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 hide
2.7.7.4
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RECOMMENDED NAME
GeneOntology No.
sulfate adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
selenate reduction
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sulfate activation for sulfonation
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sulfate reduction II (assimilatory)
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sulfate reduction III (assimilatory)
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sulfate reduction IV (dissimilatory, to hydrogen sufide))
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sulfate reduction V (dissimilatory, to thiosulfate)
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sulfite oxidation III
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sulfate reduction
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Purine metabolism
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Monobactam biosynthesis
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Selenocompound metabolism
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Sulfur metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
ATP:sulfate adenylyltransferase
The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).
CAS REGISTRY NUMBER
COMMENTARY hide
9012-39-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
animal
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Columbi aecotype
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Brassica capitata
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Manually annotated by BRENDA team
strain Cm
SwissProt
Manually annotated by BRENDA team
strain Cm
SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
cress
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
mixed SRB (sulfate reducing bacteria)-containing consortium consisting mainly of the Desulfovibrio genus
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain NCA 1503
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Penicillium duponti
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
protozoa
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Sacardo, strongly sulfite producing strain
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Manually annotated by BRENDA team
Sacardo, strongly sulfite producing strain
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Manually annotated by BRENDA team
shrimp
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
6301
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Manually annotated by BRENDA team
6301
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
yeasts
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Automatic Mining of ENzyme DAta
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + CrO42-
AMP + adenylyl-chromate
show the reaction diagram
ATP + FPO32-
?
show the reaction diagram
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-
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
show the reaction diagram
ATP + SeO42-
AMP + adenylylselenate
show the reaction diagram
ATP + sulfate
adenylyl sulfate + diphosphate
show the reaction diagram
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-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
show the reaction diagram
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
ATP + WO42-
AMP + adenylyl-wolframate
show the reaction diagram
dATP + SO42-
diphosphate + deoxyadenylylsulfate
show the reaction diagram
MgATP2- + adenylyl sulfate
MgADP- + 3-phosphoadenylyl sulfate
show the reaction diagram
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reaction carried out by the APS kinase activity of the bifunctional enzyme
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r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
show the reaction diagram
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reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
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r
MgATP2- + sulfate
Mg-diphosphate + adenylyl sulfate
show the reaction diagram
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r
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylylsulfate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
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stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Cobalt
Fe2+
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stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
SO42-
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stimulatory to ATPS
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-adenosine diphosphate
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3'-phosphoadenosine 5'-phosphosulfate
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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
5,5'-dithiobis(2-nitrobenzoic acid)
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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
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adenosine 5'-phosphoramidate
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adenosine 5'-phosphosulfate
Ba2+
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2 mM
beta-fluoro-adenosine 5'-phosphosulfate
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beta-methylene-adenosine 5'-phosphosulfate
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ClO3-
deoxyadenylylsulfate
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1 mM, in presence of about 20% inhibition
diacetyl
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significant inhibition in the presence of borate, protection by adenosine 5'-phosphosulfate, ATP or MgATP2- plus nitrate
diphosphate
FSO3-
guanylylsulfate
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1 mM, in presence of adenylylsulfate about 20% inhibition
inosylylsulfate
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1 mM, in presence of adenylylsulfate about 20% inhibition
methylene blue
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inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate
MgATP2-
N-Acetylimidazole
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76% of the original activity can be restored by treatment with hydroxylamine
Ni2+
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2 mM
PCMB
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5 mM, inhibits reaction with diphosphate and adenylylsulfate
Phenylglyoxal
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3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
phosphate
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inhibition is enhanced by increasing concentrations of Mg2+
S2O32-
SeO42-
SO32-
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1 mM, 10-25% inhibition
SO42-
Sulfide
Tetranitromethane
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partial
thiosulfate
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competitive with molybdate and noncompetitive with MgATP
Tris-malic acid-KOH buffer
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Zn2+
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inhibitory effect even at concentrations as low as 40 mg/l
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
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AMP
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activates
dithiothreitol
activates
FSO3-
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activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
S2O32-
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activates SO42dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
additional information
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enzyme activity is positively correlated with seed yield and influenced by sulfur assimilation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.17
adenosine 5'-phosphosulfate
0.0045 - 0.0245
adenylyl sulfate
0.0004 - 0.025
adenylylsulfate
0.027 - 2.6
ATP
0.12
CrO42-
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30C, pH 8.0
0.16 - 0.84
dATP
0.00071 - 1
diphosphate
1.3
FPO32-
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pH 8.0, 30C, chloroplastic enzyme
0.0191
magnesium diphosphate
reverse reaction, ATP synthesis
0.0077 - 1.1
MgATP2-
1.3
molybdate
pH 8.0, 30C
0.076 - 0.64
MoO42-
0.1 - 1
SeO42-
0.18 - 3.3
SO42-
0.00211 - 17
sulfate
0.47
WO42-
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30C, pH 8.0
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
36
adenosine 5'-phosphosulfate
Brassica capitata
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pH 8.0, 30C, synthesis of ATP
24.5 - 260
adenylyl sulfate
46.6
adenylylsulfate
Penicillium chrysogenum
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pH 8.0, 30C, truncated mutant enzyme del396-573; pH 8.0, 30C, wild-type enzyme
1.49 - 36
ATP
36 - 73.3
diphosphate
19.1
magnesium diphosphate
Glycine max
Q8SAG1
reverse reaction, ATP synthesis
13.7 - 24.4
MoO42-
3.13
SO42-
Brassica capitata
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pH 8.0, 30C, synthesis of adenosine 5'-phosphosulfate
1.8 - 23.2
sulfate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 1.3
3',5'-adenosine diphosphate
0.0008
3'-phosphoadenosine-5'-phosphate
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pH 8.0, 30C
0.000057 - 0.0004
3'-phosphoadenosine-5'-phosphosulfate
0.25 - 0.42
adenosine 5'-monosulfate
0.24
adenosine 5'-phosphoramidate
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pH 8.0, 30C, synthesis of AMP
0.000018 - 0.3
adenosine 5'-phosphosulfate
0.06 - 1.15
ADP
0.165 - 2.1
AMP
1 - 1.1
ATP
0.0047 - 0.005
beta-fluoro-adenosine 5'-phosphosulfate
0.0025 - 0.003
beta-methylene-adenosine 5'-phosphosulfate
0.033 - 0.3
ClO3-
0.28
ClO4-
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pH 8.0, 30C
0.001
diphosphate
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pH 8.0, 30C, at 20 mM SO42- and 5 mM excess Mg2+
0.0034 - 0.5
FSO3-
0.33 - 1.3
MgATP2-
14.3
molybdate
pH 8.0, 30C
2.02
MoO42-
-
pH 8.0, 30C
0.9 - 2.5
NAD+
0.25 - 2.2
NO3-
0.36 - 1.13
S2O32-
0.5
SeO42-
-
pH 7.8, 37C
2
SO42-
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pH 8.0, 30C
1.7
sulfate
pH 8.0, 30C
0.66 - 3.4
Sulfide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000066
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formation of adenosine 5'-phosphosulfate
0.000246
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formation of ATP
0.013
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purified enzyme has an activity of 0.013-0.016 micromol/min/mg
1.1
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cell extract
2.9
specific activity for APS synthesis
3.3
Brassica capitata
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synthesis of adenosine 5'-phosphosulfate
4.3
Brassica capitata
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Mg-diphosphate-MgATP2-exchange
11.98
ratio AcATPS1-AcAPR1 1:1
15.25
ratio AcATPS1-AcAPR1 1:5, five-fold excess of AcAPR1 slightly increases the activity of AcATPS1
30
Brassica capitata
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31.5
adenylyl sulfate synthesis
38
Brassica capitata
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molybdolysis, and synthesis of MgATP2-
48.7
specific activity for ATP synthesis
205.2
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enzyme form ATPSc
237.7
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enzyme form ATPSm
247
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cytosolic enzyme
267
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chloroplastic enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
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enzyme form ATPSc, incorporation of SO42-
7.8 - 8
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0.1 M phosphate buffer