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Information on EC 1.8.4.10 - adenylyl-sulfate reductase (thioredoxin) and Organism(s) Pseudomonas aeruginosa and UniProt Accession O05927

for references in articles please use BRENDA:EC1.8.4.10
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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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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: O05927
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
Synonyms
5'-adenylylsulfate reductase, adenosine-5'-phosphosulfate reductase, adenylylsulfate reductase, APR, APR-B, APS reductase, PaAPR, PpAPR-B, thioredoxin dependent 5'-adenylylsulfate reductase, thioredoxin-dependent APS reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-adenylylsulfate reductase
354
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thioredoxin dependent 5'-adenylylsulfate reductase
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-
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thioredoxin-dependent APS reductase
354
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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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SUBSTRATE
PRODUCT                       
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
5'-adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
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-
-
-
?
adenylyl sulfate + thioredoxin
AMP + sulfite + thioredoxin disulfide
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe-S cluster
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[4Fe-4S] cluster
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-AMP
competitive vs. adenosine-5'-phosphosulfate
adenosine-5'-phosphosulfate
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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
0.00175
adenosine-5'-phosphosulfate
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0.0196
thioredoxin
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0.0114
5'-adenylyl sulfate
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0.01 - 0.054
thioredoxin
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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a heterologous system is constructed in which the C domain of EiAPR (EC 1.8.4.9) is fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (EC 1.8.4.10), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR, can use both thioredoxin and glutathione as an electron donor for APS reduction. The ability to use glutathione is enhanced by the addition of Na2SO4 to the reaction buffer, a property that the hybrid enzyme shares with EiAPR
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
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the enzyme is unstable at 30°C in 20 mM phosphate buffer (pH 5.7)
698950
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is unstable at 30°C in 20 mM phosphate buffer (pH 5.7)
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in transgenic Zea mays
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bick, J.A.; Dennis, J.J.; Zylstra, G.J.; Nowack, J.; Leustek, T.
Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria
J. Bacteriol.
182
135-142
2000
Burkholderia cepacia (Q9RFS6), Burkholderia cepacia DBO1 / ATCC 29424 (Q9RFS6), Mycobacterium sp., Pseudomonas aeruginosa (O05927), Pseudomonas putida, Ralstonia pickettii, Rhizobium tropici
Manually annotated by BRENDA team
Kim, S.K.; Gomes, V.; Gao, Y.; Chandramouli, K.; Johnson, M.K.; Knaff, D.B.; Leustek, T.
The two-domain structure of 5-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity
Biochemistry
46
591-601
2007
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Kim, S.; Rahman, A.; Mason, J.T.; Hirasawa, M.; Conover, R.C.; Johnson, M.K.; Miginiac-Maslow, M.; Keryer, E.; Knaff, D.B.; Leustek, T.
The interaction of 5-adenylylsulfate reductase from Pseudomonas aeruginosa with its substrates
Biochim. Biophys. Acta
1710
103-112
2005
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Martin, M.N.; Tarczynski, M.C.; Shen, B.; Leustek, T.
The role of 5-adenylylsulfate reductase in controlling sulfate reduction in plants
Photosyn. Res.
86
309-323
2005
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Chung, J.S.; Noguera-Mazon, V.; Lancelin, J.M.; Kim, S.K.; Hirasawa, M.; Hologne, M.; Leustek, T.; Knaff, D.B.
Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase
J. Biol. Chem.
284
31181-31189
2009
Pseudomonas aeruginosa
Manually annotated by BRENDA team
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