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3S + 3H2O
HSO3- + 2HS- + 3H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 sulfite
-
-
-
-
?
S + O2
SO32- + S2O32- + H2S
S + O2 + H2O
HSO3- + H2S + H+
S + OH- + O2
HSO3- + S2O32- + HS- + H+
-
-
-
r
additional information
?
-
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
initial enzyme in the sulfur-oxidation pathway
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
in the presence of oxygen but not under a hydrogen atmosphere, the enzyme simultaneously produces sulfite, thiosulfate, and hydrogen sulfide from sulfur. Nonenzymatic control experiments show that thiosulfate is produced mainly in a chemical reaction between sulfite and sulfur. The ratio of sulfite to hydrogen sulfide production is 5:4 in the presence of zinc ions
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
in the presence of oxygen but not under a hydrogen atmosphere, the enzyme simultaneously produces sulfite, thiosulfate, and hydrogen sulfide from sulfur. Nonenzymatic control experiments show that thiosulfate is produced mainly in a chemical reaction between sulfite and sulfur. The ratio of sulfite to hydrogen sulfide production is 5:4 in the presence of zinc ions
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
initial enzyme in the sulfur-oxidation pathway
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method
-
-
?
S + O2
SO32- + S2O32- + H2S
-
-
-
-
?
S + O2
SO32- + S2O32- + H2S
-
-
-
-
?
S + O2
SO32- + S2O32- + H2S
-
-
-
?
S + O2 + H2O
HSO3- + H2S + H+
-
-
-
-
?
S + O2 + H2O
HSO3- + H2S + H+
-
-
-
-
?
sulfur + H2O + O2
?
initial enzyme in the sulfur oxidation pathway
-
-
?
sulfur + H2O + O2
?
-
-
-
-
?
sulfur + H2O + O2
?
-
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
-
-
?
additional information
?
-
not active with tetrathionate
-
-
?
additional information
?
-
-
not active with tetrathionate
-
-
?
additional information
?
-
not active with tetrathionate
-
-
?
additional information
?
-
SOR catalyzes simultaneously oxidation and reduction of elementar sulfur to produce sulfite, thiosulfate and sulfide, in the presence of molecule oxygen
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
-
at 50°C, nonenzymatic sulfur disproportionation is observed at pH 11 and above. At pH 12, the enzyme activity cannot be distinguished from the background anymore. At 50°C, sulfite exceeds thiosulfate production at all pH value, at 80°C, the main product is thiosulfate with only minor amounts of sulfite (maximum 6%)
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-
?
additional information
?
-
-
at 50°C, nonenzymatic sulfur disproportionation is observed at pH 11 and above. At pH 12, the enzyme activity cannot be distinguished from the background anymore. At 50°C, sulfite exceeds thiosulfate production at all pH value, at 80°C, the main product is thiosulfate with only minor amounts of sulfite (maximum 6%)
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-
?
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0.02
mutant C101S, U/mg, reductase reaction
0.04
-
mutant C104S, formation of sulfite plus thiosulfate, 70°C
0.05
crude enzyme extract, sulfur reductase activity, pH 7.5, 75°C
0.074
-
wild type in cellular lysate, formation of sulfite plus thiosulfate, 70°C
0.08
-
mutant C101S, formation of sulfite plus thiosulfate, 70°C
0.1078
-
wild type in supernatant, formation of sulfite plus thiosulfate, 70°C
0.11
mutant E114D, U/mg, oxygenase reaction
0.12
mutant C101S, U/mg, oxygenase reaction
0.21
-
wild-type enzyme in absence of GSH, pH 8.0, 80°C
0.22
crude enzyme extract, sulfur oxygenase activity, pH 7.5, 75°C
0.23
mutant C104A, U/mg, reductase reaction
0.43
mutant C101A, U/mg, reductase reaction
0.476
-
wild type in pellet, formation of sulfite plus thiosulfate, 70°C
0.5
cytoplasm, pH 7.4, 85°C, sulfur reduction
0.6
mutant C104S, U/mg, reductase reaction
0.64
mutant C101/104A, U/mg, reductase reaction
0.95
-
80°C, pH 6, production of hydrogen sulfite
1.12
mutant C101/104A, U/mg, oxygenase reaction
1.17
mutant C101/104S, U/mg, reductase reaction
1.35
mutant C104A, U/mg, oxygenase reaction
1.47
mutant C101, U/mg, oxygenase reaction
1.75
-
mutant C101S, pH 8.0, 80°C
1.89
cytoplasm, pH 7.4, 85°C, sulfur oxidation
10.5
-
80°C, pH 6, oxygenase reaction
11.52
wild type, U/mg, oxygenase reaction
17.17
-
wild-type enzyme in presence of GSH, pH 8.0, 80°C
186.7
-
formation of sulfite and thiosulfate
2.28
mutant C104S, U/mg, oxygenase reaction
2.29
mutant C101/104S, U/mg, oxygenase reaction
28600
wild type, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
29700
wild type, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
3.28
-
mutant H90A, pH 8.0, 80°C
3.47
-
mutant H86A, pH 8.0, 80°C
308 - 454
-
purified recombinant enzyme, pH 9.0, 80°C, thiosulfate- and sulfite-producing oxygenase activity
3100
wild type, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
3300
wild type, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
4.19
wild type, U/mg, reductase reaction
4.85
-
wild type, formation of sulfite plus thiosulfate, 70°C
45200
Escherichia coli HB101, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
5.46
-
mutant E114A, pH 8.0, 80°C
6300
Escherichia coli HB101, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
75000
Escherichia coli HB101, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
753000
Escherichia coli HB101, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
8.09
-
mutant C104S, pH 8.0, 80°C
0.03
mutant E114D, U/mg, reductase reaction
0.03
-
purified recombinant enzyme, pH 9.0, 80°C, reductase activity
10.6
pH 7.4, 85°C, formation of sulfite
additional information
0% activity with 0.2 mM 2.2'-dipyridyl compared to activity without any treatment
additional information
0.3% activity with 1 mM Fe3+ compared to activity without any treatment
additional information
17.8% activity with 1.0 mM 8-hydroxyquinoline compared to activity without any treatment
additional information
199.4% activity with 10 mM 2.2'-dipyridyl after ultrafiltration compared to activity without any treatment, the SOR activity recovers after removal (washing/untrafiltration) of the excessive iron
additional information
21.1% activity with 0.04 mM 2.2'-dipyridyl compared to activity without any treatment
additional information
239.7% activity with 10 mM 4,5-dihydroxy-meta-benzenedisulfonic acid after ultrafiltration compared to activity without any treatment, the SOR activity recovers after removal (washing and ultrafiltration) of the excessive iron
additional information
31.5% activity with 1 mM Fe2+ compared to activity without any treatment
additional information
44% activity with 0.1 mM 8-hydroxyquinoline compared to activity without any treatment
additional information
52.8% activity with 1.0 mM 4,5-dihydroxy-meta-benzenedisulfonic acid compared to activity without any treatment
additional information
55% activity with 0.1 mM 4,5-dihydroxy-meta-benzenedisulfonic acid compared to activity without any treatment
additional information
-
recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production
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evolution
-
the enzyme belongs to the SOR protein family, phylogenetic analysis, overview
evolution
-
the enzyme belongs to the SOR protein family, phylogenetic analysis, overview
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metabolism
sulfur oxygenase reductase is the initial enzyme of the sulfur oxidation pathway in the thermoacidophilic Archaeon Acidianus ambivalens catalyzing an oxygen-dependent sulfur disproportionation to H2S, sulfite and thiosulfate
metabolism
-
proposed sulfur metabolism pathways of Sulfobacillus acidophilus strain TPY involving the enzyme, overview
metabolism
the enzyme is involved in the sulfur oxidation metabolism of Acidithiobacillus thiooxidans strain A01, sulfur oxidation model, overview
metabolism
-
the enzyme is involved in the sulfur oxidation metabolism of Acidithiobacillus thiooxidans strain A01, sulfur oxidation model, overview
-
metabolism
-
proposed sulfur metabolism pathways of Sulfobacillus acidophilus strain TPY involving the enzyme, overview
-
physiological function
catalyzes the initial step in the dissimilatory sulfur oxidation pathway
physiological function
initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens
physiological function
initial enzyme in the sulfur-oxidation pathway
physiological function
-
the enzyme oxidizes the cytoplasmic elemental sulfur, but cannot couple the sulfur oxidation with the electron transfer chain or substrate-level phosphorylation
physiological function
-
the enzyme is involved in the dissimilatory oxidation of sulfur compounds, schematic overview. Sulfur oxygenase reductases (SORs) catalyze a dioxygen-dependent disproportionation reaction of elemental sulfur (S0, consisting mostly of cyclo-octasulfur) with sulfite, thiosulfate, and sulfide as detectable products
physiological function
-
the enzyme is involved in the dissimilatory oxidation of sulfur compounds, schematic overview. Sulfur oxygenase reductases (SORs) catalyze a dioxygen-dependent disproportionation reaction of elemental sulfur (S0, consisting mostly of cyclo-octasulfur) with sulfite, thiosulfate, and sulfide as detectable products. Recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production
physiological function
-
initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens
-
physiological function
-
the enzyme is involved in the dissimilatory oxidation of sulfur compounds, schematic overview. Sulfur oxygenase reductases (SORs) catalyze a dioxygen-dependent disproportionation reaction of elemental sulfur (S0, consisting mostly of cyclo-octasulfur) with sulfite, thiosulfate, and sulfide as detectable products. Recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production
-
physiological function
-
initial enzyme in the sulfur-oxidation pathway
-
physiological function
-
the enzyme oxidizes the cytoplasmic elemental sulfur, but cannot couple the sulfur oxidation with the electron transfer chain or substrate-level phosphorylation
-
additional information
-
modeling of the sulfur oxidation system in Acidithiobacillus caldus , overview
additional information
the spherical, hollow, cytoplasmic enzyme is composed of 24 identical subunits with an active site pocket each comprising a mononuclear non-heme iron site and a cysteine persulfide. Substrate access and product exit occur via apolar chimney-like protrusions at the fourfold symmetry axes, via narrow polar pores at the threefold symmetry axes and via narrow apolar pores within in each subunit. The expansion of the pores in the outer shell leads to an increased enzyme activity while the integrity of the active site pore seems to be important. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine. Modeling of the SOR and its pores, overview. Opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products
additional information
-
the spherical, hollow, cytoplasmic enzyme is composed of 24 identical subunits with an active site pocket each comprising a mononuclear non-heme iron site and a cysteine persulfide. Substrate access and product exit occur via apolar chimney-like protrusions at the fourfold symmetry axes, via narrow polar pores at the threefold symmetry axes and via narrow apolar pores within in each subunit. The expansion of the pores in the outer shell leads to an increased enzyme activity while the integrity of the active site pore seems to be important. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine. Modeling of the SOR and its pores, overview. Opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products
additional information
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three-dimensional modeling of the enzyme, overview
additional information
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modeling of the sulfur oxidation system in Acidithiobacillus caldus , overview
-
additional information
-
three-dimensional modeling of the enzyme, overview
-
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C101/104A
enzyme with decreased specific activity
C101/104S
enzyme with decreased specific activity
C101A/C104A
iron content is 124% of that of the recombinant wild-type enzyme, oxygenase activity is 9.7% of the activity of recombinant wild-type enzyme, reductase activity is 15.3% of the activity of recombinant wild-type enzyme
C101S/C104S
iron content is 89% of that of the recombinant wild-type enzyme, oxygenase activity is 19.8% of the activity of recombinant wild-type enzyme, reductase activity is 27.9% of the activity of recombinant wild-type enzyme
F133A
site-directed mutagenesis of a tetramer channel residue, the mutant shows reduced activity compared to the wild-type enzyme
F133A/F141A
site-directed mutagenesis of a tetramer channel residue, the mutant shows increased activity compared to the wild-type enzyme
F141A
site-directed mutagenesis of a tetramer channel residue, the mutant shows increased activity compared to the wild-type enzyme
H166A
site-directed mutagenesis of the zinc site residue, the mutant shows reduced activity compared to the wild-type enzyme
H277A
site-directed mutagenesis of the zinc site residue, the mutant shows activity similar to the wild-type enzyme
M296V
site-directed mutagenesis of the active site pore residue, the mutant shows slightly increased activity compared to the wild-type enzyme
M297A
site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme
MM296/297TT
site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme
MM296/297VT
site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme
R99A
site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme
R99I
site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme
S226A
site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme
S226I
site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme
S226L
site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme
S226T
site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme
E129A
site-directed mutagenesis, no change of the secondary structure, but mutant is completely inactive, 0.81 mol iron content per mol subunit
H86F
site-directed mutagenesis, no change of the secondary structure, but mutant is completely inactive, 0 mol iron content per mol subunit
H90F
site-directed mutagenesis, no change of the secondary structure, but mutant is completely inactive, 0.6 mol iron content per mol subunit
His86F
-
mutation results in a dramatic reduction in SOR activity
His90F
-
mutation results in a dramatic reduction in SOR activity
C101S
-
site-directed mutagenesis, 10% reamining activity compared to the wild-type enzyme
C104S
-
site-directed mutagenesis, 47% reamining activity compared to the wild-type enzyme
C31S
-
site-directed mutagenesis, inactive mutant
E114A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H86A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H90A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
C101S
-
site-directed mutagenesis, 10% reamining activity compared to the wild-type enzyme
-
C104S
-
site-directed mutagenesis, 47% reamining activity compared to the wild-type enzyme
-
H86A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
H90A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
C101A
-
about 10% residual activtiy for both oxygenase and reductase activity
C104A
-
about 10% residual activtiy for both oxygenase and reductase activity
C31A
-
complete loss of activity
E114A
-
complete loss of activity
H86A
-
complete loss of activity
H90A
-
complete loss of activity
C113A
-
site-directed mutagenesis, almost inactive mutant
C116A
-
site-directed mutagenesis, almost inactive mutant
C44A
-
site-directed mutagenesis, inactive mutant
C113A
-
site-directed mutagenesis, almost inactive mutant
-
C116A
-
site-directed mutagenesis, almost inactive mutant
-
C44A
-
site-directed mutagenesis, inactive mutant
-
C101A
enzyme with decreased specific activity
C101A
iron content is 49% of that of the recombinant wild-type enzyme, oxygenase activity is 12.8% of the activity of recombinant wild-type enzyme, reductase activity is 10.3% of the activity of recombinant wild-type enzyme
C101S
enzyme with decreased specific activity and a proportional decrease in iron content
C101S
mutant enzyme contains no iron, oxygenase activity is 1.04% of the activity of recombinant wild-type enzyme, reductase activity is 0.5% of the activity of recombinant wild-type enzyme
C104A
enzyme with decreased specific activity
C104A
iron content is 42% of that of the recombinant wild-type enzyme, oxygenase activity is 11.8% of the activity of recombinant wild-type enzyme, reductase activity is 5.5% of the activity of recombinant wild-type enzyme
C104S
enzyme with decreased specific activity
C104S
iron content is 67% of that of the recombinant wild-type enzyme, oxygenase activity is 19.8% of the activity of recombinant wild-type enzyme, reductase activity is 14.3% of the activity of recombinant wild-type enzyme
C31A
inactive enzyme
C31A
inactive mutant enzyme, iron content is similar to that of recombinant wild-type enzyme
C31S
inactive enzyme
C31S
inactive mutant enzyme, iron content is similar to that of recombinant wild-type enzyme
E114A
inactive enzyme with no iron incorporated
E114A
mutation results in inactive enzyme with no measurable iron found
E114D
enzyme with 1% of wild type activity
E114D
iron content is 4.4% of wild-type value, sulfur-oxidizing and sulfur-reducing activity is about 1% of the activity of activity of the recombinant wild-type enzyme
H86A
inactive enzyme with no iron incorporated
H86A
mutation results in inactive enzyme with no measurable iron found
H90A
inactive enzyme with no iron incorporated
H90A
mutation results in inactive enzyme with no measurable iron found
C101S
-
mutant with reduced activity
C101S
-
98.4% loss of activity
C101S
-
mutation of any cysteine residues (C31S, C101S, and C104S) at the active site leads to complete loss of SOR catalytic ability
C101S
1.95 mol iron content per mol subunit, cysteine residue is essential for activity
C104S
-
mutant with reduced activity
C104S
-
99.2% loss of activity
C104S
-
mutation of any cysteine residues (C31S, C101S, and C104S) at the active site leads to complete loss of SOR catalytic ability
C104S
2.4 mol iron content per mol subunit, cysteine residue is essential for activity
C31A
-
complete loss of activity
C31A
-
mutant with reduced activity
C31S
-
complete loss of activity
C31S
-
mutant with reduced activity
C31S
-
mutation of any cysteine residues (C31S, C101S, and C104S) at the active site leads to complete loss of SOR catalytic ability
C31S
1.86 mol iron content per mol subunit, cysteine residue is essential for activity
C101S
-
mutant with reduced activity
-
C101S
-
98.4% loss of activity
-
C104S
-
mutant with reduced activity
-
C104S
-
99.2% loss of activity
-
C31A
-
complete loss of activity
-
C31A
-
site-directed mutagenesis, inactive mutant
additional information
modeling of active site pore mutants based on the wild-type structure, overview
additional information
-
modeling of active site pore mutants based on the wild-type structure, overview
additional information
-
generation of an enzyme mutant lacking the sulfur oxygenase reductase gene sor, comparative transcriptome analysis, microarrays and real-time quantitative PCR, of the wild-type and the DELTAsor mutant, growth analysis on sulfur or K2S4O6 as the sole substrates reveals that the mutant has an obvious growth advantage compared to the wild-type strain and its maximum cell concentration is 70% higher than the wild-type, overview
additional information
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generation of an enzyme mutant lacking the sulfur oxygenase reductase gene sor, comparative transcriptome analysis, microarrays and real-time quantitative PCR, of the wild-type and the DELTAsor mutant, growth analysis on sulfur or K2S4O6 as the sole substrates reveals that the mutant has an obvious growth advantage compared to the wild-type strain and its maximum cell concentration is 70% higher than the wild-type, overview
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additional information
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mutations of putative SOR active site residues, C31, C101, C104, H86 and H90, and E114: replacement of any cysteine residues reduced SORactivity by 53-100%, while the mutants of H86A, H90A and E114A lost their enzyme activities largely, only remaining 20%, 19% and 32% activity of the wild type SOR respectively
additional information
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mutations of putative SOR active site residues, C31, C101, C104, H86 and H90, and E114: replacement of any cysteine residues reduced SORactivity by 53-100%, while the mutants of H86A, H90A and E114A lost their enzyme activities largely, only remaining 20%, 19% and 32% activity of the wild type SOR respectively
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expressed in Escherichia coli HB101
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expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli HB101
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expression in Escherichia coli results in active, soluble SOR and in inclusion bodies from which active SOR can be refolded as long as ferric ions are present in the refolding solution. Wild-type, recombinant and refolded enzyme possesses indistinguishable properties
expression of wild type and mutant enzyme in Escherichia coli
gene AaSOR, phylogenetic analysis, recombinant expression of wild-type and mutant enzymes in Escherichia coli
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gene SAMN00768000_1627, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene SAMN00768000_1798, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene SOR, DNA and amino acid sequence determination and analysis, sequence comparisons, real-time quantitative PCR enzyme exxpression analysis
gene sor, DNA and amino acid sequence determination, comparison, and analysis, phylogenetic tree, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain B21 in inclusion bodies
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gene sor, expression anaysis
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gene sor, sequence comparisons and phylogenetic analysis, expression in Escherichia coli
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gene sor, sequence comparisons, expression in Escherichia coli strain BL21 Codon plus (DE3) RIL
gene TPY_0405, conjugation-based transformation of pTrc99A derived plasmid from heterotrophic Escherichia coli to facultative autotrophic Sulfobacillus acidophilus strain TPY, recombinant overexpression of enzyme SOR in Sulfobacillus acidophilus strain TPY, transconjugation between Escherichia coli and SUlfobacillus acidophilus is performed on modified solid 2:2 medium at pH 4.8 and 37°C for 72h. The transgenic strain shows increased sulfate concentration and accumulation
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overexpressed by Escherichia coli HB 101 opon a temperature shift from 30-42°C
overexpression in Escherichia coli
overexpression of wild-type and mutant enzymes in Escherichia coli
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phylogenetic analysis, synthetic gene encoding TpSOR, recombinant expression of wild-type and mutant enzymes in Escherichia coli
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recombinantly expressed in Escherichia coli
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the sor gene, including codons for a C-terminally fused Strep tag, is cloned under the control of the tf55alpha promoter. Single transformants of Sulfolobus solfataricus PH1-16 containing the pMJ05-sor construct are grown at 78°C and subsequently shifted to 88°C to induce the expression of the sor gene
expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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