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Literature summary for 2.7.7.4 extracted from

  • 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.
    Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation (2014), J. Biol. Chem., 289, 10919-10929.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.4

Cloned(Commentary)

Cloned (Comment) 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 (Comment) Organism
ATP sulfurylase isoform 1 in complex with APS, X-ray diffraction structure determination and analysis Glycine max

Protein Variants

Protein Variants Comment 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 Comment 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 Comment 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 Comment Organism Structure
Mg2+ required Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Comment Textmining
Arabidopsis thaliana Q9LIK9 isozyme atps1
-
Arabidopsis thaliana Col-0 Q9LIK9 isozyme atps1
-
Glycine max Q8SAG1 ATP sulfurylase isoform 1
-

Purification (Commentary)

Purification (Comment) 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 Comment 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
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment 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 Arabidopsis thaliana
0.135
-
 recombinant ATPS1 mutant L122V, pH 8.0, 25°C Arabidopsis thaliana
0.14
-
 recombinant ATPS1 mutant T198A, pH 8.0, 25°C Arabidopsis thaliana
0.14
-
 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits

Subunits Comment Organism
homodimer ATP sulfurylase domain structure and oligomerization, overview Glycine max

Synonyms

Synonyms Comment Organism
ATP sulfurylase
-
 Glycine max
ATP sulfurylase
-
 Arabidopsis thaliana
ATPS1
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Glycine max
25
-
 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Glycine max
8
-
 assay at Arabidopsis thaliana

General Information

General Information Comment 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 Glycine max
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
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