1.13.11.55: sulfur oxygenase/reductase
This is an abbreviated version!
For detailed information about sulfur oxygenase/reductase, go to the full flat file.
Word Map on EC 1.13.11.55
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1.13.11.55
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ambivalens
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thiosulfate
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acidianus
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thermoacidophilic
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hollow
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non-heme
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disproportionation
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acidithiobacillus
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acidophil
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sulfobacillus
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tetrathionate
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tokodaii
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heterodisulfide
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bioleaching
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degradation
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low-potential
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caldus
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pharmacology
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industry
- 1.13.11.55
- ambivalens
- thiosulfate
- acidianus
-
thermoacidophilic
-
hollow
-
non-heme
-
disproportionation
- acidithiobacillus
-
acidophil
- sulfobacillus
- tetrathionate
- tokodaii
-
heterodisulfide
-
bioleaching
- degradation
-
low-potential
- caldus
- pharmacology
- industry
Reaction
4 sulfur
+
4 H2O
+
Synonyms
AaSOR, SAMN00768000_1627, SAMN00768000_1798, SOR, SOR protein, SOR-AT, sulfur oxygenase, sulfur oxygenase reductase, sulfuroxygenasereductase, sulphur oxygenase reductase, TpSOR, TPY_0405
ECTree
1.13.11.55 sulfur oxygenase/reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.13.11.55 - sulfur oxygenase/reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C101A
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
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
C104A
C104S
C31A
C31S
E114A
E114D
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
H86A
H90A
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
C101S
C104S
C31A
C31S
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
C101S
C104S
C31A
C101S
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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
E114A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H86A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H90A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
C101S
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site-directed mutagenesis, 10% reamining activity compared to the wild-type enzyme
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C104S
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site-directed mutagenesis, 47% reamining activity compared to the wild-type enzyme
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H86A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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H90A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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C101A
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about 10% residual activtiy for both oxygenase and reductase activity
C104A
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about 10% residual activtiy for both oxygenase and reductase activity
additional information
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
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
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 mutant enzyme, iron content is similar to that of recombinant wild-type enzyme
C31S
inactive mutant enzyme, iron content is similar to that of recombinant wild-type enzyme
E114A
mutation results in inactive enzyme with no measurable iron found
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
mutation results in inactive enzyme with no measurable iron found
H90A
mutation results in inactive enzyme with no measurable iron found
C101S
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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
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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
C31S
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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
additional information
modeling of active site pore mutants based on the wild-type structure, overview
additional information
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modeling of active site pore mutants based on the wild-type structure, 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
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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