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Information on EC 1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin)
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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
-
assimilatory
-
sulfate-reducing
- o-acetylserine
-
sulfonucleotide
-
sulfur-oxidizing
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
aps reductase, paps reductase, adenosine 5'-phosphosulfate reductase, 5'-adenylylsulfate reductase, paps sulfotransferase, 3'-phosphoadenosine 5'-phosphosulfate reductase, adenosine 3'-phosphate 5'-phosphosulfate reductase, adenylyl phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, padops reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-Phosphoadenosine 5'-phosphosulfate reductase
3'-Phosphoadenylylsulfate reductase
Adenosine 3'-phosphate 5'-phosphosulfate reductase
-
-
-
-
Adenylyl phosphosulfate reductase
-
-
-
-
APR
APS reductase
EC 1.8.99.4
-
-
formerly
-
PAdoPS reductase
-
-
-
-
PAPS reductase
PAPS reductase, thioredoxin dependent
-
-
-
-
PAPS reductase, thioredoxin-dependent
-
-
-
-
PAPS sulfotransferase
-
-
-
-
Phospho-adenylylsulfate (PAPS) reductase
-
-
-
-
Phospho-adenylylsulfate reductase
-
-
-
-
Reductase, 3'-phosphoadenosine 5'-phosphosulfate
-
-
-
-
Thioredoxin: 3'-phospho-adenylylsulfate reductase
-
-
-
-
Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase
-
-
-
-
3'-Phosphoadenosine 5'-phosphosulfate reductase
-
-
-
-
3'-Phosphoadenylylsulfate reductase
-
-
-
-
PAPS reductase
-
-
-
-
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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
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
from the kinetic data it is concluded that the enzyme follows an ordered mechanism with thioredoxin as the first substrate followed by 5-phosphoadenosine 3-phosphosulfate as the second
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
ping pong type reaction mechanism, Cys239 is the active site residue
-
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
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.
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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'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
3'-phosphoadenylyl sulfate + glutaredoxin 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
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
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide
3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
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
-
human thioredoxin, 59% of the activity with thioredoxin Trx1
-
-
?
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
-
Arabidopsis thaliana thioredoxin, 18% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH2
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH2 disulfide
-
Arabidopsis thaliana thioredoxin, 23% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH3
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH3 disulfide
-
Arabidopsis thaliana thioredoxin, 154% of the activity with thioredoxin Trx1
-
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH4
adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH4 disulfide
-
Arabidopsis thaliana thioredoxin, 45% of the activity with thioredoxin Trx1
-
-
?
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
adenosine 5'-phosphosulfate + thioredoxin
AMP + sulfite + oxidized thioredoxin
-
-
-
-
?
adenosine 5'-phosphosulfate + thioredoxin I
AMP + sulfite + oxidized thioredoxin I
-
-
-
-
?
3'-phosphoadenylyl sulfate + glutaredoxin 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
-
-
-
-
r
3'-phosphoadenylyl sulfate + glutaredoxin 1
adenosine 3',5'-bisphosphate + sulfite + glutaredoxin 1 disulfide
-
-
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide
-
thioredoxin from Escherichia coli
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin
adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide
-
thioredoxin from Saccharomyces cerevisiae
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
-
-
-
-
r
3'-phosphoadenylyl sulfate + thioredoxin 1
adenosine 3',5'-bisphosphate + sulfite + thioredoxin 1 disulfide
-
-
-
-
r
3'-phosphoadenylyl-sulfate + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
-
?
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
-
-
?
3'-phosphoadenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
thioredoxin m from spinach
-
-
?
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
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
?
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
?
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
?
-
-
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
thioredoxin I mutant W31A shows no detectable activity, whereas W31F, K36E, and D61N are able to serve as electron donors for the APR-catalyzed reaction but with lower turnover numbers than that exhibited by the wild type thioredoxin I. The Km for thioredoxin mutant R73E is increased by 7.7fold compared with wild type thioredoxin I
-
-
?
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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'-adenylyl-sulfate + thioredoxin
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
-
-
-
?
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 + glutaredoxin
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
-
-
-
?
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
?
-
-
thioredoxin1 and glutaredoxin 1 are essential for sulfate reduction but not for ribonucleotide reduction
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
-
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
-
iron-sulfur protein, each mole of protein contains 3.3 mol of Fe
Iron
-
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 3',5'-bisphosphate
-
competitive with respect to 5-phosphoadenosine 3-phosphosulfate
oxidized glutathione
-
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutaredoxin
-
required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo
additional information
-
The activity of 3'-phosphoadenosine 5'-phosphosulfate reductase is increased by sulfur starvation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Deciphering the Role of Histidine 252 in Mycobacterial Adenosine 5'-Phosphosulfate (APS) Reductase Catalysis.
Infections
Design, synthesis and evaluation of fe-s targeted adenosine 5'-phosphosulfate reductase inhibitors.
Infections
Structure-based virtual screening and biological evaluation of Mycobacterium tuberculosis adenosine 5'-phosphosulfate reductase inhibitors.
Latent Infection
Spectroscopic studies on the [4Fe-4S] cluster in adenosine 5'-phosphosulfate reductase from Mycobacterium tuberculosis.
Latent Tuberculosis
Design, synthesis and evaluation of fe-s targeted adenosine 5'-phosphosulfate reductase inhibitors.
Latent Tuberculosis
Structure-based virtual screening and biological evaluation of Mycobacterium tuberculosis adenosine 5'-phosphosulfate reductase inhibitors.
phosphoadenylyl-sulfate reductase (thioredoxin) deficiency
Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum.
Starvation
Regulation of sulfur assimilation in higher plants: a sulfate transporter induced in sulfate-starved roots plays a central role in Arabidopsis thaliana.
Starvation
The role of 5'-adenylylsulfate reductase in the sulfur assimilation pathway of soybean: molecular cloning, kinetic characterization, and gene expression.
Tuberculosis
Crystal Structure of the [4Fe-4S] Cluster-Containing Adenosine-5'-phosphosulfate Reductase from Mycobacterium tuberculosis.
Tuberculosis
Deciphering the Role of Histidine 252 in Mycobacterial Adenosine 5'-Phosphosulfate (APS) Reductase Catalysis.
Tuberculosis
Design, synthesis and evaluation of fe-s targeted adenosine 5'-phosphosulfate reductase inhibitors.
Tuberculosis
Identification of critical ligand binding determinants in Mycobacterium tuberculosis adenosine-5'-phosphosulfate reductase.
Tuberculosis
Investigation of the iron-sulfur cluster in Mycobacterium tuberculosis APS reductase: implications for substrate binding and catalysis.
Tuberculosis
Noncovalent complexes of APS reductase from M. tuberculosis: delineating a mechanistic model using ESI-FTICR MS.
Tuberculosis
Spectroscopic studies on the [4Fe-4S] cluster in adenosine 5'-phosphosulfate reductase from Mycobacterium tuberculosis.
Tuberculosis
Structure-based virtual screening and biological evaluation of Mycobacterium tuberculosis adenosine 5'-phosphosulfate reductase inhibitors.
Tuberculosis
Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0637
glutaredoxin Grx
-
pH 8.0, temperature not specified in the publication
-
0.0149
glutaredoxin Grx1
-
pH 8.0, temperature not specified in the publication
-
0.0681
thioredoxin hTrx1
-
pH 8.0, temperature not specified in the publication
-
0.01
thioredoxin I
-
wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4
0.0137
thioredoxin Trx1
-
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
-
0.0431
thioredoxin TrxH2
-
pH 8.0, temperature not specified in the publication
-
0.0178
thioredoxin TrxH3
-
pH 8.0, temperature not specified in the publication
-
0.0261
thioredoxin TrxH4
-
pH 8.0, temperature not specified in the publication
-
0.0287
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.1054
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.0064
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.0107
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.0225
3'-phosphoadenylyl-sulfate
-
with cofactors Trx1, Trx2, or Grx1, pH 8.0
0.019
5-Phosphoadenosine 3-phosphosulfate
-
with thioredoxin from Saccharomyces cerevisiae as cosubstrate
0.021
5-Phosphoadenosine 3-phosphosulfate
-
with thioredoxin from E. coli as cosubstrate
0.0225
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
-
0.0606
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
-
0.0543
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
0.0675
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.149
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.335
3'-phosphoadenylyl sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.172
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with thioredoxin 1
0.382
3'-phosphoadenylyl-sulfate
-
recombinant enzyme, pH 8.0, with glutaredoxin 1
0.146
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
-
0.421
glutaredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
-
0.174
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-adenylyl-sulfate
0.219
thioredoxin 1
-
recombinant enzyme, pH 8.0, with substrate 3'-phosphoadenylyl-sulfate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
adenosine 5'-phosphosulfate
-
mutant enzyme K144A, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5
2500
adenosine 5'-phosphosulfate
-
wild type enzyme, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (4752 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
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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
-
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K144A |
-
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
-
a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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