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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
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
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
in plants, gene families encode multiple isoforms of ATP sulfurylase with varied expression patterns and organelle localization
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
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
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
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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
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
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
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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
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
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. Transcription regulation of Arabidopsis thaliana APS genes by external factors, detailed overview
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
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 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
molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
metabolism
sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase
metabolism
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
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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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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 catalyzes the first reaction in the activation of inorganic sulfate
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metabolism
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molecular mechanisms differentiating sulfate assimilation pathways in plastids and cytosol in plants, overview
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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
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metabolism
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ATP sulfurylase precedes adenosine 5'-phosphosulfate reductase in the sulfate assimilation pathway. The ATPS1 transcript variation is controlled in cis
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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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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
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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
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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
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
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
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
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 sulfur assimilation pathway provides sulfide for a range of biosynthetic pathways that supply methionine, glutathione, ironsulfur clusters, vitamin cofactors such as biotin and thiamin, and multiple specialized metabolites such as glucosinolates
physiological function
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comparative analysis of both enzyme characteristics and growth parameters of sulfate-reducing bacteria isolated from various ecotopes such as soils, corrosion products and human large intestine
physiological function
transgenic soybean seeds overexpressing ATP sulfurylase without the transit peptide show predominant localization in the cytoplasm. Transgenic plants accumulate very low levels of the beta-subunit of beta-conglycinin. The accumulation of the cysteine-rich Bowman-Birk protease inhibitor is several fold higher in transgenic soybean plants. Their overall protein content is lowered by about 3%. 84 out of 124 seed metabolites are present in higher amounts and 40 are present in lower amounts in ATP sulfurylase overexpressing seeds compared to the wild-type seeds. ATP sulfurylase overexpressing seeds contain significantly higher amounts of phospholipids, lysophospholipids, diacylglycerols, sterols, and sulfolipids. Overexpression of ATP sulfurylase results in 37-52% and 15-19% increases in the protein-bound cysteine and methionine content of transgenic seeds, respectively
physiological function
upon expression in Medicago sativa, transgenic plants grow more efficiently compared with their non-transgenic counterparts under heavy metal stress conditions, with significant increase in shoot and root dry weight. Transgenic lines show higher levels of heavy metal accumulation in shoot and root tissues. The transgenic lines are fertile and do not exhibit any apparent morphological abnormality
physiological function
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the enzyme is dispensible for growth on reduced sulfur compounds due to the presence of an alternate sulfite-oxidizing pathway in Allochromatium vinosum
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physiological function
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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
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physiological function
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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
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additional information
sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, 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
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
additional information
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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
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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
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three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
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three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
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three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
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three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
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three-dimensional model structure comparison of ATPS-B from Thalassiosira pseudonana and ATPS-A from Synechocystis sp., overview
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sulfate contents and genetic regulation of ATPS1 in different Arabidopsis thaliana genotypes, overview
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