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
-
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
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Monobactam biosynthesis
-
-
Purine metabolism
-
-
selenate reduction
-
-
Selenocompound metabolism
-
-
sulfate activation for sulfonation
-
-
sulfate reduction
-
-
sulfate reduction II (assimilatory)
-
-
sulfate reduction III (assimilatory)
-
-
sulfate reduction IV (dissimilatory)
-
-
sulfate reduction V (dissimilatory)
-
-
sulfite oxidation III
-
-
Sulfur metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Columbi aecotype
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Brassica capitata
-
-
-
Manually annotated by BRENDA team
transgenics overexpressing ATP sulfurylase
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Cm
SwissProt
Manually annotated by BRENDA team
strain Cm
SwissProt
Manually annotated by BRENDA team
mixed SRB (sulfate reducing bacteria)-containing consortium consisting mainly of the Desulfovibrio genus
-
-
Manually annotated by BRENDA team
Klebs var. bacillaris Cori, aplastidic mutant W10BSmL
-
-
Manually annotated by BRENDA team
strain NCA 1503
-
-
Manually annotated by BRENDA team
strain NCA 1503
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Penicillium duponti
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sacardo, strongly sulfite producing strain
-
-
Manually annotated by BRENDA team
Sacardo, strongly sulfite producing strain
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
6301
-
-
Manually annotated by BRENDA team
6301
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
-
-
-
-
?
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
-
-
-
-
?
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
-
reaction carried out by the APS kinase activity of the bifunctional enzyme
-
-
r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
show the reaction diagram
-
reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
-
-
r
MgATP2- + sulfate
Mg-diphosphate + adenylyl sulfate
show the reaction diagram
-
-
-
r
additional information
?
-
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Cobalt
Fe2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
SO42-
-
stimulatory to ATPS
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-adenosine diphosphate
-
-
3'-phosphoadenosine 5'-phosphosulfate
-
allosteric, binding of the inhibitor to the catalytic site as well as to the allosteric site of the wild type enzyme acts to decrease the degree of cooperativity
3'-phosphoadenosine-5'-phosphate
3'-phosphoadenosine-5'-phosphosulfate
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.05 mM, rapid decrease in activity of wild-type enzyme (t1/2: 20 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min
adenosine 5'-monosulfate
-
-
adenosine 5'-phosphoramidate
-
-
adenosine 5'-phosphosulfate
Ba2+
-
2 mM
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
diphosphate
guanylylsulfate
-
1 mM, in presence of adenylylsulfate about 20% inhibition
inosylylsulfate
-
1 mM, in presence of adenylylsulfate about 20% inhibition
methylene blue
-
inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate
MgATP2-
molybdate
-
N-Acetylimidazole
-
76% of the original activity can be restored by treatment with hydroxylamine
Ni2+
-
2 mM
PCMB
-
5 mM, inhibits reaction with diphosphate and adenylylsulfate
Phenylglyoxal
-
3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
phosphate
-
inhibition is enhanced by increasing concentrations of Mg2+
S2O32-
SeO42-
SO32-
-
1 mM, 10-25% inhibition
Sulfide
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
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
-
AMP
-
activates
dithiothreitol
activates
FSO3-
-
activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
S2O32-
-
activates SO42dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
additional information
-
enzyme activity is positively correlated with seed yield and influenced by sulfur assimilation
-
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-
-
30C, pH 8.0
0.16 - 0.84
dATP
0.00071 - 1
diphosphate
1.3
FPO32-
-
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-
-
30C, pH 8.0
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
36
adenosine 5'-phosphosulfate
Brassica capitata
-
pH 8.0, 30C, synthesis of ATP
24.5 - 260
adenylyl sulfate
46.6
adenylylsulfate
Penicillium chrysogenum
-
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
-
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
-
pH 8.0, 30C
0.000057 - 0.0004
3'-phosphoadenosine-5'-phosphosulfate
0.25 - 0.42
adenosine 5'-monosulfate
0.24
adenosine 5'-phosphoramidate
-
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-
-
pH 8.0, 30C
0.001
diphosphate
-
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-
-
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
-
formation of adenosine 5'-phosphosulfate
0.000246
-
formation of ATP
0.013
-
purified enzyme has an activity of 0.013-0.016 micromol/min/mg
1.1
-
cell extract
2.9
specific activity for APS synthesis
3.3
Brassica capitata
-
synthesis of adenosine 5'-phosphosulfate
4.3
Brassica capitata
-
Mg-diphosphate-MgATP2-exchange
11.98
ratio AcATPS1-AcAPR1 1:1
15.25
ratio AcATPS1-AcAPR1 1:5, five-fold excess of AcAPR1 slightly increases the activity of AcATPS1
30
Brassica capitata
-
-
31.5
adenylyl sulfate synthesis
38
Brassica capitata
-
molybdolysis, and synthesis of MgATP2-
48.7
specific activity for ATP synthesis
205.2
-
enzyme form ATPSc
237.7
-
enzyme form ATPSm
247
-
cytosolic enzyme
267
-
chloroplastic enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
enzyme form ATPSc, incorporation of SO42-
7.8 - 8
-
0.1 M phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
in Tris-malate and Tris-HCl buffer active between pH 5.5 and pH 9.0
6 - 9
-
pH 6.0: about 65% of maximal activity, pH 9.0: about 65% of maximal activity
6.8 - 9.4
-
the enzyme is active in Tris-buffer between pH 6.8 and 9.4
7 - 7.9
-
pH 7.0: about 70% of maximal activity, pH 7.0: about 65% of maximal activity, enzyme form ATPSc, incorporation of SO42-
7.2 - 9.1
-
pH 7.2: about 45% of maximal activity, pH 9.1: about 50% of maximal activity
7.2 - 8.5
-
about 90% of maximal activity at pH 7.2 and pH 8.5
7.7 - 9
-
pH 7.7: about 75% of maximal activity, pH 9.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
incubation of the bioreactor
46
-
bimodal temperature optima: 46C and 52-54C
100
-
recombinant enzyme
additional information
-
assay performed at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
30C: about 35% of maximal activity, 50C: about 75% of maximal activity
30 - 40
-
full activity up to 40C, completely inactive at 55C
35 - 60
-
35C: about 40% of maximal activity, 60C: about 35% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 4.4
-
isoelectric focusing
5.8
-
isoelectric focusing, enzyme form ATPSm
7.3
predicted from cDNA sequence
7.9
-
isoelectric focusing, enzyme form ATPSc
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
PAPSs2 mRNA is highly expressed in duodenum
Manually annotated by BRENDA team
-
PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus; PAPSs2mRNA is expressed in kidney, expression is higher in female than in male mice
Manually annotated by BRENDA team
-
PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus; PAPSs2mRNA is expressed in lung
Manually annotated by BRENDA team
-
root and leaf
Manually annotated by BRENDA team
-
PAPSs2 mRNA is highly expressed in small intestine
Manually annotated by BRENDA team
-
PAPSs2mRNA is expressed in stomach
Manually annotated by BRENDA team
-
PAPSs1mRNA is detectable in all tissues except for liver of adult mice, highest expression in lung, kidney and uterus
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isoform PAPSS2 is localised mainly within the cytoplasm
Manually annotated by BRENDA team
-
enzyme form ATPSm is mainly associated with mitochondrial membrane
Manually annotated by BRENDA team
isoform PAPSS1 is predominantly nuclear
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)
Human immunodeficiency virus type 1 group M subtype B
Pseudomonas syringae pv. tomato (strain DC3000)
Riftia pachyptila sulfur-oxidizing endosymbiont
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40540
isozyme APS1, calculated from sequence of cDNA
42000
-
gel filtration
50000
SDS-PAGE; SDS-PAGE and gel filtration
51780
isozyme APS2, calculated from sequence of cDNA
51810
calculated from sequence of cDNA
52000
predicted from cDNA sequence, enzyme functions as a 100 kDa homodimer
61100
recombinant isozyme APS1, SDS-PAGE
66000
-
enzyme ATPSm and ATPSc, gel filtration
70200
recombinant isozyme APS2, SDS-PAGE
85000
-
gel filtration
100000
-
gel filtration
108000
Brassica capitata
-
glycerol density gradient centrifugation
122000
-
gel filtration
133000
isoform PAPSS1, gel filtration
138000
-
gel filtration
150000
-
gel filtration
151000
-
gel filtration
160000
-
non-denaturing PAGE
170000
-
gel filtration
260000
290000
-
gel filtration
410000
-
gel filtration
420000 - 440000
-
-
440000
470000
-
recombinant enzyme, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
monomer
octamer
tetramer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
-
-
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop vapor diffusion at 25C in 40% (v/v) ethanol, 1% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM MgATP, X-ray crystal structure analysis shows that the protein dimerizes through its APS kinase domain and contains ADP bound in all four active sites; hanging drop vapour diffusion method, at 25 C, in 40% (v/v) ethanol, 1.0% (w/v) PEG 6000, 50 mM sodium acetate and 5 mM Mg-ATP
-
hanging drop vapour diffusion method, using 3 M ammonium sulfate, 100 mM Tris-HCl pH 7.5 with 10% (v/v) MPD
-
recombinant enzyme expressed in Escherichia coli, crystals are grown at 22C by vapor diffusion in hanging drops, crystal structure of the enzyme bound to the allosteric inhibitor 3'-phosphoadenosine-5'-phosphosulfate determined at 2.6 A resolution
-
recombinant enzyme expressed in Escherichia coli, crystals are grown by hanging drop vapor diffusion at 4C
-
X-ray crystal structure analysis of complex between Pseudomonas syringae ATPS (CysD) and its associated regulatory G protein (CysN)
-
crystal structures of ATP sulfurylase with thiosulfate, ADP and chlorate
crystal structure of the enzyme in complex with adenosine 5'-phosphate is determined at 2.5 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
unstable in Tris, diethylbarbiturate, glycine, triethanolamine and bicarbonate buffer, but stable in phosphate buffers of the same pH
643259
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
2 h, wild-type enzyme and individually expressed ATP sulfurylase domain of the bifunctional are stable
37
-
2 h, wild-type enzyme is stable, individually expressed ATP sulfurylase domain of the bifunctional enzyme loses 98% of its activity
45
-
t1/2 for mutant enzyme del396-573: 1.5 min
55
-
5 min, 50% loss of activity
60
-
stable for 10 min
62
-
t1/2 for wild-type enzyme: 1.5 min
70
-
15 min, stable below. 20% loss of activity after 1 h
75
-
1 min, complete loss of activity
90
half-life: more than 1 h
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5C, enzyme solution with 5-10 mg/ml, stable for several months
-
freezing and thawing inactivates the purified enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
not stable to freezing and thawing
-
643259
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 80% loss of activity within 1 month
-
-15C, stable for at least 4 months
-
-6C, enzyme is stable for over 21 days
-
0-4C, purified enzyme solution, 1 mg protein per ml, 15% loss of activity after 5 weeks
-
4C, 50 mM MOPS buffer, pH 7.4, 0.2 mM CoCl2, 0.2 mM ZnCl2, stable for 48 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a chloroplastic and a cytosolic enzyme form
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified
DEAE-52 cellulose column chromatography, Source 15Q column chromatography, Superdex 200 gel filtration, and hydroxyapatite column chromatography
-
enzyme form ATPSm and ATPSc
-
expressed enzyme is purified by affinity chromatography using glutathione-Sepharose and subsequent ion-exchange chromatography; glutathione-Sepharose column chromatography and Mono Q column chromatography
glutathione Sepharose column chromatography and Superdex 200 gel filtration
hydroxyapatite column chromatography, DEAE cellulose column chromatography, and gel filtration; protein is purified by sequential chromatographies on hydroxyapatite, DEAE cellulose and gel filtration
-
immobilized metal ion affinity chromatography
N-terminal His-tagged protein is passed over a Ni2+-NTA column
partial
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Aquifex aeolicus ATP-sulfurylase-APS kinase is expressed in an Escherichia coli pET vector expression system; expressed in Escherichia coli
-
ATP sulfurylase cDNA from MET3 on chromosome X is amplified and expressed in Escherichia coli XL1-Blue. The synthesis of the enzyme is directed by an expression system that employs the regulatory genes of Vibrio fischeri
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. Full-length enzyme and its constituent adenosine 5'-phosphosulfate kinase and ATP sulfurylase domains are individually expressed and purified. Expressed protein generated from the ATP-sulfurylase domain alone is fully active in both the forward and the reverse assays. APS kinase-only recombinants exhibit no kinase activity
-
cloned in Escherichia coli as a truncated version of soybean ATPS lacking the first 48 amino acids, removal of the putative localisation sequence improves the yield of N-terminally His-tagged protein in Escherichia coli; the protein is insoluble when the full-length cDNA of soybean ATPS, including the chloroplast/plastid localisation sequence, is used for expression in Escherichia coli
cloned in Escherichia coli BL-21
-
cloned in Escherichia coli; expressed in Escherichia coli BL21 cells
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells; expressed in Escherichia coli BL21 (DE3) cells; expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21-DE3
expressed in Escherichia coli BL21Star (DE3) cells
-
expression in Escherichia coli BL-21
His-tag version expressed in Escherichia coli BL21-DE3
isoform PAPS synthase 1 wild type and mutant proteins are expressed in Escherichia coli
overexpression in Eacherichia coli
-
truncated enzyme form
-