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Enzyme Nomenclature
Information on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin)
for references in articles please use BRENDA:EC1.8.4.8
Word Map on EC 1.8.4.8
- 1.8.4.8
-
sulfurylase
-
assimilatory
-
sulfate-reducing
- glutaredoxins
-
sulfonucleotide
- o-acetylserine
-
sulfur-oxidizing
- cysc
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.4.8
-
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RECOMMENDED NAME
GeneOntology No.
phosphoadenylyl-sulfate reductase (thioredoxin)
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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
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism, Cys239 is the active site residue
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adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9068-63-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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
-
-
-
-
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5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
-
additional information
?
-
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enzyme is essential for sulfate assimilation using phosphoadenosine 5'-phosphosulfate, not adenosine 5'-phosphosulfate, phylogenetic comparison of the 2 different groups, overview
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-
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additional information
?
-
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enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview
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-
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additional information
?
-
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thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
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-
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additional information
?
-
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
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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
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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
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INHIBITORS
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
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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
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The activity of 3'-phosphoadenosine 5'-phosphosulfate reductase is increased by sulfur starvation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
thioredoxin I
-
wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
-
0.0287
3'-phosphoadenylyl sulfate
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recombinant enzyme, pH 8.0, with thioredoxin 1
0.1054
3'-phosphoadenylyl sulfate
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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
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recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
-
0.0606
glutaredoxin 1
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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
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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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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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
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in strain BL21(DE3) as His-tagged protein
-
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ENGINEERING
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
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a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
in Mycobacterium tuberculosis, APR is a validated target against the latent phase of infection
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