Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation
Herrmann, J.; Ravilious, G.E.; McKinney, S.E.; Westfall, C.S.; Lee, S.G.; Baraniecka, P.; Giovannetti, M.; Kopriva, S.; Krishnan, H.B.; Jez, J.M.; J. Biol. Chem. 289, 10919-10929 (2014) 
Data extracted from this reference:
Cloned(Commentary)
Cloned (Commentary)
Organism
sequence comparisons and phylogenetic tree, recombinant expression of wild-type and mutant N-terminally truncated and His6-tagged enzymes in Escherichia coli strain Rosetta (DE3)
Glycine max
Crystallization (Commentary)
Crystallization (Commentary)
Organism
ATP sulfurylase isoform 1 in complex with APS, X-ray diffraction structure determination and analysis
Glycine max
Engineering
Protein Variants
Commentary
Organism
A144T/T150S
site-directed mutagenesis
Arabidopsis thaliana
A337S
site-directed mutagenesis, shows activity unaltered to the wild-type enzyme
Arabidopsis thaliana
E169A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
E312V
site-directed mutagenesis
Arabidopsis thaliana
F245A
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
Glycine max
F245L
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
Glycine max
G342D
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
G56S
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
H252N
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
H255A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
Glycine max
H255Q
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
H333Q
site-directed mutagenesis, shows highly increased activity compared to the wild-type enzyme
Glycine max
K372R
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
L122V
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
L258A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
Glycine max
L258V
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
additional information
enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants
Glycine max
N160K
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
N202S
site-directed mutagenesis
Arabidopsis thaliana
N249A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
Glycine max
N249D
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
Glycine max
Q246A
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
Q246E
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
Q246N
site-directed mutagenesis, shows very highly increased activity compared to the wild-type enzyme
Glycine max
R248K
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
Glycine max
R349K
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
Glycine max
S166N
site-directed mutagenesis
Arabidopsis thaliana
S9R
site-directed mutagenesis, a transit peptide mutant, inactive mutant
Arabidopsis thaliana
T150S
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
T198A
site-directed mutagenesis, shows activity similar to the wild-type enzyme
Arabidopsis thaliana
V316F
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
Arabidopsis thaliana
V43N
site-directed mutagenesis, a transit peptide mutant, shows activity similar to the wild-type enzyme
Arabidopsis thaliana
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic analysis of wild-type and mutant enzymes, overview
Glycine max
0.0044
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H255A
Glycine max
0.0065
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant N249D
Glycine max
0.0127
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H333Q
Glycine max
0.022
-
diphosphate
pH 8.0, 25°C, recombinant mutant H333Q
Glycine max
0.0226
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H255Q
Glycine max
0.0247
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant F245L
Glycine max
0.0272
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H252D
Glycine max
0.0282
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant L258A
Glycine max
0.0342
-
adenylyl sulfate
pH 8.0, 25°C, recombinant wild-type enzyme
Glycine max
0.0346
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant R349K
Glycine max
0.0363
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant F245A
Glycine max
0.0385
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant L258V
Glycine max
0.0399
-
diphosphate
pH 8.0, 25°C, recombinant mutant H255A
Glycine max
0.0402
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246A
Glycine max
0.0432
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant N249A
Glycine max
0.045
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246N
Glycine max
0.0458
-
diphosphate
pH 8.0, 25°C, recombinant wild-type enzyme
Glycine max
0.047
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant R248K
Glycine max
0.0556
-
diphosphate
pH 8.0, 25°C, recombinant mutant Q246N
Glycine max
0.0694
-
diphosphate
pH 8.0, 25°C, recombinant mutant N249D
Glycine max
0.085
-
diphosphate
pH 8.0, 25°C, recombinant mutant H252D
Glycine max
0.114
-
diphosphate
pH 8.0, 25°C, recombinant mutant H255Q
Glycine max
0.117
-
diphosphate
pH 8.0, 25°C, recombinant mutant Q246A
Glycine max
0.118
-
diphosphate
pH 8.0, 25°C, recombinant mutant F245L
Glycine max
0.153
-
diphosphate
pH 8.0, 25°C, recombinant mutant F245A
Glycine max
0.208
-
diphosphate
pH 8.0, 25°C, recombinant mutant L258V
Glycine max
0.312
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246E
Glycine max
0.373
-
diphosphate
pH 8.0, 25°C, recombinant mutant L258A
Glycine max
0.428
-
diphosphate
pH 8.0, 25°C, recombinant mutant R248K
Glycine max
0.59
-
diphosphate
pH 8.0, 25°C, recombinant mutant R349K
Glycine max
0.611
-
diphosphate
pH 8.0, 25°C, recombinant mutant Q246E
Glycine max
1.078
-
diphosphate
pH 8.0, 25°C, recombinant mutant N249A
Glycine max
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
chloroplast
the enzyme has a plastid localization sequence (residues 1-48)
Glycine max
9507
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + sulfate
Glycine max
-
diphosphate + adenylyl sulfate
-
-
?
ATP + sulfate
Arabidopsis thaliana
-
diphosphate + adenylyl sulfate
-
-
?
ATP + sulfate
Arabidopsis thaliana Col-0
-
diphosphate + adenylyl sulfate
-
-
?
diphosphate + adenylyl sulfate
Glycine max
-
ATP + sulfate
-
-
r
diphosphate + adenylyl sulfate
Arabidopsis thaliana
-
ATP + sulfate
-
-
r
diphosphate + adenylyl sulfate
Arabidopsis thaliana Col-0
-
ATP + sulfate
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Arabidopsis thaliana
Q9LIK9
isozyme atps1
-
Arabidopsis thaliana Col-0
Q9LIK9
isozyme atps1
-
Glycine max
Q8SAG1
ATP sulfurylase isoform 1
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant wild-type and mutant N-terminally truncated and His6-tagged enzymes from Escherichia coli strain Rosetta (DE3) by nicke affinity chromatography and gel filtration
Glycine max
Reaction
Reaction
Commentary
Organism
Reaction ID
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
Glycine max
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.072
-
recombinant ATPS1 mutant G342D, pH 8.0, 25°C
Arabidopsis thaliana
0.121
-
recombinant ATPS1 mutant G56S, pH 8.0, 25°C
Arabidopsis thaliana
0.135
-
recombinant ATPS1 mutant E169A, pH 8.0, 25°C; recombinant ATPS1 mutant L122V, pH 8.0, 25°C
Arabidopsis thaliana
0.14
-
recombinant ATPS1 mutant T198A, pH 8.0, 25°C; recombinant ATPS1 mutant V43N, pH 8.0, 25°C
Arabidopsis thaliana
0.145
-
recombinant wild-type enzyme ATPS1 and mutant A337S, pH 8.0, 25°C
Arabidopsis thaliana
0.247
-
recombinant ATPS1 mutant V316F, pH 8.0, 25°C
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + sulfate
-
738608
Glycine max
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
-
738608
Arabidopsis thaliana
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
-
738608
Arabidopsis thaliana Col-0
diphosphate + adenylyl sulfate
-
-
-
?
diphosphate + adenylyl sulfate
-
738608
Glycine max
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
-
738608
Arabidopsis thaliana
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
-
738608
Arabidopsis thaliana Col-0
ATP + sulfate
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
ATP sulfurylase domain structure and oligomerization, overview
Glycine max
Synonyms
Synonyms
Commentary
Organism
ATP sulfurylase
-
Glycine max
ATP sulfurylase
-
Arabidopsis thaliana
ATPS1
-
Arabidopsis thaliana
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Arabidopsis thaliana
25
-
assay at
Glycine max
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Arabidopsis thaliana
8
-
assay at
Glycine max
Cloned(Commentary) (protein specific)
Commentary
Organism
sequence comparisons and phylogenetic tree, recombinant expression of wild-type and mutant N-terminally truncated and His6-tagged enzymes in Escherichia coli strain Rosetta (DE3)
Glycine max
Crystallization (Commentary) (protein specific)
Crystallization
Organism
ATP sulfurylase isoform 1 in complex with APS, X-ray diffraction structure determination and analysis
Glycine max
Engineering (protein specific)
Protein Variants
Commentary
Organism
A144T/T150S
site-directed mutagenesis
Arabidopsis thaliana
A337S
site-directed mutagenesis, shows activity unaltered to the wild-type enzyme
Arabidopsis thaliana
E169A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
E312V
site-directed mutagenesis
Arabidopsis thaliana
F245A
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
Glycine max
F245L
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
Glycine max
G342D
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
G56S
site-directed mutagenesis, a transit peptide mutant, shows slightly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
H252N
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
H255A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
Glycine max
H255Q
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
H333Q
site-directed mutagenesis, shows highly increased activity compared to the wild-type enzyme
Glycine max
K372R
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
L122V
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
L258A
site-directed mutagenesis, shows slightly reduced activity compared to the wild-type enzyme
Glycine max
L258V
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
additional information
enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants
Glycine max
N160K
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
N202S
site-directed mutagenesis
Arabidopsis thaliana
N249A
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
Glycine max
N249D
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
Glycine max
Q246A
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
Q246E
site-directed mutagenesis, shows reduced activity compared to the wild-type enzyme
Glycine max
Q246N
site-directed mutagenesis, shows very highly increased activity compared to the wild-type enzyme
Glycine max
R248K
site-directed mutagenesis, shows highly reduced activity compared to the wild-type enzyme
Glycine max
R349K
site-directed mutagenesis, shows very highly decreased activity compared to the wild-type enzyme
Glycine max
S166N
site-directed mutagenesis
Arabidopsis thaliana
S9R
site-directed mutagenesis, a transit peptide mutant, inactive mutant
Arabidopsis thaliana
T150S
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
T198A
site-directed mutagenesis, shows activity similar to the wild-type enzyme
Arabidopsis thaliana
V316F
site-directed mutagenesis, shows increased activity compared to the wild-type enzyme
Arabidopsis thaliana
V43N
site-directed mutagenesis, a transit peptide mutant, shows activity similar to the wild-type enzyme
Arabidopsis thaliana
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetic analysis of wild-type and mutant enzymes, overview
Glycine max
0.0044
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H255A
Glycine max
0.0065
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant N249D
Glycine max
0.0127
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H333Q
Glycine max
0.022
-
diphosphate
pH 8.0, 25°C, recombinant mutant H333Q
Glycine max
0.0226
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H255Q
Glycine max
0.0247
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant F245L
Glycine max
0.0272
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant H252D
Glycine max
0.0282
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant L258A
Glycine max
0.0342
-
adenylyl sulfate
pH 8.0, 25°C, recombinant wild-type enzyme
Glycine max
0.0346
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant R349K
Glycine max
0.0363
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant F245A
Glycine max
0.0385
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant L258V
Glycine max
0.0399
-
diphosphate
pH 8.0, 25°C, recombinant mutant H255A
Glycine max
0.0402
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246A
Glycine max
0.0432
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant N249A
Glycine max
0.045
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246N
Glycine max
0.0458
-
diphosphate
pH 8.0, 25°C, recombinant wild-type enzyme
Glycine max
0.047
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant R248K
Glycine max
0.0556
-
diphosphate
pH 8.0, 25°C, recombinant mutant Q246N
Glycine max
0.0694
-
diphosphate
pH 8.0, 25°C, recombinant mutant N249D
Glycine max
0.085
-
diphosphate
pH 8.0, 25°C, recombinant mutant H252D
Glycine max
0.114
-
diphosphate
pH 8.0, 25°C, recombinant mutant H255Q
Glycine max
0.117
-
diphosphate
pH 8.0, 25°C, recombinant mutant Q246A
Glycine max
0.118
-
diphosphate
pH 8.0, 25°C, recombinant mutant F245L
Glycine max
0.153
-
diphosphate
pH 8.0, 25°C, recombinant mutant F245A
Glycine max
0.208
-
diphosphate
pH 8.0, 25°C, recombinant mutant L258V
Glycine max
0.312
-
adenylyl sulfate
pH 8.0, 25°C, recombinant mutant Q246E
Glycine max
0.373
-
diphosphate
pH 8.0, 25°C, recombinant mutant L258A
Glycine max
0.428
-
diphosphate
pH 8.0, 25°C, recombinant mutant R248K
Glycine max
0.59
-
diphosphate
pH 8.0, 25°C, recombinant mutant R349K
Glycine max
0.611
-
diphosphate
pH 8.0, 25°C, recombinant mutant Q246E
Glycine max
1.078
-
diphosphate
pH 8.0, 25°C, recombinant mutant N249A
Glycine max
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
chloroplast
the enzyme has a plastid localization sequence (residues 1-48)
Glycine max
9507
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + sulfate
Glycine max
-
diphosphate + adenylyl sulfate
-
-
?
ATP + sulfate
Arabidopsis thaliana
-
diphosphate + adenylyl sulfate
-
-
?
ATP + sulfate
Arabidopsis thaliana Col-0
-
diphosphate + adenylyl sulfate
-
-
?
diphosphate + adenylyl sulfate
Glycine max
-
ATP + sulfate
-
-
r
diphosphate + adenylyl sulfate
Arabidopsis thaliana
-
ATP + sulfate
-
-
r
diphosphate + adenylyl sulfate
Arabidopsis thaliana Col-0
-
ATP + sulfate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant N-terminally truncated and His6-tagged enzymes from Escherichia coli strain Rosetta (DE3) by nicke affinity chromatography and gel filtration
Glycine max
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.072
-
recombinant ATPS1 mutant G342D, pH 8.0, 25°C
Arabidopsis thaliana
0.121
-
recombinant ATPS1 mutant G56S, pH 8.0, 25°C
Arabidopsis thaliana
0.135
-
recombinant ATPS1 mutant E169A, pH 8.0, 25°C; recombinant ATPS1 mutant L122V, pH 8.0, 25°C
Arabidopsis thaliana
0.14
-
recombinant ATPS1 mutant T198A, pH 8.0, 25°C; recombinant ATPS1 mutant V43N, pH 8.0, 25°C
Arabidopsis thaliana
0.145
-
recombinant wild-type enzyme ATPS1 and mutant A337S, pH 8.0, 25°C
Arabidopsis thaliana
0.247
-
recombinant ATPS1 mutant V316F, pH 8.0, 25°C
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + sulfate
-
738608
Glycine max
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
-
738608
Arabidopsis thaliana
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
-
738608
Arabidopsis thaliana Col-0
diphosphate + adenylyl sulfate
-
-
-
?
diphosphate + adenylyl sulfate
-
738608
Glycine max
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
-
738608
Arabidopsis thaliana
ATP + sulfate
-
-
-
r
diphosphate + adenylyl sulfate
-
738608
Arabidopsis thaliana Col-0
ATP + sulfate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
ATP sulfurylase domain structure and oligomerization, overview
Glycine max
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Arabidopsis thaliana
25
-
assay at
Glycine max
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Arabidopsis thaliana
8
-
assay at
Glycine max
General Information
General Information
Commentary
Organism
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
Arabidopsis thaliana
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
Glycine max
additional information
the enzyme has several highly conserved substrate binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but is similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Residues involved in catalysis and substrate binding, overview
Glycine max
General Information (protein specific)
General Information
Commentary
Organism
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
Arabidopsis thaliana
metabolism
ATP sulfurylase plays a critical role in the plant sulfur assimilation pathway by catalyzing its first committed step via the energetically unfavorable formation of APS. ATP sulfurylase synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP
Glycine max
additional information
the enzyme has several highly conserved substrate binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but is similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Residues involved in catalysis and substrate binding, overview
Glycine max
Other publictions for EC
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737621
Prioretti
Redox regulation of ATP sulfur ...
Synechocystis sp., Thalassiosira pseudonana, Thalassiosira pseudonana PLY-693
Biochem. Biophys. Res. Commun.
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1555-1562
2016
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4
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2
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6
6
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738100
Barrett
Upregulation of UGT2B4 express ...
Homo sapiens
Drug Metab. Dispos.
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2015
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-
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1
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1
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1
1
-
-
-
738302
Anjum
ATP-sulfurylase, sulfur-compou ...
Arabidopsis thaliana, Avena sativa, Brassica juncea, Brassica napus, Camellia sinensis, Glycine max, Hordeum vulgare, Lemna gibba, Lepidium sativum, Nicotiana tabacum, Noccaea caerulescens, Oryza sativa, Salvinia minima, Sedum alfredii, Stanleya pinnata, Triticum aestivum, Zea mays
Front. Plant Sci.
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2015
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17
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24
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25
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1
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24
-
54
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17
-
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19
-
4
24
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14
24
-
24
-
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1
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-
24
-
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17
34
48
26
-
-
739744
Kushkevych
Kinetic properties of adenosin ...
Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger, Desulfovibrio piger Vib-7
Ukr. Biochem. J.
86
129-138
2015
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10
2
2
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8
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14
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4
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2
2
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10
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3
4
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8
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2
2
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2
2
-
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2
2
-
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-
738299
Bohrer
Alternative translational init ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Front. Plant Sci.
5
750
2014
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1
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7
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5
1
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2
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6
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4
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2
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1
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1
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7
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1
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4
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2
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1
1
-
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738608
Herrmann
Structure and mechanism of soy ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0, Glycine max
J. Biol. Chem.
289
10919-10929
2014
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1
1
32
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33
2
1
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6
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7
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1
1
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6
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6
1
3
2
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2
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1
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1
32
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33
2
1
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6
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1
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6
-
6
1
2
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2
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3
3
-
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-
737880
Ravilious
-
Kinetic mechanism of the dimer ...
Glycine max
Biosci. Rep.
33
585-591
2013
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1
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1
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1
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1
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1
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-
-
-
2
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3
3
-
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738206
Mueller
Adenosine-5-phosphosulfate - a ...
Homo sapiens
FEBS J.
280
3050-3057
2013
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-
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1
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2
1
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6
2
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2
4
-
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739345
Koprivova
Natural variation in the ATPS1 ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Plant Physiol.
163
1133-1141
2013
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1
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4
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4
4
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739483
Parey
Structural, biochemical and ge ...
Allochromatium vinosum, Allochromatium vinosum DSM 180
PLoS ONE
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e74707
2013
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1
1
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3
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1
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5
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1
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1
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4
1
1
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1
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3
3
-
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-
721772
Jaramillo
Cloning, expression and bioinf ...
Acidithiobacillus ferrooxidans
Bioinformation
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695-704
2012
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1
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2
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5
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1
1
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723546
Schroeder
Human PAPS synthase isoforms a ...
Homo sapiens
PLoS ONE
7
e29559
2012
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1
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2
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1
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3
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1
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2
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5
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1
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722558
Saggu
Sodium selenate effect on Syne ...
Synechococcus elongatus, Synechococcus elongatus PCC 7942
J. Basic Microbiol.
50
351-359
2010
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2
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701923
Gay
Kinetic properties of ATP sulf ...
Thiobacillus denitrificans ATCC 25259
Arch. Biochem. Biophys.
489
110-117
2009
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1
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4
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2
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702743
Adachi
Development of a homologous tr ...
Aspergillus aculeatus
Biosci. Biotechnol. Biochem.
73
1197-1199
2009
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-
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703605
Harada
Expression of genes for sulfur ...
Candidatus Ruthia magnifica, Candidatus Ruthia magnifica Cm, Candidatus Vesicomyosocius okutanii HA
Extremophiles
13
895-903
2009
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7
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Bradley
Sulfate activation enzymes: ph ...
Phytophthora infestans T30-4
J. Mol. Evol.
68
1-13
2009
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1
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705437
Guo
Response of ATP sulfurylase an ...
Sedum alfredii
J. Zhejiang Univ. Sci. B
10
251-257
2009
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690263
Gavel
Purification, crystallization ...
Desulfovibrio desulfuricans
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593-595
2008
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1
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1
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694749
Zhu
Cloning of two cDNAs encoding ...
Camellia sinensis
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731-738
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1
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Cumming
Complex formation between reco ...
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Crystal structure of the bifun ...
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Ahmad
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Interactive effect of sulfur a ...
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Phartiyal
Soybean ATP sulfurylase, a hom ...
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Mougous
Molecular basis for G protein ...
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Oyekola
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ATP-sulfurylase: An enzymatic ...
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Sun
Anatomy of an energy-coupling ...
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Taguchi
Crystal structure of a novel z ...
Thermus thermophilus HB8
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Lansdon
Human 3'-phosphoadenosine 5'-p ...
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11
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Wangeline
Overexpression of ATP sulfuryl ...
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Hanna
ATP sulfurylase from the hyper ...
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1
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1
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643289
MacRae
Allosteric inhibition via R-st ...
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2002
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643285
MacRae
Crystal structure of ATP sulfu ...
Penicillium chrysogenum
Biochemistry
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2001
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1
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1
1
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643288
Medina
Temperature effects on the all ...
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2001
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1
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1
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The complex structures of ATP ...
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1
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-
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393950
Rotte
Differential subcellular local ...
Arabidopsis sp.
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4
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1
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2
-
-
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641225
Deyrup
Activity and stability of reco ...
Mus musculus
J. Biol. Chem.
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1999
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1
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1
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1
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1
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1
1
-
-
2
-
-
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-
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643287
Deyrup
Chemical modification and site ...
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J. Biol. Chem.
274
28929-28936
1999
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10
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1
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1
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10
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1
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1
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643290
Karamohamed
Production, Purification, and ...
Saccharomyces cerevisiae
Protein Expr. Purif.
15
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1
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1
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2
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1
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1
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1
1
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643277
Deyrup
Deletion and site-directed mut ...
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9
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1
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1
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1
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9
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1
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1
-
-
-
-
-
1
-
-
-
-
-
-
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-
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643291
Sperling
Dissimilatory ATP sulfurylase ...
Archaeoglobus fulgidus
FEMS Microbiol. Lett.
162
257-264
1998
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1
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2
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1
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1
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2
1
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2
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1
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2
1
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1
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1
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2
1
2
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-
-
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-
-
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-
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643293
Yanagisawa
cDNA cloning, expression, and ...
Homo sapiens
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62
1037-1040
1998
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1
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1
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1
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1
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1
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1
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1
1
-
-
-
-
-
-
-
-
-
-
-
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643294
Gavel
ATP Sulfurylases from sulfate- ...
Desulfovibrio desulfuricans, Desulfovibrio gigas
Biochemistry
37
16225-16232
1998
-
-
-
-
-
-
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4
3
2
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7
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2
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2
2
4
2
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4
3
2
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2
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2
2
4
2
-
-
-
-
-
-
-
-
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-
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643262
Lappartient
Glutathione-mediated regulatio ...
Brassica napus
Plant Physiol.
114
177-183
1997
-
-
-
-
-
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-
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1
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3
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1
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2
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1
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1
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2
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643292
Onda
-
Purification and properties of ...
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60
1740-1742
1996
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3
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3
2
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13
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1
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1
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6
1
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1
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1
1
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3
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3
2
2
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1
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1
-
6
1
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-
1
-
1
1
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643282
Renosto
ATP sulfurylase from higher pl ...
Spinacia oleracea
Arch. Biochem. Biophys.
307
272-285
1993
-
-
-
-
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10
14
6
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3
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1
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3
2
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1
1
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14
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10
14
14
6
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3
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1
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3
2
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3
1
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1
1
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643274
Mishra
-
Regulation and partly purifica ...
Synechococcus sp., Synechococcus sp. 6301
Z. Naturforsch. C
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95-101
1992
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2
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1
1
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2
1
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643278
Li
Purification and properties of ...
Euglena gracilis
Biochim. Biophys. Acta
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1991
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3
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1
2
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1
1
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2
1
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2
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643258
Renosto
Regulation of inorganic sulfat ...
Aspergillus nidulans, Neurospora crassa, Penicillium chrysogenum, Penicillium duponti, Rattus norvegicus, Saccharomyces cerevisiae, Spinacia oleracea
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16
7
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7
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8
7
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643275
Dahl
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Purification and characterizat ...
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27-32
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1
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1
1
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Rat liver ATP-sulfurylase: pur ...
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269
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1
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Renosto
Sulfate-activating enzymes of ...
Penicillium chrysogenum
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643253
Kanno
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Properties of ATP-sulfurylase ...
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54
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3
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Geller
Co-purification and characteri ...
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Renosto
Comparative stability and cata ...
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4
4
12
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4
1
2
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2
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643268
Seubert
Adenosinetriphosphate sulfuryl ...
Penicillium chrysogenum
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240
509-523
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5
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643276
Cooper
-
Sulfate activation in Rhodobac ...
Blastochloris viridis, Rhodobacter capsulatus, Rhodobacter sphaeroides, Rhodopseudomonas palustris, Rhodospirillum rubrum, Rhodovulum sulfidophilum, Rubrivivax gelatinosus
Arch. Microbiol.
141
384-391
1985
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8
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1
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643266
Seubert
ATP sulfurylase from Penicilli ...
Penicillium chrysogenum
Arch. Biochem. Biophys.
225
679-691
1983
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6
2
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-
643270
Bicknell
The stereochemical course of n ...
Saccharomyces cerevisiae
J. Biol. Chem.
257
8922-8927
1982
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1
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643280
Osslund
ATP sulfurylase from higher pl ...
Brassica capitata
Plant Physiol.
70
39-45
1982
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3
6
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1
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5
1
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643254
Menon
-
ATP sulfurylase from Spirulina ...
Arthrospira platensis
Proc. Indian Natl. Sci. Acad. Part B
46
223-228
1980
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2
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643255
Kaul
-
Some properties of ATP sulfhyd ...
Candida albicans
Indian J. Exp. Biol.
18
1517-1518
1980
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643260
Nozawa
Purification and some properti ...
Heliocidaris crassispina
Biochim. Biophys. Acta
611
309-313
1980
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643264
Farley
Adenosine triphosphate sulfury ...
Penicillium chrysogenum
J. Biol. Chem.
254
3537-3542
1979
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5
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1
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643273
Menon
Adenosine 5'-triphosphate sulp ...
Arthrospira platensis
Experientia
35
854-855
1979
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1
1
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1
1
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1
1
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643259
Burnell
Purification and properties of ...
Rattus norvegicus
Biochim. Biophys. Acta
527
239-248
1978
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1
11
6
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5
6
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1
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1
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643272
Sawhney
Effects of adenine nucleotides ...
Anabaena cylindrica
Biochem. J.
164
161-167
1977
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3
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643267
Farley
Adenosine triphosphate sulfury ...
Penicillium chrysogenum
J. Biol. Chem.
251
4389-4397
1976
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2
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643271
Heinzel
-
Sulfite formation by wine yeas ...
Saccharomyces bayanus, Saccharomyces bayanus Sacardo, Saccharomyces cerevisiae
Arch. Microbiol.
107
293-297
1976
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2
1
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643284
Onajobi
Effects of adenine nucleotides ...
Oryza sativa
Biochem. J.
149
301-304
1975
1
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643252
Peck
-
Sulfation linked to ATP cleava ...
Bacillus subtilis, Desulfotomaculum nigrificans, Desulfovibrio desulfuricans, Escherichia coli, Mus musculus, Nitrobacter winogradskyi, Nitrosomonas europaea, Ovis aries, Penicillium chrysogenum, Penicillium sp., Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Spinacia oleracea, Thiobacillus thioparus
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
10
651-669
1974
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17
2
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14
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53
1
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53
1
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643283
Shaw
Comparative enzymology of the ...
Astragalus bisulcatus, Astragalus hamosus, Astragalus racemosus, Astragalus sinicus
Biochem. J.
139
37-42
1974
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20
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4
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643269
Hawes
Adenosine 5-triphosphate sulph ...
Saccharomyces cerevisiae
Biochem. J.
133
541-550
1973
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4
2
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3
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1
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643279
Onajobi
Adenosine 5'-triphosphate-sulf ...
Zea mays
Plant Physiol.
52
580-584
1973
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643261
Shoyab
Purification and properties of ...
Mus musculus
Biochim. Biophys. Acta
258
113-124
1972
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1
7
1
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1
1
2
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1
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643281
Shaw
Purification, properties and s ...
Spinacia oleracea
Biochem. J.
127
237-247
1972
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4
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1
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1
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641219
Robbins
-
The enzymatic sequence in the ...
Saccharomyces cerevisiae
J. Am. Chem. Soc.
78
6409-6410
1956
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