Information on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin)

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

EC NUMBER
COMMENTARY hide
1.8.4.10
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RECOMMENDED NAME
GeneOntology No.
adenylyl-sulfate reductase (thioredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction III (assimilatory)
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
9027-75-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Chromatium vinosum
SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Burkholderia cepacia DBO1 / ATCC 29424
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UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
DSM 12254
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
also known as Sinorhizobium fredii
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Manually annotated by BRENDA team
also known as Sinorhizobium meliloti
SwissProt
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'-phosphoadenosine-5'-phosphosulfate + thioredoxin
? + thioredoxin disulfide
show the reaction diagram
substrate of phosphoadenylyl-sulfate reductase, EC 1.8.4.8
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-
?
5'-adenylyl sulfate + glutathione
AMP + sulfite + glutathione disulfide
show the reaction diagram
enzyme contains a C-terminal thioredoxin-like PDI domain, physiological electron acceptor unknown
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?
5'-adenylyl sulfate + reduced dithiothreitol
AMP + sulfite + oxidized dithiothreitol
show the reaction diagram
enzyme contains a C-terminal thioredoxin-like PDI domain, physiological electron acceptor unknown
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?
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
adenosine 5'-phosphosulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
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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
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-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
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
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
additional information
?
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
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iron-sulfur protein
thioredoxin
[4Fe-4S]-center
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
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activates
Fe-S center
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in the native state, two clusters of the enzyme are in the [4Fe-4S]2+ oxidized state
Fe-S cluster
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[4Fe-4S] cluster
Iron
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4Fe-4S containing protein. Oxidation state of +2 for the 4Fe-4S cluster, with no disulfide bond in the holoenzyme
KNO3
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activates
sulfate
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activates
additional information
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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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-[(2-sulfanylethyl)amino]-9H-purin-9-yl]oxolan-2-yl]ethyl phosphate
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best inhibitor analyzed. The S atom is capable of establishing favorable interactions with the Fe-S cluster
5'-AMP
adenosine-5'-phosphosulfate
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additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
not activated by sodium sulfate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
1,4-dimercaptobutane-2,3-diol
recombinant enzyme lacking transit peptide
0.04 - 0.049
3'-phosphoadenosine-5'-phosphosulfate
0.0058 - 0.0243
5'-adenylyl sulfate
0.00175 - 0.004
adenosine-5'-phosphosulfate
3
glutathione
recombinant enzyme lacking transit peptide
0.01 - 0.054
thioredoxin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001 - 0.0002
3'-phosphoadenosine-5'-phosphosulfate
0.015 - 0.333
5'-adenylyl sulfate
2.1 - 3.4
adenosine-5'-phosphosulfate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 0.0037
3'-phosphoadenosine-5'-phosphosulfate
0.53 - 48.3
5'-adenylyl sulfate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
adenosine-5'-phosphosulfate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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PpAPR-B activity in terms of APS reduction increases gradually and less markedly with increasing pH compared to PpAPR, EC 1.8.4.9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
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1 * 75000 + 1 * 18000, denaturing SDS-PAGE
29142
x * 29142, deduced from nucleotide sequence
51394
x * 51394, preprotein, deduced from nucleotide sequence
64000
gel filtration
71000
dynamic light scattering
75000
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1 * 75000 + 1 * 18000, denaturing SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
virtual ligand docking simulations with inhibitors. For 2-[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-[(2-sulfanylethyl)amino]-9H-purin-9-yl]oxolan-2-yl]ethyl phosphate, the AMP scaffold binds within the substrate-binding pocket and establishes interactions with key active site residues
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crystal structure is consistent with a preference for adenosine 5'-phosphosulfate. The [Fe4-S4] cluster enhances the enzyme's activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
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the enzyme is unstable at 30C in 20 mM phosphate buffer (pH 5.7)
698950
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is unstable at 30C in 20 mM phosphate buffer (pH 5.7)
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 day, PpAPR-B retains 30% of its activity
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4C, PpAPR-B, completely stable for 5 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FFQ column chromatography
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recombinant His-tagged enzyme, metal affinity resin
recombinant His-tagged enzyme, Ni-nitrilotriacetic acid column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APR-B, DNA and amino acid sequence determination and analysis, semiquantitative expression analysis, overexpression of His-tagged APR-B isozyme in Escherichia coli
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epression of His-tagged enzyme in Escherichia coli
expression in Escherichia coli
expression in transgenic Zea mays
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expression of wild-type and mutant enzymes lacking transit sequence or transit sequence and C-terminal domain in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D122G
mutant does not display improved activity with 3'-phosphoadenosine-5'-phosphosulfate and shows significantly reduced activity with 5'-adenylylsulfate as the substrate
C139S
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no activity
C140S
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mutant enzyme shows 3% of wild-type activity
C228S
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no activity
C231S
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no activity
C256S
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no activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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development of a continuous spectrophotometric method for measuring APR activity by using sulfite-selective colorimetric or off-on fluorescent levulinate-based probes. The APR activity can be followed by monitoring the increase in absorbance or fluorescence of the resulting phenolate product
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