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Information on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin) and Organism(s) Escherichia coli and UniProt Accession P17854
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1.8.4.8 phosphoadenylyl-sulfate reductase (thioredoxin)IUBMB Comments
Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.
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Word Map
- 1.8.4.8
-
sulfurylase
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assimilatory
-
sulfate-reducing
- o-acetylserine
-
sulfonucleotide
-
sulfur-oxidizing
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aps reductase, paps reductase, adenosine 5'-phosphosulfate reductase, adenosine 3'-phosphate 5'-phosphosulfate reductase, 5'-adenylylsulfate reductase, paps sulfotransferase, 3'-phosphoadenosine 5'-phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, adenylyl phosphosulfate reductase, cysh1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-Phosphoadenosine 5'-phosphosulfate reductase
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-
-
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3'-Phosphoadenylylsulfate reductase
Adenosine 3'-phosphate 5'-phosphosulfate reductase
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-
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Adenylyl phosphosulfate reductase
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-
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PAdoPS reductase
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-
-
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PAPS reductase
PAPS reductase, thioredoxin dependent
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PAPS reductase, thioredoxin-dependent
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PAPS sulfotransferase
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Phospho-adenylylsulfate (PAPS) reductase
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Phospho-adenylylsulfate reductase
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Reductase, 3'-phosphoadenosine 5'-phosphosulfate
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Thioredoxin: 3'-phospho-adenylylsulfate reductase
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Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase
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3'-Phosphoadenylylsulfate reductase
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PAPS reductase
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-
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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
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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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
9068-63-7
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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'-phosphoadenylyl sulfate + glutaredoxin 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
-
-
-
-
r
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 + glutaredoxin mutant 1C14S
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin mutant 1C14S disulfide
-
-
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
-
-
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin 2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 2 disulfide
-
-
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin hTrx1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin hTrx1 disulfide
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human thioredoxin, 59% of the activity with thioredoxin Trx1
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-
?
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
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Arabidopsis thaliana thioredoxin, 18% of the activity with thioredoxin Trx1
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-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH2 disulfide
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Arabidopsis thaliana thioredoxin, 23% of the activity with thioredoxin Trx1
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-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH3
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH3 disulfide
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Arabidopsis thaliana thioredoxin, 154% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH4
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH4 disulfide
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Arabidopsis thaliana thioredoxin, 45% of the activity with thioredoxin Trx1
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-
?
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
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
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-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
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thioredoxin m from spinach
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-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
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enzyme is involved in sulfur metabolism
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-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
?
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essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
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-
?
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
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-
-
?
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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?
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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?
additional information
?
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thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
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?
additional information
?
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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
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-
?
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'-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
?
-
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thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
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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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 3',5'-bisphosphate
-
competitive with respect to 5-phosphoadenosine 3-phosphosulfate
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
-
required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0225
3'-phosphoadenylyl-sulfate
-
with cofactors Trx1, Trx2, or Grx1, pH 8.0
0.0637
glutaredoxin Grx
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pH 8.0, temperature not specified in the publication
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0.0149
glutaredoxin Grx1
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pH 8.0, temperature not specified in the publication
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0.0681
thioredoxin hTrx1
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pH 8.0, temperature not specified in the publication
-
0.0137
thioredoxin Trx1
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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
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0.0431
thioredoxin TrxH2
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pH 8.0, temperature not specified in the publication
-
0.0178
thioredoxin TrxH3
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pH 8.0, temperature not specified in the publication
-
0.0261
thioredoxin TrxH4
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pH 8.0, temperature not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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 (P17854), Escherichia coli
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
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