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Enzyme Nomenclature
Information on EC 2.7.7.4 - sulfate adenylyltransferase
for references in articles please use BRENDA:EC2.7.7.4
Word Map on EC 2.7.7.4
- 2.7.7.4
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two-phase
- glycol
- peg
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bottom
- dextran
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sulfotransferase
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peg-rich
- sulfite
- vr
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liquid-liquid
- selenate
- k2hpo4
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assimilatory
- chrysogenum
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mgppi
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counter-current
- juncea
- agriculture
- chlorate
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sults
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screw
- phytochelatins
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
2.7.7.4
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RECOMMENDED NAME
GeneOntology No.
sulfate adenylyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + sulfate = diphosphate + adenylyl sulfate
sequential bi-bi reaction with ATP being the first substrate bound and adenylysulfate the last product released
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ATP + sulfate = diphosphate + adenylyl sulfate
random sequence for the forward reaction with adenylylsulfate release being partially rate limiting
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ATP + sulfate = diphosphate + adenylyl sulfate
sequential reaction mechanism in which both substrates bind before any product is released
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ATP + sulfate = diphosphate + adenylyl sulfate
obligatory ordered kinetic mechanism with MgATP2- adding before MoO42- or SO42- and Mg-diphosphate leaving before AMP + MoO42- or adenosine 5'-phosphosulfate
Brassica capitata
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ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
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ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
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ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
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ATP + sulfate = diphosphate + adenylyl sulfate
ordered reaction mechanism, in which ATP is the first substrate to react with the enzyme and diphosphate is the first product released
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ATP + sulfate = diphosphate + adenylyl sulfate
analysis of the bi bi substrate kinetic mechanism of GmATPS1. The enzyme shows a kinetic mechanism in which ATP and APS are the first substrates bound in the forward and reverse reactions, respectively
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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
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ATP + sulfate = diphosphate + adenylyl sulfate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9012-39-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mixed SRB (sulfate reducing bacteria)-containing consortium consisting mainly of the Desulfovibrio genus
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. The absence of this residue in the ATPS-A of the freshwater cyanobacterium Synechocystis sp. is consistent with its lack of regulation. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-A is typical of all freshwater cyanobacteria and marine-coastal cyanobacteria that do not belong to the genera Synechococcus and Prochlorococcus, sequence alignment of ATPS from the algal species, overview
evolution
an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-B belongs to the oceanic cyanobacteria of the genera Synechococcus and Prochlorococcus and to all eukaryotic algae except dinoflagellates, sequence alignment of ATPS from the algal species, overview
evolution
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in plants, gene families encode multiple isoforms of ATP sulfurylase with varied expression patterns and organelle localization
evolution
despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes. The sat-aprMBA gene locus in Allochromatium vinosum and other phototrophic members of the family Chromatiaceae, overview
evolution
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despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes. The sat-aprMBA gene locus in Allochromatium vinosum and other phototrophic members of the family Chromatiaceae, overview
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evolution
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an ATPS type A is mostly present in freshwater cyanobacteria, with four conserved cysteine residues. Oceanic cyanobacteria and most eukaryotic algae instead, possess an ATPS-B containing seven to ten cysteines, five of them are conserved, but only one in the same position as ATPS-A. Oceanic cyanobacteria have ATPS-B structurally and functionally closer to that from most of eukaryotic algae than to the ATPS-A from other cyanobacteria suggests that life in the sea or freshwater may have driven the evolution of ATPS. ATPS-B belongs to the oceanic cyanobacteria of the genera Synechococcus and Prochlorococcus and to all eukaryotic algae except dinoflagellates, sequence alignment of ATPS from the algal species, overview
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malfunction
the suppression of PAPSS1 and 2 decreases the levels of obligate cofactor and sulfate donor PAPS and reduce cellular sulfotransferase activity. Endogenous SULT2A1 is not upregulated in PAPSS1/2 double knockdown HepG2 cells, whereas the amount of UGT2B4 mRNA is significantly increased. Mechanism(s) responsible for the PAPSS1/2 knockdown-mediated upregulation of human UGT2B4, overview
malfunction
plants with the Bay allele of ATPS1 accumulate lower steady-state levels of ATPS1 transcript than those with the Sha allele, which leads to lower enzyme activity and, ultimately, the accumulation of sulfate. Examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher. The contents of glutathione are not affected by the disruption of ATPS1 in Col-0 but are lower in Shahdara and both HIF004 lines compared with Bay-0 and the Col-0 genotypes
malfunction
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plants with the Bay allele of ATPS1 accumulate lower steady-state levels of ATPS1 transcript than those with the Sha allele, which leads to lower enzyme activity and, ultimately, the accumulation of sulfate. Examination of ATPS1 sequences of varieties Bay-0 and Shahdara identifying two deletions in the first intron and immediately downstream the gene in Bay-0 shared with multiple other Arabidopsis accessions. The average ATPS1 transcript levels are lower in these accessions than in those without the deletions, while sulfate levels are significantly higher. The contents of glutathione are not affected by the disruption of ATPS1 in Col-0 but are lower in Shahdara and both HIF004 lines compared with Bay-0 and the Col-0 genotypes
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metabolism
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the first enzymatic reaction in the sulfur assimilation pathway of plants is the non-reductive adenylation of sulfate catalysed by ATP sulfurylase to yield adenylyl sulfate, APS, and diphosphate. The enzyme also catalyzes the next step, producing ADP and 3'-phosphoadenylyl sulfate from ATP and adenylyl sulfate, cf. EC 2.7.1.25
metabolism
all sulfation reactions rely on active sulfate in the form of 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate is converted to the sulfonucleotide adenylyl sulfate, APS, by the ubiquitous ATP sulfurylase. APS represents a metabolic branchpoint in bacteria and plants, where it is reduced by APS reductase to sulfite, and finally incorporated into primary metabolites after further reduction. Alternatively, APS is phosphorylated by APS kinase to the universal sulfate donor PAPS. In metazoans and humans, ATP sulfurylase and APS kinase reside on one polypeptide, the bifunctional PAPS synthase. All eukaryotic sulfotransferases depend on the provision of active sulfate inthe form of 3?-phospho-adenosine-5'-phosphosulfate (PAPS) for their proper action. The importance of PAPS for sulfation can rival that of ATP for phosphorylation processes. Various regulatory roles of APS in the overall process of PAPS biosynthesis; all sulfation reactions rely on active sulfate in the form of 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Sulfate is converted to the sulfonucleotide adenylyl sulfate, APS, by the ubiquitous ATP sulfurylase. APS represents a metabolic branchpoint in bacteria and plants, where it is reduced by APS reductase to sulfite, and finally incorporated into primary metabolites after further reduction. Alternatively, APS is phosphorylated by APS kinase to the universal sulfate donor PAPS. In metazoans and humans, ATP sulfurylase and APS kinase reside on one polypeptide, the bifunctional PAPS synthase. All eukaryotic sulfotransferases depend on the provision of active sulfate inthe form of 3'-phospho-adenosine-5'-phosphosulfate (PAPS) for their proper action. The importance of PAPS for sulfation can rival that of ATP for phosphorylation processes. Various regulatory roles of APS in the overall process of PAPS biosynthesis
metabolism
molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors; as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
metabolism
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as the first committed step of S-assimilation, ATP-sulfurylase (ATP-S) catalyzes sulfate activation and yields the activated high-energy compound adenosine-5'-phosphosulfate that is reduced to sulfide and incorporated into cysteine. In turn, cysteine acts as a precursor or donor of reduced S for arange of S-compounds such as methionine, glutathione (GSH), homo-GSH,and phytochelatins. Schematic representation of pathway of sulfate assimilation, reaction catalyzed by ATP-sulfurylase (ATP-S), and its regulation by major factors
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
metabolism
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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
metabolism
ATP sulfurylase precedes adenosine 5'-phosphosulfate reductase in the sulfate assimilation pathway. The ATPS1 transcript variation is controlled in cis
metabolism
sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase
metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
metabolism
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sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase
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metabolism
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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; ATP sulfurylase precedes adenosine 5'-phosphosulfate reductase in the sulfate assimilation pathway. The ATPS1 transcript variation is controlled in cis; molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
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metabolism
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ATP sulfurylase catalyzes the first reaction in the activation of inorganic sulfate
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physiological function
ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-A of the freshwater cyanobacterium Synechocystis sp. shows that the lack of residue Cys247 causes a lack of regulation
physiological function
ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-B from the marine diatom Thalassiosira pseudonana shows that the residue Cys247 is presumably involved in the redox regulation
physiological function
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the sulfur assimilation pathway provides sulfide for a range of biosynthetic pathways that supply methionine, glutathione, iron–sulfur clusters, vitamin cofactors such as biotin and thiamin, and multiple specialized metabolites such as glucosinolates
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
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S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase; S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
-
S-compound-mediated role of enzyme ATP-S in plant stress tolerance, ATP-S-intrinsic regulation by major S-compounds, overview. Sulfur stands fourth in the list of major plant nutrients after N, P, and K, and its importance is being increasingly emphasized in agriculture and plant stress tolerance, because S-deficiency in agricultural-soils is becoming widespread globally. Plant harbored-S is metabolically inert and is of no significance if it is not efficiently assimilated into physiologically/biochemically exploitable organic forms that is performed by the process of S-assimilation involving the ATP-sulfurylase
physiological function
sulfate content in Arabidopsis thaliana is controlled by two genes encoding subsequent enzymes in the sulfate assimilation pathway but using different mechanisms, variation in amino acid sequence and variation in expression levels
physiological function
the enzyme is dispensible for growth on reduced sulfur compounds due to the presence of an alternate sulfite-oxidizing pathway in Allochromatium vinosum
physiological function
-
the enzyme is dispensible for growth on reduced sulfur compounds due to the presence of an alternate sulfite-oxidizing pathway in Allochromatium vinosum
-
physiological function
-
sulfate content in Arabidopsis thaliana is controlled by two genes encoding subsequent enzymes in the sulfate assimilation pathway but using different mechanisms, variation in amino acid sequence and variation in expression levels
-
physiological function
-
ATP sulfurylase (ATPS) catalyzes the first step of sulfur assimilation in photosynthetic organisms, role of cysteines on the regulation of the different algal enzymes ATPS-A and ATPS-B. The LC-MS/MS analysis of ATPS-B from the marine diatom Thalassiosira pseudonana shows that the residue Cys247 is presumably involved in the redox regulation
-
additional information
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
-
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
-
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
additional information
the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase; the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase
additional information
the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase; the bifunctional PAPS synthase comprises a C-terminal ATP sulfurylase domain and an N-terminal APS kinase domain connected by a short irregular linker, no intermediate channeling by the human enzyme. The human PAPS synthases, PAPS synthase 1 (PAPSS1) and PAPS synthase 2 (PAPSS2) are bifunctional enzymes that consist of ATP sulfurylase and APS kinase domains connected by a flexible linker. Adenylyl sulfate, APS, is a highly specific stabilizer of bifunctional PAPS synthases. APS most likely stabilizes the APS kinase part of these proteins by forming a dead-end enzyme-ADP-APS complex at APS concentrations between 0.0005 and 0.005 mM. At higher concentrations, APS may bind to the catalytic centers of ATP sulfurylase
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
additional information
sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, overview
additional information
-
sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, overview
-
additional information
-
three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
MgATP2- + adenylyl sulfate
MgADP- + 3-phosphoadenylyl sulfate
-
reaction carried out by the APS kinase activity of the bifunctional enzyme
-
-
r
MgATP2- + sulfate
magnesium diphosphate + adenylyl sulfate
-
reaction carried out by the ATP sulfurylase activity of the bifunctional enzyme
-
-
r
MgATP2- + sulfate
Mg-diphosphate + adenylyl sulfate
-
-
-
r
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
-
followed by nonenzymatic reaction of adenylylmolybdate with H2O to AMP and molybdate
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + CrO42-
AMP + adenylyl-chromate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
mechanism of molybdolysis is a sequential type in which MgATP2- binds to the enzyme before molybdate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + MoO42-
AMP + adenylylmolybdate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + SeO42-
AMP + adenylylselenate
-
20% of the activity with SO42-
reaction is followed by nonenzymatic reaction of adenylylselenate with H2O to AMP and SeO42-
?
ATP + sulfate
diphosphate + adenylyl sulfate
it is shown that AcATPS1 and adenosine-5'-phopshosulfate reductase (AcAPR1) from Allium cepa form protein-protein complexes in vitro, thereby a slight stimulation AcATPS1 activity is detectable
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
reaction is carried out in an anaerobic bioreactor
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
-
X-ray chrystal structure of a complex between ATPS and its associated regulatory G protein (CysN) is analysed, both proteins are in tight association, with CysD bound to a central cavity formed by the junction of the three domains of CysN
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
catalyzes a reaction in the sulfate assimilation pathway. The chloroplast isoenzyme, representing the more abundant enzyme form, declines in parallel with APS reductase activity during aging of leaf. The cytosolic isoenzyme plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfate reactions
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
adenylylsulfate transgenics are more tolerant than wild-type to As(III), As(V), Cd2+, Cu2+, Hg2+, and Zn2+, but less tolerant to Mo6+ and V6+. The APS seedlings has up to 2.5-fold higher shoot concentrations of As(III), As(V), Hg2+, Mo6+, Pb2+, and V6+, and somewhat lower Cr3+ levels. Mature APS plants contained up to 2.5fold higher shoot concentrations of Cd2+, Cr3+, Cu2+, Mo6+, V6+, and W than wild type. They also contain 1.5fold to 2fold higher levels of the essential elements Fe, Mo, and S in most of the treatments
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
regulation of ATP sulfurylase activity and SO42- uptake by S demand is related to GSH rather than to the GSH/GSSG ratio, and is distinct from the oxidative stress response
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
enzyme plays a crucial role in sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate metabolism
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the ATP sulfurylase-adenylylsulfate complex does not serve as a substrate for APS kinase, i.e. there is no substrate chanelling of APS between the two sulfate-activating enzymes
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
first enzyme of the two-step sulfate activation sequence
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
key enzyme of sulfate assimilation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes nucleotidyl transfer with inversion of configuration at phosphorus and with a stereoselectivity in excess of 94%
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
-
-
r
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
-
followed by nonenzymatic reaction of adenylyl-WO42- with H2O to AMP and WO42-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
ATP + WO42-
AMP + adenylyl-wolframate
-
the ATP-sulfurylase catalyzes the hydrolysis of ATP to AMP and diphosphate in presence of MoO42-, CrO42-, WO42- or SO32-. The rate of the reaction with MoO42- is almost 100fold faster than the rate with sulfate
-
-
?
dATP + SO42-
diphosphate + deoxyadenylylsulfate
-
-
-
-
?
diphosphate + adenylyl sulfate
ATP + sulfate
-
-
-
r
additional information
?
-
-
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
-
catalyzes the rate-limiting step in the assimilatory pathway for sulfate
-
-
-
additional information
?
-
no binding of diphosphate to enzyme GmATPS1
-
-
-
additional information
?
-
substrate binding structure analysis, overview
-
-
-
additional information
?
-
substrate binding structure analysis, overview
-
-
-
additional information
?
-
the bifunctional PAPS synthases 1 and 2 consist of an N-terminal adenosine-5'-phosphosulphate kinase domain and a C-terminal ATP sulphurylase domain connected by a short irregular linker
-
-
-
additional information
?
-
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
additional information
?
-
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
additional information
?
-
-
enzyme catalyzes ATP-diphosphate exchange reaction. The enzyme does notto catalyze the incorporation of diphosphate into ATP in the absence of SO42-. The enzyme catalyzes SeO42–dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
radioisotopic exchange between the adenosine 5'-sulfatophosphate and SO42- occurs only in the presence of either MgATP2- or diphosphate
-
-
-
additional information
?
-
-
sulfate is the only form of sulfur that catalyzes diphosphate-ATP exchange. The enzyme catalyzes diphosphate-dATP exchange. Selenate catalyzes diphosphate-ATP exchange, but no AMP is formed. Molybdate does not catalyze diphosphate-ATP exchange but AMP is formed
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + sulfate
diphosphate + adenylyl sulfate
O23324, Q43870, Q9LIK9, Q9S7D8
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
Q9LIK9
-
-
-
?
ATP + sulfate
diphosphate + adenylyl sulfate
I1LWX5, I1N6H7, I1NGL3, Q8SAG1
-
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
catalyzes a reaction in the sulfate assimilation pathway. The chloroplast isoenzyme, representing the more abundant enzyme form, declines in parallel with APS reductase activity during aging of leaf. The cytosolic isoenzyme plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfate reactions
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
constitutive enzyme
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
adenylylsulfate transgenics are more tolerant than wild-type to As(III), As(V), Cd2+, Cu2+, Hg2+, and Zn2+, but less tolerant to Mo6+ and V6+. The APS seedlings has up to 2.5-fold higher shoot concentrations of As(III), As(V), Hg2+, Mo6+, Pb2+, and V6+, and somewhat lower Cr3+ levels. Mature APS plants contained up to 2.5fold higher shoot concentrations of Cd2+, Cr3+, Cu2+, Mo6+, V6+, and W than wild type. They also contain 1.5fold to 2fold higher levels of the essential elements Fe, Mo, and S in most of the treatments
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
regulation of ATP sulfurylase activity and SO42- uptake by S demand is related to GSH rather than to the GSH/GSSG ratio, and is distinct from the oxidative stress response
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
enzyme plays a crucial role in sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
energy-coupling mechanism-the interlocking catalytic cycles of the ATP sulfurylase-GTPase system
-
-
?
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate activation
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the enzyme catalyzes the first step of sulfate metabolism
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
the ATP sulfurylase-adenylylsulfate complex does not serve as a substrate for APS kinase, i.e. there is no substrate chanelling of APS between the two sulfate-activating enzymes
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
first enzyme of the two-step sulfate activation sequence
-
-
r
ATP + sulfate
diphosphate + adenylylsulfate
-
key enzyme of sulfate assimilation
-
-
r
diphosphate + adenylyl sulfate
ATP + sulfate
Q9LIK9
-
-
-
r
additional information
?
-
-
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
O67174
the enzyme may also function to produce 3'-phosphoadenosine 5'-phosphosulfate for sulfate ester formation or sulfate assimilation
-
-
-
additional information
?
-
-
catalyzes the rate-limiting step in the assimilatory pathway for sulfate
-
-
-
additional information
?
-
O43252
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
additional information
?
-
O95340
for human PAPS synthase 1, the steady-state concentration of APS is modelled to be 0.0016 mM, but this may increase up to 0.060 mM under conditions of sulfate excess. The APS concentration for maximal APS kinase activity is 0.015 mM
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cl-
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Co2+
Cobalt
Fe2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Mg2+
Mn2+
Zinc
Zn2+
Ca2+
-
stimulatory at low concentrations (40-120 mg/l), but toxic to ATPS activity at higher concentrations (4120 mg/l)
Cobalt
-
contains 1.89 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Cobalt
-
contains 1.53 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Mg2+
required; required; required; required
Mg2+
for APS synthesis assay contains 15 mM MgCl2, for ATP synthesis assay contains 5 mM MgCl2
Mg2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Mg2+
-
formation of ATP from diphosphate and adenylylsulfate is absolutely dependent upon the presence of Mg2+
Mg2+
-
divalent cation required, Mg2+ is optimal for bacteria
Mn2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
Zinc
-
contains 0.72 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Zinc
-
contains 1.38 mol of zinc per mol of protein; metalloprotein. Either cobalt or zinc binds endogenously at presumably equivalent metal binding sites and is tetrahedrally coordinated to one nitrogen and three sulfur atoms
Zinc
-
zinc ion is tetrahedrally coordinated by Cys294, Cys297, Cys306, and His310, and can not be removed from the protein by treatment with EDTA. The zinc ion binding site is far from the active site. Zinc ion chelation may contribute to the thermal stability of these ATPSs
Zn2+
-
no absolute requirement for metal ions, but activity is increased by Mn2+, Mg2+ and Zn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
adenylyl sulfate
APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site; APS, binding mode, overview. On the ATP sulfurylase domain that initially produces APS from sulfate and ATP, APS acts as a potent product inhibitor, being competitive with both ATP and sulfate. For the APS kinase domain that phosphorylates APS to PAPS, APS is an uncompetitive substrate inhibitor that can bind both at the ATP/ADP-binding site and the PAPS/APS-binding site
diacetyl
-
significant inhibition in the presence of borate, protection by adenosine 5'-phosphosulfate, ATP or MgATP2- plus nitrate
methylene blue
-
inactivated by light in presence of methylene blue, protection by adenosine 5'-phosphosulfate
N-Acetylimidazole
-
76% of the original activity can be restored by treatment with hydroxylamine
Phenylglyoxal
-
3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
thiosulfate
-
competitive with molybdate and noncompetitive with MgATP
adenosine 5'-phosphosulfate
-
potent product inhibition, competitive with both MgATP2- and MoO42- in molybdolysis assay
adenosine 5'-phosphosulfate
-
potent product inhibitor, competitive with respect to MgATP2-, and a mixed type inhibitor with respect to molybdate
ADP
-
linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP
AMP
-
linear competitive inhibitor with respect to SO42-, uncompetitive with respect to ATP
ATP
-
MgATP2- is the actual substrate, free ATP is an inhibitor of the forward reaction
ATP
-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
ClO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
ClO4-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
ClO4-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
ClO4-
-
linear competitive inhibitor with respect to SO42- and uncompetitive with respect to ATP
FSO3-
-
competitive with SO42- or MoO42-, competitive against MgATP2-
FSO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
MgATP2-
-
competitive with respect to adenosine 5'-phosphosulfate; mixed-type with respect to diphosphate
NEM
-
0.15 mM, rapid decrease in activity of wild-type enzyme (t1/2: 45 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min
NO3-
-
competitive with SO42- and apparently uncompetitive with respect to MgATP2-
NO3-
-
linear competitive inhibitor with respect to SO42- and uncompetitive with respect to ATP
S2O32-
-
dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2-
SO42-
-
product inhibitor in formation of ATP from diphosphate and adenylylsulfate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
-
FSO3-
-
activates in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
S2O32-
-
activates SO42–dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation; the enzyme responds to sulfate starvation, increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea, but not to increased light irradiation
-
additional information
-
the enzyme responds to increased cadmium level, increased salinity, and infection by Phytopthorainfestans and/or Botrytiscinerea
-
additional information
-
the enzyme responds to sulfate starvation, and increased salinity, but not to increased light irradiation, H2O2, and glutathione level
-
additional information
-
enzyme activity is positively correlated with seed yield and influenced by sulfur assimilation
-
additional information
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress; the enzyme responds to chilling or cold stress
-
additional information
-
the enzyme responds to increased light irradiation
-
additional information
-
the enzyme in cultured cells responds to sulfate starvation
-
additional information
-
the enzyme responds to increased cadmium level
-
additional information
-
the enzyme responds to increased glutathione level
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
adenylylsulfate
-
pH 8.0, 30°C, truncated mutant enzyme del396-573
0.027
ATP
-
pH 8.0, 30°C, molybdolysis, truncated mutant enzyme del396-573; pH 8.0, 30°C, molybdolysis, wild-type enzyme
0.21
ATP
-
pH 8.0, 30°C, synthesis of adenylylsulfate, wild-type enzyme
2.6
ATP
-
pH 8.0, 30°C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573
0.61
SeO42-
-
pH 7.8, 37°C, SeO42–dependent ATP-diphosphate exchange reaction