HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin)
for references in articles please use BRENDA:EC1.8.4.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.8.4.8 phosphoadenylyl-sulfate reductase (thioredoxin)IUBMB Comments
Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
Specify your search results
Word Map
- 1.8.4.8
-
sulfurylase
-
assimilatory
-
sulfate-reducing
- o-acetylserine
-
sulfonucleotide
-
sulfur-oxidizing
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
3'-Phosphoadenosine 5'-phosphosulfate reductase, 3'-Phosphoadenylylsulfate reductase, 4Fe-4S adenylyl sulfate/phosphoadenylyl sulfate reductase, 5'-adenylylsulfate reductase, Adenosine 3'-phosphate 5'-phosphosulfate reductase, adenosine 5'-phosphosulfate reductase, Adenylyl phosphosulfate reductase, APR, APS reductase, CysH1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-Phosphoadenosine 5'-phosphosulfate reductase
3'-Phosphoadenylylsulfate reductase
Adenosine 3'-phosphate 5'-phosphosulfate reductase
-
-
-
-
Adenylyl phosphosulfate reductase
-
-
-
-
APR
APS reductase
PAdoPS reductase
-
-
-
-
PAPS reductase
PAPS reductase, thioredoxin dependent
-
-
-
-
PAPS reductase, thioredoxin-dependent
-
-
-
-
PAPS sulfotransferase
-
-
-
-
Phospho-adenylylsulfate (PAPS) reductase
-
-
-
-
Phospho-adenylylsulfate reductase
-
-
-
-
Reductase, 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
Thioredoxin: 3'-phospho-adenylylsulfate reductase
-
-
-
-
Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase
-
-
-
-
3'-Phosphoadenosine 5'-phosphosulfate reductase
-
-
-
-
3'-Phosphoadenylylsulfate reductase
-
-
-
-
PAPS reductase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
from the kinetic data it is concluded that the enzyme follows an ordered mechanism with thioredoxin as the first substrate followed by 5-phosphoadenosine 3-phosphosulfate as the second
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
special ping-pong mechanism with 5-phosphoadenosine 3-phosphosulfate reacting with the reduced enzyme isomer in a Theorell-Chance mechanism
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism, Cys239 is the active site residue
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming)
Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9068-63-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl sulfate + glutaredoxin Grx
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx disulfide
-
poplar glutaredoxin, 33% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + glutaredoxin Grx1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx1 disulfide
-
Escherichia coli glutaredoxin, 70% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin hTrx1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin hTrx1 disulfide
-
human thioredoxin, 59% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin Trx1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx1 disulfide
-
Escherichia coli thioredoxin
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin Trx2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx2 disulfide
-
Escherichia coli thioredoxin, 38% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH1 disulfide
-
Arabidopsis thaliana thioredoxin, 18% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH2 disulfide
-
Arabidopsis thaliana thioredoxin, 23% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH3
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH3 disulfide
-
Arabidopsis thaliana thioredoxin, 154% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH4
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH4 disulfide
-
Arabidopsis thaliana thioredoxin, 45% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
adenosine 5'-phosphosulfate + thioredoxin
AMP + sulfite + oxidized thioredoxin
-
-
-
-
?
adenosine 5'-phosphosulfate + thioredoxin I
AMP + sulfite + oxidized thioredoxin I
-
-
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
enzyme catalyzes the first reductive step in sulfate assimilation
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
thioredoxin m from spinach
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
-
enzyme is involved in sulfur metabolism
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
-
essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
-
additional information
?
-
-
enzyme is essential for sulfate assimilation using phosphoadenosine 5'-phosphosulfate, not adenosine 5'-phosphosulfate, phylogenetic comparison of the 2 different groups, overview
-
-
-
additional information
?
-
-
enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
-
-
-
additional information
?
-
-
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
-
-
-
additional information
?
-
-
the redox potential does not determine specificity nor efficiency of the redoxins as reductant. The efficiency of PAPS reductase with various redoxins correlates strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces
-
-
-
additional information
?
-
-
thioredoxin I mutant W31A shows no detectable activity, whereas W31F, K36E, and D61N are able to serve as electron donors for the APR-catalyzed reaction but with lower turnover numbers than that exhibited by the wild type thioredoxin I. The Km for thioredoxin mutant R73E is increased by 7.7fold compared with wild type thioredoxin I
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
enzyme catalyzes the first reductive step in sulfate assimilation
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
-
enzyme is involved in sulfur metabolism
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
-
essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
-
-
-
additional information
?
-
-
enzyme is essential for sulfate assimilation using phosphoadenosine 5'-phosphosulfate, not adenosine 5'-phosphosulfate, phylogenetic comparison of the 2 different groups, overview
-
-
-
additional information
?
-
-
enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
-
-
-
additional information
?
-
-
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
-
in vitro, variant Grx1 is active similar to the thioredoxins, while Grx2 and Grx3 are not active, and a mutant form Grx1C14S is a poor cofactor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
-
iron-sulfur protein, each mole of protein contains 3.3 mol of Fe
Iron
-
the enzyme contains a [4Fe-4S] cluster per subunit, absolutely required for activity, constitution is altered in presence of oxygen, activity is restored after decomposition and reassembly
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 3',5'-bisphosphate
-
competitive with respect to 5-phosphoadenosine 3-phosphosulfate
oxidized glutathione
-
reversible inhibition, forms mixed disulfides with the enzymes active site residue Cys239, inactivation kinetics, inhibition is reversible by glutaredoxin, not by DTT, glutaredoxin together with glutathione exhibits regulatory function in vivo
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
-
required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo
additional information
-
The activity of 3'-phosphoadenosine 5'-phosphosulfate reductase is increased by sulfur starvation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0637
glutaredoxin Grx
-
pH 8.0, temperature not specified in the publication
-
0.0149
glutaredoxin Grx1
-
pH 8.0, temperature not specified in the publication
-
0.0681
thioredoxin hTrx1
-
pH 8.0, temperature not specified in the publication
-
0.01
thioredoxin I
-
wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
0.0137
thioredoxin Trx1
-
pH 8.0, temperature not specified in the publication
-
0.0342
thioredoxin Trx2
-
pH 8.0, temperature not specified in the publication
-
0.059
thioredoxin TrxH1
-
pH 8.0, temperature not specified in the publication
-
0.0431
thioredoxin TrxH2
-
pH 8.0, temperature not specified in the publication
-
0.0178
thioredoxin TrxH3
-
pH 8.0, temperature not specified in the publication
-
0.0261
thioredoxin TrxH4
-
pH 8.0, temperature not specified in the publication
-
0.0287
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.1054
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.0064
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.0107
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.0225
3'-phosphoadenylyl-sulfate
-
with cofactors Trx1, Trx2, or Grx1, pH 8.0
0.019
5-Phosphoadenosine 3-phosphosulfate
-
with thioredoxin from Saccharomyces cerevisiae as cosubstrate
0.021
5-Phosphoadenosine 3-phosphosulfate
-
with thioredoxin from E. coli as cosubstrate
0.0225
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
-
0.0606
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
-
0.0543
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
0.0675
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.149
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.335
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.172
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.382
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.146
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
-
0.421
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
-
0.174
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
0.219
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
adenosine 5'-phosphosulfate
-
mutant enzyme K144A, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5
2500
adenosine 5'-phosphosulfate
-
wild type enzyme, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (11385 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
-
reduction of the enzyme by dithiothreitol results in a shift of the apparent MW to 62000 without formation of an enzyme-thioredoxin complex, HPLC gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.0 A. The enzyme shows striking similarity to the structure of the ATP pyrophosphatase domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold
-
crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate reductase in complex with Escherichia coli thioredoxin 1 determined to 3.0 A resolution, crystals are grown by vapor diffusion in sitting drops
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K144A |
-
the mutation causes a 63000fold increase of kcat/KM and decreases the value of kmax by 270fold. Relative to the wild type enzyme, the affinity of adenosine 5’-phosphosulfate for K144A is decreased by 400fold
additional information
-
a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating column chromatography and Superdex 200 gel filtration
-
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
-
recombinant His10-tagged enzyme from strain BL21(DE3) by chelate affinity chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in strain BL21(DE3) as His-tagged protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
in Mycobacterium tuberculosis, APR is a validated target against the latent phase of infection
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwenn, J.D.; Krone, F.A.; Husmann, K.
Yeast PAPS reductase: properties and requirements of the purified enzyme
Arch. Microbiol.
150
313-319
1988
Saccharomyces cerevisiae
brenda
Savage, H.; Montoya, G.; Svensson, C.; Schwenn, J.D.; Sinning, I.
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases
Structure
5
895-906
1997
Escherichia coli
brenda
Montoya, G.; Svensson, C.; Savage, H.; Schwenn, J.D.; Sinning, I.
Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli
Acta Crystallogr. Sect. D
54
281-283
1998
Escherichia coli
brenda
Berendt, U.; Haverkamp, T.; Prior, A.; Schwenn, J.D.
Reaction mechanism of thioredoxin:3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis
Eur. J. Biochem.
233
347-356
1995
Escherichia coli
brenda
Niehaus, A.; Gisselmann, G.; Schwenn, J.D.
Primary structure of Synechococcus PCC 7942 PAPS reductase gene
Plant Mol. Biol.
20
1179-1183
1992
Synechococcus sp., Synechococcus sp. PCC 7942
brenda
Krone, A.; Westphal, G.; Schwenn, J.D.
Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli
Mol. Gen. Genet.
225
314-319
1991
Escherichia coli
brenda
Kopriva, S.; Buchert, T.; Fritz, G.; Suter, M.; Benda, R.; Schunemann, V.; Koprivova, A.; Schurmann, P.; Trautwein, A.X.; Kroneck, P.M.H.; Brunold, C.
The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation
J. Biol. Chem.
277
21786-21791
2002
Escherichia coli
brenda
Lillig, C.H.; Prior, A.; Schwenn, J.D.; Aslund, F.; Ritz, D.; Vlamis-Gardikas, A.; Holmgren, A.
New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase
J. Biol. Chem.
274
7695-7698
1999
Escherichia coli
brenda
Lillig, C.H.; Potamitou, A.; Schwenn, J.D.; Vlamis-Gardikas, A.; Holmgren, A.
Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins
J. Biol. Chem.
278
22325-22330
2003
Escherichia coli
brenda
Berndt, C.; Lillig, C.H.; Wollenberg, M.; Bill, E.; Mansilla, M.C.; de Mendoza, D.; Seidler, A.; Schwenn, J.D.
Characterization and reconstitution of a 4Fe-4S adenylyl sulfate/phosphoadenylyl sulfate reductase from Bacillus subtilis
J. Biol. Chem.
279
7850-7855
2004
Bacillus subtilis
brenda
Mansouri-Bauly, H.; Kruse, J.; Sykorova, Z.; Scheerer, U.; Kopriva, S.
Sulfur uptake in the ectomycorrhizal fungus Laccaria bicolor S238N
Mycorrhiza
16
421-427
2006
Laccaria bicolor, Laccaria bicolor S238N
brenda
Chartron, J.; Shiau, C.; Stout, C.D.; Carroll, K.S.
3-Phosphoadenosine-5-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle
Biochemistry
46
3942-3951
2007
Escherichia coli, Escherichia coli (P17854)
brenda
Chung, J.S.; Noguera-Mazon, V.; Lancelin, J.M.; Kim, S.K.; Hirasawa, M.; Hologne, M.; Leustek, T.; Knaff, D.B.
Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase
J. Biol. Chem.
284
31181-31189
2009
Pseudomonas aeruginosa
brenda
Bhave, D.P.; Hong, J.A.; Lee, M.; Jang, W.; Krebs, C.; Carroll, K.S.
Spectroscopic studies on the [4Fe-4S] cluster in adenosine 5-phosphosulfate reductase from Mycobacterium tuberculosis
J. Biol. Chem.
286
1216-1226
2011
Mycobacterium tuberculosis
brenda
Berndt, C.; Schwenn, J.; Lillig, C.
The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity
Chem. Sci.
6
7049-7058
2015
Escherichia coli
-
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.8.4.8)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
