anovulation
Inactivating PAPSS2 mutations in a patient with premature pubarche.
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.
Heart Diseases
Lipid metabolism in the heart--contribution of BMIPP to the diseased heart.
Hepatitis C
A continuous nonradioactive assay for RNA-dependent RNA polymerase activity.
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.
Malaria
Single-step, paper-based concentration and detection of a malaria biomarker.
Mastocytoma
Activation of mouse mastocytoma ATP sulfurylase by p-hydroxymercuribenzoate.
Mastocytoma
Enzyme-substrate complexes of ATP-sulfurylase from mouse mastocytoma.
Mastocytoma
Purification and properties of ATP-sulfurylase from Furth mouse mastocytoma.
Mastocytoma
Two forms of ATP sulfurylase in Furth mouse mastocytoma.
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
Interfacial Tension Effect on Cell Partition in Aqueous Two-Phase Systems.
Neoplasms
Molecular determinants as therapeutic targets in cancer chemotherapy: An update.
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
Cysteine biosynthetic enzymes are the pieces of a metabolic energy pump.
Stroke
Mechanochemistry of a viral DNA packaging motor.
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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0.0003 - 0.17
adenosine 5'-phosphosulfate
0.0044 - 2.95
adenylyl sulfate
0.0004 - 0.025
adenylylsulfate
0.12
CrO42-
-
30°C, pH 8.0
0.00071 - 19.41
diphosphate
1.3
FPO32-
-
pH 8.0, 30°C, chloroplastic enzyme
1.3
molybdate
pH 8.0, 30°C
0.47
WO42-
-
30°C, pH 8.0
additional information
additional information
-
0.0003
adenosine 5'-phosphosulfate

-
pH 8.0, 30°C
0.0003
adenosine 5'-phosphosulfate
Penicillium duponti
-
pH 8.0, 30°C
0.00053
adenosine 5'-phosphosulfate
-
pH 8.0, 30°C, cytosolic enzyme
0.001
adenosine 5'-phosphosulfate
Brassica capitata
-
pH 8.0, 30°C
0.001
adenosine 5'-phosphosulfate
-
less than
0.00135
adenosine 5'-phosphosulfate
-
-
0.00162
adenosine 5'-phosphosulfate
-
-
0.0037
adenosine 5'-phosphosulfate
-
pH 8.0, 30°C, chloroplastic enzyme
0.005
adenosine 5'-phosphosulfate
-
30°C
0.0051
adenosine 5'-phosphosulfate
pH 8.0, 37°C
0.17
adenosine 5'-phosphosulfate
-
-
0.17
adenosine 5'-phosphosulfate
-
pH 7.5, 85°C
0.0044
adenylyl sulfate

pH 8.0, 25°C, recombinant mutant H255A
0.0045
adenylyl sulfate
ATP synthesis
0.0065
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant N249D
0.0095
adenylyl sulfate
recombinant enzyme, pH 8.0, 30°C
0.0127
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H333Q
0.0226
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H255Q
0.0245
adenylyl sulfate
reverse reaction, ATP synthesis
0.0247
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant F245L
0.0272
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H252D
0.0282
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant L258A
0.0342
adenylyl sulfate
pH 8.0, 25°C, recombinant wild-type enzyme
0.0346
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant R349K
0.0363
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant F245A
0.0385
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant L258V
0.0402
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246A
0.0432
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant N249A
0.045
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246N
0.047
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant R248K
0.312
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246E
2.69
adenylyl sulfate
-
pH 8.0, 35°C
2.95
adenylyl sulfate
-
pH 8.0, 35°C
0.0004
adenylylsulfate

pH 8.0, 30°C, wild-type enzyme
0.0005
adenylylsulfate
pH 8.0, 30°C, truncated mutant enzyme del396-573
0.0048
adenylylsulfate
pH 8.0, 30°C
0.025
adenylylsulfate
-
pH 7.8, 37°C
0.0077
ATP

-
pH 8.0, 30°C, reaction with CrO42-
0.0077
ATP
-
ATP in form of MgATP2-
0.012
ATP
-
30°C, pH 8.0, reaction with CrO42-
0.012
ATP
-
ATP in form of MgATP2-
0.019
ATP
-
30°C, pH 8.0, reaction with SeO42-
0.019
ATP
-
ATP in form of MgATP2-
0.023
ATP
-
pH 8.0, 30°C, reaction with MoO42-
0.023
ATP
-
ATP in form of MgATP2-
0.027
ATP
pH 8.0, 30°C, molybdolysis, truncated mutant enzyme del396-573
0.027
ATP
pH 8.0, 30°C, molybdolysis, wild-type enzyme
0.03
ATP
Penicillium duponti
-
pH 8.0, 30°C, at saturating concentrations of MoO42-
0.03
ATP
Penicillium duponti
-
ATP in form of MgATP2-
0.031
ATP
-
pH 8.0, 30°C, reaction with SeO42-
0.031
ATP
-
ATP in form of MgATP2-
0.0374
ATP
-
pH 8.0, 30°C, reaction with MoO42-
0.0374
ATP
-
ATP in form of MgATP2-
0.045
ATP
-
pH 8.0, 30°C, chloroplastic enzyme, reaction with MoO42-
0.045
ATP
-
pH 6.0, 40°C
0.045
ATP
-
ATP in form of MgATP2-
0.046
ATP
-
pH 8.0, 30°C, chloroplastic enzyme, reaction with SO42-
0.046
ATP
-
ATP in form of MgATP2-
0.05
ATP
-
pH 8.0, 30°C, at saturating concentrations of MoO42-
0.05
ATP
-
ATP in form of MgATP2-
0.059
ATP
-
pH 8.0, 30°C, reaction with WO42-
0.059
ATP
-
ATP in form of MgATP2-
0.07
ATP
-
ATP in form of MgATP2-
0.1
ATP
pH 8.0, 30°C, reaction with molybdate
0.13
ATP
-
30°C, pH 8.0, reaction with MoO42-
0.13
ATP
-
ATP in form of MgATP2-
0.13
ATP
-
ATP in form of MgATP2-
0.15
ATP
-
pH 8.0, 30°C, cytosolic enzyme, reaction with MoO42-
0.15
ATP
pH 8.0, 30°C, reaction with sulfate
0.15
ATP
-
ATP in form of MgATP2-
0.15
ATP
-
ATP in form of MgATP2-
0.18
ATP
-
pH 8.0, 30°C, at saturating concentrations of SO42-
0.18
ATP
-
ATP in form of MgATP2-
0.19
ATP
Penicillium duponti
-
pH 8.0, 30°C, at saturating concentrations of SO42-
0.19
ATP
Penicillium duponti
-
ATP in form of MgATP2-
0.195
ATP
forward reaction, APS synthesis
0.21
ATP
-
30°C, pH 8.0, reaction with SO42-
0.21
ATP
pH 8.0, 30°C, synthesis of adenylylsulfate, wild-type enzyme
0.21
ATP
-
ATP in form of MgATP2-
0.24
ATP
-
pH 8.0, 30°C, cytosolic enzyme
0.24
ATP
-
ATP in form of MgATP2-
0.27
ATP
-
30°C, pH 8.0, reaction with WO42-
0.27
ATP
-
ATP in form of MgATP2-
0.31
ATP
Brassica capitata
-
pH 8.0, 30°C, SO42- as substrate
0.31
ATP
Brassica capitata
-
ATP in form of MgATP2-
0.33
ATP
Brassica capitata
-
pH 8.0, 30°C, MoO42- as substrate
0.33
ATP
Brassica capitata
-
ATP in form of MgATP2-
0.38
ATP
-
ATP in form of MgATP2-
0.5
ATP
-
pH 8.0, 30°C, chloroplastic enzym, reaction with FPO32-
0.5
ATP
-
ATP in form of MgATP2-
0.67
ATP
-
ATP in form of MgATP2-
2.6
ATP
pH 8.0, 30°C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573
0.16
dATP

-
pH 6.0, 40°C
0.84
dATP
-
pH 7.8, 35°C
0.00071
diphosphate

Brassica capitata
-
pH 8.0, 30°C
0.001
diphosphate
-
pH 8.8, enzyme form ATPSm
0.004
diphosphate
-
pH 8.0, 30°C
0.0065
diphosphate
-
pH 8.0, 30°C
0.0083
diphosphate
-
pH 8.0, 30°C
0.0092
diphosphate
pH 8.0, 30°C, wild-type enzyme
0.017
diphosphate
-
pH 8.0, 30°C, cytosolic enzyme
0.018
diphosphate
-
pH 7.8, 37°C
0.0191
diphosphate
reverse reaction, ATP synthesis
0.0191
diphosphate
diphosphate in form of magnesium diphosphate
0.022
diphosphate
pH 8.0, 25°C, recombinant mutant H333Q
0.025
diphosphate
pH 8.0, 30°C, truncated mutant enzyme del396-573
0.029
diphosphate
ATP synthesis
0.0346
diphosphate
pH 8.0, 30°C
0.0389
diphosphate
-
30°C
0.0389
diphosphate
-
pH 7.8, 37°C
0.0399
diphosphate
pH 8.0, 25°C, recombinant mutant H255A
0.0458
diphosphate
pH 8.0, 25°C, recombinant wild-type enzyme
0.0476
diphosphate
recombinant enzyme, pH 8.0, 30°C
0.0556
diphosphate
pH 8.0, 25°C, recombinant mutant Q246N
0.057
diphosphate
pH 8.0, 30°C
0.0694
diphosphate
pH 8.0, 25°C, recombinant mutant N249D
0.085
diphosphate
pH 8.0, 25°C, recombinant mutant H252D
0.1
diphosphate
-
pH 8.0, 30°C, chloroplastic enzyme
0.114
diphosphate
pH 8.0, 25°C, recombinant mutant H255Q
0.117
diphosphate
pH 8.0, 25°C, recombinant mutant Q246A
0.118
diphosphate
pH 8.0, 25°C, recombinant mutant F245L
0.13
diphosphate
-
pH 7.5, 85°C
0.153
diphosphate
pH 8.0, 25°C, recombinant mutant F245A
0.208
diphosphate
pH 8.0, 25°C, recombinant mutant L258V
0.373
diphosphate
pH 8.0, 25°C, recombinant mutant L258A
0.428
diphosphate
pH 8.0, 25°C, recombinant mutant R248K
0.59
diphosphate
pH 8.0, 25°C, recombinant mutant R349K
0.611
diphosphate
pH 8.0, 25°C, recombinant mutant Q246E
1
diphosphate
-
pH 8.8, enzyme form ATPSc
1.078
diphosphate
pH 8.0, 25°C, recombinant mutant N249A
11.07
diphosphate
-
pH 8.0, 35°C
19.41
diphosphate
-
pH 8.0, 35°C
0.23
MgATP2-

pH 8.0, 30°C, reaction with MoO42-
0.78
MgATP2-
adenylyl sulfate synthesis
1.1
MgATP2-
pH 8.0, 30°C, reaction with SO42-
0.076
MoO42-

pH 8.0, 30°C, wild-type enzyme
0.08
MoO42-
Penicillium duponti
-
pH 8.0, 30°C
0.093
MoO42-
-
pH 8.0, 30°C
0.11
MoO42-
-
pH 8.0, 30°C
0.15
MoO42-
pH 8.0, 30°C
0.17
MoO42-
-
pH 8.0, 30°C
0.24
MoO42-
-
30°C, pH 8.0
0.32
MoO42-
-
pH 8.0, 30°C, chloroplastic enzyme
0.36
MoO42-
-
pH 8.0, 30°C, cytosolic enzyme
0.53
MoO42-
pH 8.0, 30°C, truncated mutant enzyme del396-573
0.64
MoO42-
Brassica capitata
-
pH 8.0, 30°C
0.1
SeO42-

-
30°C, pH 8.0
0.61
SeO42-
-
pH 7.8, 37°C, SeO42âdependent ATP-diphosphate exchange reaction
0.18
SO42-

-
30°C, pH 8.0
0.2
SO42-
-
pH 6.0, 40°C
0.25
SO42-
-
pH 8.0, 30°C, chloroplastic enzyme, reaction with SO42-
0.33
SO42-
-
pH 8.0, 30°C
0.36
SO42-
-
pH 8.0, 30°C
0.5
SO42-
-
pH 8.0, 30°C
0.55
SO42-
-
pH 8.0, 30°C
0.55
SO42-
Penicillium duponti
-
pH 8.0, 30°C
0.87
SO42-
-
cytosolic enzyme
0.87
SO42-
-
pH 8.0, 30°C
0.87
SO42-
Brassica capitata
-
pH 8.0, 30°C
2.5
SO42-
-
pH 7.8, 37°C, exchange reaction
3.1
SO42-
-
pH 7.8, 35°C
3.2
SO42-
-
pH 7.8, 37°C, formation of adenylylsulfate
0.00211
sulfate

forward reaction, APS synthesis
0.16
sulfate
pH 8.0, 30°C
0.29
sulfate
pH 8.0, 30°C, wild-type enzyme
2.93
sulfate
-
pH 8.0, 35°C
3.13
sulfate
-
pH 8.0, 35°C
3.6
sulfate
pH 8.0, 30°C, truncated mutant enzyme del396-573
17
sulfate
adenylyl sulfate synthesis
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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
-
additional information
additional information
-
the Michaelis constants are 1.55-2.29 mM for corrosive and 2.93-3.13 mM for intestinal bacteria strains
-
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