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Information on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)
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EC Tree
1.8.4.10 adenylyl-sulfate reductase (thioredoxin)IUBMB Comments
Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin). Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate reductase).
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Word Map
- 1.8.4.10
- aeruginosa
- sulfur
- thioredoxins
- reductases
- gamma-glutamylcysteine
-
physcomitrella
-
moss
- thiosulfate
-
assimilatory
- patens
-
two-electron
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
paapr, apr-b, thioredoxin-dependent aps reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
APR
APS reductase
thioredoxin dependent 5'-adenylylsulfate reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin
-
-
-
-
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin
the reaction catalyzed by APR can be divided into three steps. In the first step, APS binds to the protein, and a reductive transfer results in sulfite bound to the active-site cysteine in a stable reaction intermediate. In the second step, free sulfite is released by the action of free thioredoxin. In the third step, the thioredoxin is regenerated by reduction with thioredoxin reductase
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming)
Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin). Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate reductase).
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CAS REGISTRY NUMBER
COMMENTARY
9027-75-2
-
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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'-phosphoadenosine-5'-phosphosulfate + thioredoxin
? + thioredoxin disulfide
substrate of phosphoadenylyl-sulfate reductase, EC 1.8.4.8
-
-
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
enzyme contains a C-terminal thioredoxin-like PDI domain, physiological electron acceptor unknown
-
?
5'-adenylyl sulfate + reduced dithiothreitol
AMP + sulfite + oxidized dithiothreitol
enzyme contains a C-terminal thioredoxin-like PDI domain, physiological electron acceptor unknown
-
?
adenosine 5'-phosphosulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
noncovalent complexes of the holoprotein with several ligands, including adenosine 5'-phosphosulfate, thioredoxin, and AMP, are investigated. AMP binds with a higher affinity to the enzyme intermediate than to the free enzyme
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
Burkholderia cepacia DBO1 / ATCC 29424
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
Burkholderia cepacia DBO1 / ATCC 29424
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
-
ir
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
P71752
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
P71752
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
involved in assimilatory sulfate reduction
-
-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
-
-
-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
in Physcomitrella patens, APS reduction is not the major control step of sulfate assimilation
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-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
sulfate assimilation pathway in Physcomitrella patens, overview
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-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
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dependent on thioredoxin, APS is the preferred substrate, substrate binding structure, modelling, overview
-
-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
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-
-
-
?
additional information
?
-
-
importance of specific substituent groups for substrate binding
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-
?
additional information
?
-
-
the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes
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-
?
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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
additional information
?
-
-
the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
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no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
Burkholderia cepacia DBO1 / ATCC 29424
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
P71752
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
involved in assimilatory sulfate reduction
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
no activity with 3'-phosphoadenosine-5'-phosphosulfate, i.e. PAPS
-
-
?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
involved in assimilatory sulfate reduction
-
-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
in Physcomitrella patens, APS reduction is not the major control step of sulfate assimilation
-
-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
-
sulfate assimilation pathway in Physcomitrella patens, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioredoxin
5fold lower activity with dithiothreithol, 70fold lower activity with E. coli Grx1 or dithionite, 580fold lower activity with lipoic acid, no activity with ferredoxin
thioredoxin
activity drops approx. 5fold in the absence of thioredoxin, glutathione can not replace thioredoxin
additional information
-
PpAPR-B does not contain the FeS cluster, which is believed to determine the substrate specificity of other APR enzymes from seed plants
-
additional information
-
PpAPR-B does not contain the FeS cluster, which is believed to determine the substrate specificity of other APR enzymes from seed plants. The lack of the FeS cluster in PpAPR-B catalysis is connected with a lower turnover rate but higher stability of the protein. No activity with glutathione or DTT
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe-S center
-
in the native state, two clusters of the enzyme are in the [4Fe-4S]2+ oxidized state
Iron
-
4Fe-4S containing protein. Oxidation state of +2 for the 4Fe-4S cluster, with no disulfide bond in the holoenzyme
Mg2+
additional information
-
PpAPR-B does not contain the FeS cluster, which is believed to determine the substrate specificity of other APR enzymes from seed plants. The lack of the FeS cluster in PpAPR-B catalysis is connected with a lower turnover rate but higher stability of the protein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-[(2-sulfanylethyl)amino]-9H-purin-9-yl]oxolan-2-yl]ethyl phosphate
-
best inhibitor analyzed. The S atom is capable of establishing favorable interactions with the Fe-S cluster
additional information
-
development of a roadmap for rational design of small molecules as potential inhibitors of APS reductase
-
additional information
-
analysis of inhibitors and molecular docking shows a clearly defined spacing requirement between the Fe-S targeting group and adenosine scaffold. Smaller Fe-S targeting groups are better tolerated. The S atom of the most potent inhibitor may establish a favorable interaction with an S atom in the cluster
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
reduced dithiothreitol
recombinant enzyme lacking transit peptide
-
0.04
3'-phosphoadenosine-5'-phosphosulfate
mutant D122G, pH not specified in the publication, temperature not specified in the publication
0.049
3'-phosphoadenosine-5'-phosphosulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0058
5'-adenylyl sulfate
mutant D122G, pH not specified in the publication, temperature not specified in the publication
0.0069
5'-adenylyl sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0109
5'-adenylyl sulfate
-
levulinate/rhodol-based assay, pH 7.5, 22°C
0.015
5'-adenylyl sulfate
-
levulinate/-hydroxy-4-methyl-2H-chromen-2-one-based assay, pH 7.5, 22°C
0.0025
adenosine-5'-phosphosulfate
recombinant enzyme lacking transit peptide, artificial reductand glutathione
0.0038
adenosine-5'-phosphosulfate
recombinant enzyme lacking transit peptide, artificial reductand dithiothreitol
0.01
thioredoxin
-
wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
3'-phosphoadenosine-5'-phosphosulfate
mutant D122G, pH not specified in the publication, temperature not specified in the publication
0.0002
3'-phosphoadenosine-5'-phosphosulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.015
5'-adenylyl sulfate
mutant D122G, pH not specified in the publication, temperature not specified in the publication
0.058
5'-adenylyl sulfate
-
levulinate/rhodol-based assay, pH 7.5, 22°C
0.08
5'-adenylyl sulfate
-
levulinate/-hydroxy-4-methyl-2H-chromen-2-one-based assay, pH 7.5, 22°C
0.333
5'-adenylyl sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
2.1
adenosine-5'-phosphosulfate
recombinant enzyme lacking transit peptide, artificial reductant glutathione
3.4
adenosine-5'-phosphosulfate
recombinant enzyme lacking transit peptide, artificial reductant dithiothreitol
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0034
3'-phosphoadenosine-5'-phosphosulfate
mutant D122G, pH not specified in the publication, temperature not specified in the publication
0.0037
3'-phosphoadenosine-5'-phosphosulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.53
5'-adenylyl sulfate
-
levulinate/-hydroxy-4-methyl-2H-chromen-2-one-based assay, pH 7.5, 22°C
0.53
5'-adenylyl sulfate
-
levulinate/rhodol-based assay, pH 7.5, 22°C
2.6
5'-adenylyl sulfate
mutant D122G, pH not specified in the publication, temperature not specified in the publication
48.3
5'-adenylyl sulfate
wild-type, pH not specified in the publication, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
PpAPR-B activity in terms of APS reduction increases gradually and less markedly with increasing pH compared to PpAPR, EC 1.8.4.9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT