Information on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.8.4.8
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RECOMMENDED NAME
GeneOntology No.
phosphoadenylyl-sulfate reductase (thioredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction I (assimilatory)
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sulfate reduction
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Sulfur metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-63-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cysH, bispecific enzyme
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Manually annotated by BRENDA team
K12
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Manually annotated by BRENDA team
strain S238N
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Manually annotated by BRENDA team
strain S238N
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Manually annotated by BRENDA team
PCC7942
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Manually annotated by BRENDA team
PCC7942
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
show the reaction diagram
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-
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
show the reaction diagram
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
show the reaction diagram
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
show the reaction diagram
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
show the reaction diagram
adenosine 5'-phosphosulfate + thioredoxin
AMP + sulfite + oxidized thioredoxin
show the reaction diagram
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-
-
-
?
adenosine 5'-phosphosulfate + thioredoxin I
AMP + sulfite + oxidized thioredoxin I
show the reaction diagram
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-
-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
show the reaction diagram
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
show the reaction diagram
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
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the enzyme harbors a [4Fe-4S]2+ cluster
glutaredoxin
thioredoxin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
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iron-sulfur protein, each mole of protein contains 3.3 mol of Fe
Iron
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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
additional information
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enzyme contains no iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 3',5'-bisphosphate
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competitive with respect to 5-phosphoadenosine 3-phosphosulfate
glutathione
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0.002 to 0.6 mM
N-(Iodoacetyl-aminoethyl)-5-N'-naphthylamin-1-sulfonic acid
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N-bromosuccinimide
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oxidized glutathione
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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
p-chloromercuribenzoate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutaredoxin
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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 hide
LITERATURE
IMAGE
0.0287 - 0.1054
3'-phosphoadenylyl sulfate
0.0064 - 0.0225
3'-phosphoadenylyl-sulfate
0.01 - 0.021
5-Phosphoadenosine 3-phosphosulfate
0.0149 - 0.0606
glutaredoxin 1
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0.0072
glutaredoxin mutant 1C14S
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pH 8.0
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0.023
reduced thioredoxin
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0.0137 - 0.0675
thioredoxin 1
0.0342
thioredoxin 2
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pH 8.0
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0.0014
thioredoxin from Escherichia coli
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0.0006
thioredoxin from Saccharomyces cerevisiae
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0.01
thioredoxin I
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wild type enzyme, at 20C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
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additional information
additional information
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kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.149 - 0.335
3'-phosphoadenylyl sulfate
0.172 - 3.5
3'-phosphoadenylyl-sulfate
0.146 - 0.421
glutaredoxin 1
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0.174 - 0.219
thioredoxin 1
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 2500
adenosine 5'-phosphosulfate
425
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.2 - 9.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Oryza sativa subsp. japonica
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is lost upon exposure to air or upon dilution
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is lost upon exposure to air
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659441
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating column chromatography and Superdex 200 gel filtration
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recombinant enzyme from strain BL21(DE3)
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recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
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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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expressed in Escherichia coli BL21(DE3) cells
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expression in strain BL21(DE3) as His10-tagged protein
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gene cysH, expression in Escherichia coli strain BL21(DE3)
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overexpression in strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C239S
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mutant enzymes Cys239Ser and Tyr209Phe are inactive
Q160L
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mutant enzyme Gln160Leu is as active as the wild-type enzyme
Y209F
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mutant enzymes Cys239Ser and Tyr209Phe are inactive
K144A |
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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in Mycobacterium tuberculosis, APR is a validated target against the latent phase of infection
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