BRENDA - Enzyme Database
show all sequences of 1.8.4.10

The two-domain structure of 5-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity

Kim, S.K.; Gomes, V.; Gao, Y.; Chandramouli, K.; Johnson, M.K.; Knaff, D.B.; Leustek, T.; Biochemistry 46, 591-601 (2007)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
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
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0114
-
5'-adenylyl sulfate
-
Pseudomonas aeruginosa
0.054
-
thioredoxin
-
Pseudomonas aeruginosa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe-S cluster
[4Fe-4S] cluster
Pseudomonas aeruginosa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5'-adenylyl sulfate + thioredoxin
-
667746
Pseudomonas aeruginosa
AMP + sulfite + thioredoxin disulfide
-
-
-
?
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
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
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0114
-
5'-adenylyl sulfate
-
Pseudomonas aeruginosa
0.054
-
thioredoxin
-
Pseudomonas aeruginosa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe-S cluster
[4Fe-4S] cluster
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5'-adenylyl sulfate + thioredoxin
-
667746
Pseudomonas aeruginosa
AMP + sulfite + thioredoxin disulfide
-
-
-
?
Other publictions for EC 1.8.4.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743374
Paritala
Design, synthesis and evaluat ...
Mycobacterium tuberculosis
Nucleosides Nucleotides Nucleic Acids
34
199-220
2015
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741591
Paritala
A continuous spectrophotometr ...
Mycobacterium tuberculosis
Anal. Biochem.
440
32-39
2013
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742508
Stevenson
The X-ray crystal structure o ...
Physcomitrella patens
FEBS Lett.
587
3626-3632
2013
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698950
Chung
Interaction domain on thioredo ...
Pseudomonas aeruginosa
J. Biol. Chem.
284
31181-31189
2009
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699470
Hong
Identification of critical lig ...
Mycobacterium tuberculosis
J. Med. Chem.
52
5485-5495
2009
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667746
Kim
The two-domain structure of 5- ...
Pseudomonas aeruginosa
Biochemistry
46
591-601
2007
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4
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669057
Gao
Noncovalent Complexes of APS R ...
Mycobacterium tuberculosis
J. Am. Soc. Mass Spectrom.
18
167-178
2007
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687585
Kopriva
The putative moss 3'-phosphoad ...
Physcomitrella patens
J. Biol. Chem.
282
22930-22938
2007
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5
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694695
Wiedemann
The role of the novel adenosin ...
Physcomitrella patens
Plant Mol. Biol.
65
667-676
2007
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1
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1
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1
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667787
Kim
The interaction of 5-adenylyls ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
1710
103-112
2005
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5
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1
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667852
Lopez-Cortes
-
Purification and preliminary c ...
Desulfovibrio aminophilus
Bioinorg. Chem. Appl.
3
81-91
2005
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670496
Martin
The role of 5-adenylylsulfate ...
Pseudomonas aeruginosa
Photosyn. Res.
86
309-323
2005
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1
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636506
Williams
5'-Adenosinephosphosulfate lie ...
Bacillus subtilis, Mycobacterium tuberculosis, Mycolicibacterium smegmatis
J. Biol. Chem.
277
32606-32615
2002
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2
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4
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393947
Bick
Identification of a new class ...
Burkholderia cepacia, Burkholderia cepacia DBO1 / ATCC 29424, Mycobacterium sp., Pseudomonas aeruginosa, Pseudomonas putida, Ralstonia pickettii, Rhizobium tropici
J. Bacteriol.
182
135-142
2000
1
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1
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2
2
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8
-
7
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15
-
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1
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6
1
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1
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1
6
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2
1
2
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8
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15
-
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1
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636505
Neumann
Characterization of the cys ge ...
Allochromatium vinosum
Mol. Biol. Rep.
27
27-33
2000
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288642
Prior
Structural and kinetic propert ...
Catharanthus roseus, Pisum sativum
Biochim. Biophys. Acta
1430
25-38
1999
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1
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4
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1
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1
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1
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1
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2
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636502
Abola
Reduction of adenosine-5'-phos ...
Agrobacterium tumefaciens, Rhizobium leguminosarum, Rhizobium sp., Rhizobium sp. NGR234, Sinorhizobium fredii, Sinorhizobium meliloti
J. Bacteriol.
181
5280-5287
1999
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1
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2
1
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12
-
7
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1
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18
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5
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1
5
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2
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1
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12
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1
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18
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