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ATP + sulfate = diphosphate + adenylyl sulfate
ATP + sulfate = diphosphate + adenylyl sulfate

obligatory ordered kinetic mechanism with MgATP2- adding before MoO42- or SO42- and Mg-diphosphate leaving before AMP + MoO42- or adenosine 5'-phosphosulfate
Brassica capitata
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
sequential reaction mechanism in which both substrates bind before any product is released
-
ATP + sulfate = diphosphate + adenylyl sulfate
sequential bi-bi reaction with ATP being the first substrate bound and adenylysulfate the last product released
-
ATP + sulfate = diphosphate + adenylyl sulfate
random sequence for the forward reaction with adenylylsulfate release being partially rate limiting
-
ATP + sulfate = diphosphate + adenylyl sulfate
analysis of the bi bi substrate kinetic mechanism of GmATPS1. The enzyme shows a kinetic mechanism in which ATP and APS are the first substrates bound in the forward and reverse reactions, respectively
ATP + sulfate = diphosphate + adenylyl sulfate
reaction mechanism in which nucleophilic attack by sulfate on the alpha-phosphate of ATP involves transition state stabilization by Arg248, Asn249, His255, and Arg349. ATP sulfurylase overcomes the energetic barrier of APS synthesis by distorting nucleotide structure, identification of critical residues for catalysis, overview
ATP + sulfate = diphosphate + adenylyl sulfate
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ATP + chromate
diphosphate + adenylyl chromate
ATP + CrO42-
AMP + adenylyl-chromate
ATP + fluorophosphate
diphosphate + adenylyl fluorophosphate
-
-
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r
ATP + molybdate
diphosphate + adenylyl molybdate
ATP + MoO42-
AMP + adenylylmolybdate
ATP + selenate
diphosphate + adenylyl selenate
ATP + SeO42-
AMP + adenylylselenate
ATP + sulfate
adenylyl sulfate + diphosphate
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-
-
-
?
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
-
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r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
-
reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
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r
MgATP2- + sulfate
Mg-diphosphate + adenylyl sulfate
-
-
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r
additional information
?
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ATP + chromate

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

diphosphate + adenylyl molybdate
Brassica capitata
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r
ATP + molybdate
diphosphate + adenylyl molybdate
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-
-
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r
ATP + molybdate
diphosphate + adenylyl molybdate
Penicillium duponti
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-
-
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r
ATP + molybdate
diphosphate + adenylyl molybdate
-
-
-
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r
ATP + molybdate
diphosphate + adenylyl molybdate
-
-
-
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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
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-
-
-
?
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
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-
?
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
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-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
mechanism of molybdolysis is a sequential type in which MgATP2- binds to the enzyme before molybdate
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?
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
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-
?
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
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?
ATP + MoO42-
AMP + adenylylmolybdate
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?
ATP + MoO42-
AMP + adenylylmolybdate
-
-
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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
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?
ATP + MoO42-
AMP + adenylylmolybdate
Penicillium duponti
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-
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?
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
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-
?
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
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-
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-
r
ATP + selenate
diphosphate + adenylyl selenate
-
-
-
-
r
ATP + SeO42-

AMP + adenylylselenate
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-
-
-
?
ATP + SeO42-
AMP + adenylylselenate
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-
-
-
?
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
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-
?
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
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?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
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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
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-
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
-
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?
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
-
-
-
-
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
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
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?
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
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r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
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r