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3'-phosphoadenosine 5'-phosphosulfate + dithioerythritol
?
-
Substrates: -
Products: -
?
3'-phosphoadenosine 5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-bisphosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
Substrates: recombinant enzyme in transgenic Arabidopsis thaliana plants
Products: -
?
5'-adenylylsulfate + dithioerythritol
adenosine 5'-monophosphate + sulfite + oxidized dithioerythritol
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
5'-adenylylsulfate + glutathione + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
adenosine 5'-phosphosulfate + glutathione
?
-
Substrates: PpAPR-B is much more active with adenosine 5'-phosphosulfate as a substrate than with 3'-phosphoadenosine 5'-phosphosulfate
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
adenylyl sulfate + DTT
?
-
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
AMP + sulfite + glutathione disulfide
adenylyl sulfate + 2 glutathione
Substrates: -
Products: -
?
cystine + glutathione
cysteine + glutathione disulfide
Substrates: catalyzed by the holoenzyme APR1p and the C-domain
Products: -
?
dehydroascorbate + glutathione
ascorbate + glutathione disulfide
Substrates: catalyzed by the holoenzyme APR1p and the C-domain
Products: -
?
hydroxyethyldisulfide + glutathione
?
Substrates: catalyzed by the holoenzyme APR1p and the C-domain
Products: -
?
insulin disulfide + glutathione
insulin + glutathione disulfide
Substrates: catalyzed by the C-domain, not by the holoenzyme APR1p or the R-domain
Products: -
?
oxidized ribonucleotide reductase + glutathione
reduced ribonucleotide reductase + glutathione disulfide
Substrates: catalyzed by the C-domain, not by the holoenzyme APR1p or the R-domain
Products: -
?
additional information
?
-
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: 50fold lower activity than with 5'-adenylylsulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
3'-phosphoadenosine-5'-phosphosulfate + glutathione
adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
Substrates: no activity with 3'-phosphoadenosine-5'-phosphosulfate
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: enzyme is involved in reductive sulfate assimilation, pathway overview
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
Substrates: catalyzed by the holoenzyme APR1p, not by the C-domain
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: enzyme is involved in reductive sulfate assimilation, pathway overview
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
5'-adenylylsulfate + dithioerythritol
adenosine 5'-monophosphate + sulfite + oxidized dithioerythritol
-
Substrates: -
Products: -
?
5'-adenylylsulfate + dithioerythritol
adenosine 5'-monophosphate + sulfite + oxidized dithioerythritol
-
Substrates: -
Products: -
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
-
Substrates: -
Products: -
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
-
Substrates: -
Products: -
ir
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
-
Substrates: -
Products: -
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
?
5'-adenylylsulfate + glutathione + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
r
5'-adenylylsulfate + glutathione + glutathione
adenosine monophosphate + sulfite + oxidized glutathione
-
Substrates: -
Products: -
r
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
Substrates: -
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: sulfate assimilation pathway in Physcomitrella patens, overview
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: substrate binding structure, modelling, overview
Products: -
?
additional information
?
-
Substrates: enzyme is involved in sulfate assimilation
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in sulfate assimilation
Products: -
?
additional information
?
-
-
Substrates: APR is the key enzyme of sulfate assimilation, extensive posttranscriptional regulation of plant APR, e.g. by salt stress, sulfate assimilation pathway is controlled by a complex network of multiple signals on different regulatory levels, overview
Products: -
?
additional information
?
-
Substrates: GSH is docked into the AtAPR1 redox domain active site by manual docking, superimposing the structures of glutaredoxin bound with GSH on that of the AtAPR1 redox domain. The structure of cGrx1 complexed with GSH (PDB code 4TR1) is used as a template. Interaction between GSH and the AtAPR1 redox domain is analyzed, binding structure analysis, overview
Products: -
-
additional information
?
-
-
Substrates: no activity with thioredoxin
Products: -
?
additional information
?
-
-
Substrates: the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in sulfate assimilation, influence of chilling stress on the intercellular distribution of assimilatory sulfate reduction and thiols, overview
Products: -
?
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5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
Substrates: recombinant enzyme in transgenic Arabidopsis thaliana plants
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
AMP + sulfite + glutathione disulfide
adenylyl sulfate + 2 glutathione
Substrates: -
Products: -
?
additional information
?
-
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: enzyme is involved in reductive sulfate assimilation, pathway overview
Products: -
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: enzyme is involved in reductive sulfate assimilation, pathway overview
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
Substrates: -
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + 2 glutathione
AMP + sulfite + glutathione disulfide
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: -
Products: -
?
adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
-
Substrates: sulfate assimilation pathway in Physcomitrella patens, overview
Products: -
?
additional information
?
-
Substrates: enzyme is involved in sulfate assimilation
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in sulfate assimilation
Products: -
?
additional information
?
-
-
Substrates: APR is the key enzyme of sulfate assimilation, extensive posttranscriptional regulation of plant APR, e.g. by salt stress, sulfate assimilation pathway is controlled by a complex network of multiple signals on different regulatory levels, overview
Products: -
?
additional information
?
-
-
Substrates: the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in sulfate assimilation, influence of chilling stress on the intercellular distribution of assimilatory sulfate reduction and thiols, overview
Products: -
?
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additional information
the C-terminal domain of APR acts as a glutathione-dependent reductase. The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved alpha/beta thioredoxin fold, but not a glutaredoxin fold, crystal structure analysis, folding of the AtAPR1 redox domain is measured by circular dichroism (CD) spectroscopy, overview. The C-terminal redox domain of APR is more similar to thioredoxin than glutaredoxin. Molecular model of AtAPR1 redox domain in complex with GSH, structure modeling, overview
malfunction
a C-terminal truncated plant-type APR lacking the redox domain losses APR activity but recovers the function after the addition of thioredoxin
malfunction
transgenic plants overexpressing APR2 show improved Cd tolerance, whereas knockout of APR2 have reduced Cd tolerance. APR2-overexpressing plants with increased Cd accumulation and tolerance show higher glutathione (GSH) and phytochelatin (PC) levels than the wild-type and apr2 mutant plants, but lower H2O2 and TBARS contents upon Cd exposure. Moreover, exogenous GSH application effectively rescued Cd hypersensitivity in APR2-knockout plants. Further analysis showed that buthionine sulfoximine (BSO, an inhibitor of GSH synthesis) treatment completely eliminated the enhanced Cd tolerance phenotypes of APR2-overexpressing plants, implying that APR2-mediated enhanced Cd tolerance is GSH-dependent. In addition, overexpression of the APR2 leads to elevated expressions of the GSH/PC synthesis related genes under Cd stress
malfunction
-
transgenic plants overexpressing APR2 show improved Cd tolerance, whereas knockout of APR2 have reduced Cd tolerance. APR2-overexpressing plants with increased Cd accumulation and tolerance show higher glutathione (GSH) and phytochelatin (PC) levels than the wild-type and apr2 mutant plants, but lower H2O2 and TBARS contents upon Cd exposure. Moreover, exogenous GSH application effectively rescued Cd hypersensitivity in APR2-knockout plants. Further analysis showed that buthionine sulfoximine (BSO, an inhibitor of GSH synthesis) treatment completely eliminated the enhanced Cd tolerance phenotypes of APR2-overexpressing plants, implying that APR2-mediated enhanced Cd tolerance is GSH-dependent. In addition, overexpression of the APR2 leads to elevated expressions of the GSH/PC synthesis related genes under Cd stress
-
metabolism
in Arabidopsis there are three isoenzymes of APR (APR1, 2, and 3), of which APR2 is the major one in the sulfate reduction. Isozyme APR2 positively regulates cadmium tolerance through glutathione-dependent pathway
metabolism
in contrast to the cooperation of a sulfonucleotide reductase and a thioredoxin in prokaryote systems, in plants, the protein involved in the pathway is only a single polypeptide which consists of two distinct domains: a sulfonucleotide reductase-like one and a thioredoxin-like one
metabolism
-
in Arabidopsis there are three isoenzymes of APR (APR1, 2, and 3), of which APR2 is the major one in the sulfate reduction. Isozyme APR2 positively regulates cadmium tolerance through glutathione-dependent pathway
-
physiological function
overexpression of isoform Apr2 results in enhanced cotyledon greening and fresh weight increase when plants are treated with high glucose. A T-DNA insertion mutant line shows delayed greening and fresh weight growth inhibition in response to glucose and to 2-deoxyglucose. The expression of glucose responsive genes, hexokinase 1, phenylalanine ammonia lyase 1 and pathogenesis related gene 5, is elevated in Apr2-overexpressing and wild-type plants in response to glucose treatment, while in the T-DNA insertion mutant line the transcript level for these genes decreases. Apr2-overexpressing plants display delayed flowering under long day condition
physiological function
adenosine 5'-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. APR activity is downregulated to avoid tissue injury by a negative feedback regulation, a mechanism associated with metabolic changes that cause reduced GSH concentration and the accumulation of sulfate
physiological function
APR2 regulates Cd accumulation and tolerance possibly through modulating GSH-dependent antioxidant capability and Cd-chelation machinery in Arabidopsis thaliana. APR2 can be exploited for engineering heavy metal-tolerant plants in phytoremediation. APR2-mediated enhanced Cd tolerance is GSH-dependent
physiological function
-
chloroplast-localized adenosine-5'-phosphosulphate reductase (APR) generates sulfite and plays a pivotal role in reduction of sulfate to cysteine. The increases in APR activity in response to sulfite infiltration into wild-type and sulfite oxidase (SO)-deficient mutant leaves result in an increase in endogenous sulfite, indicating that APR has an important role in sulfite-induced increases in stomatal aperture. The importance of APR and SO and the significance of sulfite concentrations in water loss are further demonstrated during rapid, harsh drought stress in root-detached wild-type, gr2 and SO transgenic plants. Effects of sulfite infiltration on water status and sulfite accumulation in wild-type and sulfite oxidase overexpressing and deficient mutant leaves, overview
physiological function
-
chloroplast-localized adenosine-5'-phosphosulphate reductase (APR) generates sulfite and plays a pivotal role in reduction of sulfate to cysteine. The increases in APR activity in response to sulfite infiltration into wild-type and sulfite oxidase (SO)-deficient mutant leaves result in an increase in endogenous sulfite, indicating that APR has an important role in sulfite-induced increases in stomatal aperture. The importance of APR and SO and the significance of sulfite concentrations in water loss are further demonstrated during rapid, harsh drought stress in root-detached wild-type, gr2 and SO transgenic plants. Effects of sulfite infiltration on water status and sulfite accumulation in wild-type and sulfite oxidase overexpressing and deficient mutant leaves, overview
-
physiological function
-
APR2 regulates Cd accumulation and tolerance possibly through modulating GSH-dependent antioxidant capability and Cd-chelation machinery in Arabidopsis thaliana. APR2 can be exploited for engineering heavy metal-tolerant plants in phytoremediation. APR2-mediated enhanced Cd tolerance is GSH-dependent
-
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additional information
-
construction of transgenic Arabidopsis thaliana plants expressing the active enzyme from Pseudomonas aeruginosa in the chloroplasts, the plants show reduced fresh and dry weight, delayed germination, smaller leaves, slightly reduced fertility, and increased enzyme activity and sulfate reduction accumulating of sulfite, thiosulfate, cysteine, gamma-glutamylcysteine, and glutathione, feeding of O-acetylserine leads to increased accumulation of sulfite and thiosulfate in the transgenic plants, phenotype alterations, overview
additional information
gene APR1, the holoenzyme APR1p as well as the C-domain alone can complement the cysteine auxotrophy of an Escherichia coli cysH mutant strain, substituting for glutaredoxin, if the mutant is capable of producing glutathione, cysH encodes the 5'-phosphoadenylylsulfate reductase in Escherichia coli
additional information
-
gene APR1, the holoenzyme APR1p as well as the C-domain alone can complement the cysteine auxotrophy of an Escherichia coli cysH mutant strain, substituting for glutaredoxin, if the mutant is capable of producing glutathione, cysH encodes the 5'-phosphoadenylylsulfate reductase in Escherichia coli
additional information
-
regulation of APR by NaCl is not affected in mutant plants deficient in the abscisic acid synthesis, but APR is induced in mutant plants deficient in jasmonate, salicylate, ethylene, cytokinin, and auxin signaling, while the enzyme activity remians unaltered, the induction by salt is abolished in mutant plants deficient in gibberellic acid signaling, overview
additional information
generation of the APR2 T-DNA insertion mutant (apr2-1), knockout of isozyme APR2 reduces the overall APR activity by 80%, phenotype, overview
additional information
-
generation of the APR2 T-DNA insertion mutant (apr2-1), knockout of isozyme APR2 reduces the overall APR activity by 80%, phenotype, overview
-
additional information
-
construction of APR-B knockout plants, the mutant plants are able to grow on sulfate as a sole sulfur source, and the content of low molecular weight thiols is not different from wild-type plants. However, when treated with low concentrations of cadmium, the APR-B knockout plants are more sensitive than wild-type plants, phenotype, overview
additional information
-
construction of transgenic Arabidopsis thaliana plants expressing the active enzyme from Pseudomonas aeruginosa in the chloroplasts, the plants show reduced fresh and dry weight, delayed germination, smaller leaves, slightly reduced fertility, and increased enzyme activity and sulfate reduction accumulating of sulfite, thiosulfate, cysteine, gamma-glutamylcysteine, and glutathione, feeding of O-acetylserine leads to increased accumulation of sulfite and thiosulfate in the transgenic plants, phenotype alterations, overview
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Setya, A.; Murillo, M.; Leustek, T.
Sulfate reduction in higher plants: Molecular evidence for a novel 5'-adenylylsulfate reductase
Proc. Natl. Acad. Sci. USA
93
13383-13388
1996
Arabidopsis thaliana
brenda
Gutierrez-Marcos, J.F.; Roberts, M.A.; Campbell, E.I.; Wray, J.L.
Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and "APS reductase" activity
Proc. Natl. Acad. Sci. USA
93
13377-13382
1996
Arabidopsis thaliana
brenda
Prior, A.; Uhrig, J.F.; Heins, L.; Wiesmann, A.; Lillig, C.H.; Stoltze, C.; Soll, J.; Schwenn, J.D.
Structural and kinetic properties of adenylyl sulfate reductase from Catharanthus roseus cell cultures
Biochim. Biophys. Acta
1430
25-38
1999
Catharanthus roseus
brenda
Gao, Y.; Schofield, O.M.E.; Leustek, T.
Characterization of sulfate assimilation in marine algae focusing on the enzyme 5'-adenylylsulfate reductase
Plant Physiol.
123
1087-1096
2000
Arabidopsis thaliana, Brassica juncea, Conticribra weissflogii, Dunaliella salina, Emiliania huxleyi, Heterocapsa triquetra, Isochrysis galbana, Tetraselmis sp., Thalassiosira oceanica, Ulva intestinalis
brenda
Suter, M.; von Ballmoos, P.; Kopriva, S.; Op den Camp, R.; Schaller, J.; Kuhlemeier, C.; Schurmann, P.; Brunold, C.
Adenosine 5'-phosphosulfate sulfotransferase and adenosine 5'-phosphosulfate reductase are identical enzymes
J. Biol. Chem.
275
930-936
2000
Lemna minor
brenda
Kopriva, S.; Jones, S.; Kopriva, A.; Suter, M.; von Ballmoos, P.; Brander, K.; Flueckiger, J.; Brunold, C.
Influence of chilling stress on the intercellular distribution of assimilatory sulfate reduction and thiols in Zea mays
Plant Biol.
3
24-31
2001
Zea mays
-
brenda
Tsakraklides, G.; Martin, M.; Chalam, R.; Tarczynski, M.C.; Schmidt, A.; Leustek, T.
Sulfate reduction is increased in transgenic Arabidopsis thaliana expressing 5'-adenylylsulfate reductase from Pseudomonas aeruginosa
Plant J.
32
879-889
2002
Arabidopsis thaliana, Pseudomonas aeruginosa
brenda
Bick, J.A.; Aeslund, F.; Chen, Y.; Leustek, T.
Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase
Proc. Natl. Acad. Sci. USA
95
8404-8409
1998
Arabidopsis thaliana (P92979), Arabidopsis thaliana
brenda
Sun, M.; Leyh, T.S.
Channeling in sulfate activating complexes
Biochemistry
45
11304-11311
2006
Mycobacterium tuberculosis
brenda
Schiffer, A.; Fritz, G.; Kroneck, P.M.; Ermler, U.
Reaction mechanism of the iron-sulfur flavoenzyme adenosine-5-phosphosulfate reductase based on the structural characterization of different enzymatic states
Biochemistry
45
2960-2967
2006
Archaeoglobus fulgidus
brenda
Kim, S.K.; Gomes, V.; Gao, Y.; Chandramouli, K.; Johnson, M.K.; Knaff, D.B.; Leustek, T.
The two-domain structure of 5-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity
Biochemistry
46
591-601
2007
Ulva intestinalis
brenda
Duperron, S.; Fiala-Medioni, A.; Caprais, J.C.; Olu, K.; Sibuet, M.
Evidence for chemoautotrophic symbiosis in a Mediterranean cold seep clam (Bivalvia: Lucinidae): comparative sequence analysis of bacterial 16S rRNA, APS reductase and RubisCO genes
FEMS Microbiol. Ecol.
59
64-70
2007
bacteria endosymbiont of Lucinoma aff. kazani (Q0KG00)
brenda
Chartron, J.; Carroll, K.S.; Shiau, C.; Gao, H.; Leary, J.A.; Bertozzi, C.R.; Stout, C.D.
Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5-phosphosulfate reductase
J. Mol. Biol.
364
152-169
2006
Pseudomonas aeruginosa
brenda
Senaratne, R.H.; De Silva, A.D.; Williams, S.J.; Mougous, J.D.; Reader, J.R.; Zhang, T.; Chan, S.; Sidders, B.; Lee, D.H.; Chan, J.; Bertozzi, C.R.; Riley, L.W.
5-Adenosinephosphosulphate reductase (CysH) protects Mycobacterium tuberculosis against free radicals during chronic infection phase in mice
Mol. Microbiol.
59
1744-1753
2006
Mycobacterium tuberculosis
brenda
Kopriva, S.; Fritzemeier, K.; Wiedemann, G.; Reski, R.
The putative moss 3'-phosphoadenosine-5'-phosphosulfate reductase is a novel form of adenosine-5-phosphosulfate reductase without an iron-sulfur cluster
J. Biol. Chem.
282
22930-22938
2007
Physcomitrium patens
brenda
Phartiyal, P.; Kim, W.S.; Cahoon, R.E.; Jez, J.M.; Krishnan, H.B.
The role of 5-adenylylsulfate reductase in the sulfur assimilation pathway of soybean: molecular cloning, kinetic characterization, and gene expression
Phytochemistry
69
356-364
2008
Glycine max
brenda
Wiedemann, G.; Koprivova, A.; Schneider, M.; Herschbach, C.; Reski, R.; Kopriva, S.
The role of the novel adenosine 5-phosphosulfate reductase in regulation of sulfate assimilation of Physcomitrella patens
Plant Mol. Biol.
65
667-676
2007
Physcomitrium patens
brenda
Koprivova, A.; North, K.A.; Kopriva, S.
Complex signaling network in regulation of adenosine 5-phosphosulfate reductase by salt stress in Arabidopsis roots
Plant Physiol.
146
1408-1420
2008
Arabidopsis thaliana
brenda
Chung, J.; Lee, H.; Leustek, T.; Knaff, D.; Kim, C.
The Arabidopsis thaliana adenosine 5'-phosphosulfate reductase 2 (AtAPR2) participates in flowering time and glucose response
J. Plant Biol.
58
128-136
2015
Arabidopsis thaliana (P92981)
-
brenda
Chen, F.F.; Chien, C.Y.; Cho, C.C.; Chang, Y.Y.; Hsu, C.H.
C-terminal redox domain of Arabidopsis APR1 is a non-canonical thioredoxin domain with glutaredoxin function
Antioxidants (Basel)
8
461
2019
Arabidopsis thaliana (P92979)
brenda
Xu, Z.; Wang, M.; Xu, D.; Xia, Z.
The Arabidopsis APR2 positively regulates cadmium tolerance through glutathione-dependent pathway
Ecotoxicol. Environ. Saf.
187
109819
2020
Arabidopsis thaliana (P92981), Arabidopsis thaliana Col-0 (P92981)
brenda
Bekturova, A.; Oshanova, D.; Tiwari, P.; Nurbekova, Z.; Kurmanbayeva, A.; Soltabayeva, A.; Yarmolinsky, D.; Srivastava, S.; Tureckova, V.; Strnad, M.; Sagi, M.
Adenosine 5' phosphosulfate reductase and sulfite oxidase regulate sulfite-induced water loss in Arabidopsis
J. Exp. Bot.
72
6447-6466
2021
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda