Information on EC 1.13.11.55 - sulfur oxygenase/reductase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY
1.13.11.55
-
RECOMMENDED NAME
GeneOntology No.
sulfur oxygenase/reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 HSO3- + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction
-
-
Sulfur metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
sulfur:oxygen oxidoreductase (hydrogen-sulfide- and sulfite-forming)
This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Another reaction product is thiosulfate, but this is probably formed non-enzymically at elevated temperature from sulfite and sulfur [1]. This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfhydrogenase, in that both activities occur simultaneously.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOR
Acidianus ambivalens DSM 3772
;
-
SOR
Acidianus sp.
-
-
SOR
Acidianus sp.
-
SOR
Acidianus sp. S5
-
-
SOR
Acidithiobacillus caldus MTH-04
-
-
-
SOR
Halothiobacillus neapolitanus DSM15147
-
-
SOR protein
Acidianus tengchongensis, Acidithiobacillus sp.
-
-
SOR protein
-
-
-
SOR protein
-
-
sulfur oxygenase reductase
-
-
sulfur oxygenase reductase
-
sulfur oxygenase reductase
-
-
sulfur oxygenase reductase
-
sulfur oxygenase reductase
-
-
sulfur oxygenase reductase
Acidithiobacillus caldus MTH-04
-
-
-
sulfur oxygenase reductase
-
-
sulfur oxygenase reductase
-
sulfur oxygenase reductase
Halothiobacillus neapolitanus DSM15147
-
-
sulfur oxygenase reductases
Acidianus tengchongensis, Acidithiobacillus sp.
-
-
sulfur oxygenase reductases
-
-
-
sulfur oxygenase reductases
-
-
sulphur oxygenase reductase
-
sulphur oxygenase reductase
Acidianus ambivalens DSM 3772
-
-
CAS REGISTRY NUMBER
COMMENTARY
120598-92-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 3772
SwissProt
Manually annotated by BRENDA team
gene sor
SwissProt
Manually annotated by BRENDA team
strain DSM 3772
-
-
Manually annotated by BRENDA team
Acidianus ambivalens 5737
-
SwissProt
Manually annotated by BRENDA team
Acidianus ambivalens DSM 3772
-
SwissProt
Manually annotated by BRENDA team
Acidianus sp.
strain S5
SwissProt
Manually annotated by BRENDA team
Acidianus sp.
strain S5
-
-
Manually annotated by BRENDA team
Acidianus sp. S5
strain S5
SwissProt
Manually annotated by BRENDA team
Acidianus sp. S5
strain S5
-
-
Manually annotated by BRENDA team
Acidianus tengchongensis S5
strain S5
-
-
Manually annotated by BRENDA team
Acidithiobacillus caldus MTH-04
gene sor
-
-
Manually annotated by BRENDA team
Acidithiobacillus sp.
-
-
-
Manually annotated by BRENDA team
strain VF5
-
-
Manually annotated by BRENDA team
Halothiobacillus neapolitanus DSM15147
gene sor
UniProt
Manually annotated by BRENDA team
isolated from a hydrothermal vent in the Pacific Ocean, gene sor
UniProt
Manually annotated by BRENDA team
isolated from a hydrothermal vent in the Pacific Ocean, gene sor
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the SOR protein family, phylogenetic analysis, overview
evolution
Halothiobacillus neapolitanus DSM15147
-
the enzyme belongs to the SOR protein family, phylogenetic analysis, overview
-
physiological function
-
initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens
physiological function
-
catalyzes the initial step in the dissimilatory sulfur oxidation pathway
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
Acidianus ambivalens 5737
-
initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens
-
physiological function
Acidianus ambivalens DSM 3772
-
initial enzyme in the sulfur-oxidation pathway
-
physiological function
Acidithiobacillus caldus MTH-04
-
the enzyme oxidizes the cytoplasmic elemental sulfur, but cannot couple the sulfur oxidation with the electron transfer chain or substrate-level phosphorylation
-
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
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
three-dimensional modeling of the enzyme, overview
additional information
-
modeling of the sulfur oxidation system in Acidithiobacillus caldus , overview
additional information
Acidithiobacillus caldus MTH-04
-
modeling of the sulfur oxidation system in Acidithiobacillus caldus , overview
-
additional information
Halothiobacillus neapolitanus DSM15147
-
three-dimensional modeling of the enzyme, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
initial enzyme in the sulfur-oxidation pathway
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
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+
show the reaction diagram
Halothiobacillus neapolitanus DSM15147
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
Acidianus ambivalens DSM 3772
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+
show the reaction diagram
Acidianus ambivalens DSM 3772
-
initial enzyme in the sulfur-oxidation pathway
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
?
S + O2
SO32- + S2O32- + H2S
show the reaction diagram
Acidianus sp.
-
-
-
?
S + O2
SO32- + S2O32- + H2S
show the reaction diagram
Acidianus sp.
-
-
?
S + O2
SO32- + S2O32- + H2S
show the reaction diagram
Acidianus sp. S5
-
-
-
?
S + O2
SO32- + S2O32- + H2S
show the reaction diagram
Acidianus sp. S5
-
-
?
S + O2 + H2O
HSO3- + H2S + H+
show the reaction diagram
Acidianus tengchongensis, Acidianus tengchongensis S5
-
-
-
?
S + OH- + O2
HSO3- + S2O32- + HS- + H+
show the reaction diagram
-
-
r
sulfur + H2O + O2
?
show the reaction diagram
-
-
-
-
?
sulfur + H2O + O2
?
show the reaction diagram
-
initial enzyme in the sulfur oxidation pathway
-
-
?
sulfur + H2O + O2
?
show the reaction diagram
-
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
Acidithiobacillus caldus MTH-04
-
-
-
?
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
?
-
Acidianus ambivalens, Acidianus ambivalens DSM 3772
-
not active with tetrathionate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
P29082
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
D0L035
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
F8I6C7
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
-
initial enzyme in the sulfur-oxidation pathway
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
Halothiobacillus neapolitanus DSM15147
D0L035
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
Acidianus ambivalens DSM 3772
-
initial enzyme in the sulfur-oxidation pathway
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
F8I6C7
-
-
?
sulfur + H2O + O2
?
show the reaction diagram
-
initial enzyme in the sulfur oxidation pathway
-
-
?
sulfur + H2O + O2
?
show the reaction diagram
-
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
show the reaction diagram
Acidithiobacillus caldus MTH-04
-
-
-
?
additional information
?
-
-
SOR catalyzes simultaneously oxidation and reduction of elementar sulfur to produce sulfite, thiosulfate and sulfide, in the presence of molecule oxygen
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
-
iron content: 0.45 mol per mol subunit for recombinant wild-type enzyme, below 0.1 mol per mol subunit for mutant enzyme H86A, below 0.02 mol per mol subunit for mutant enzyme H90A, below 0.01 mol per mol subunit for mutant enzyme E114A, 0.02 mol per mol subunit for mutant enzyme E114D, 0.47 mol per mol subunit for mutant enzyme C31A, 0.42 mol per mol subunit for mutant enzyme C31S, 0.22 mol per mol subunit for mutant enzyme C101A, below 0.03 mol per mol subunit for mutant enzyme C101S, 0.19 mol per mol subunit for mutant enzyme C104A, 0.3 mol per mol subunit for mutant enzyme C104S, 0.56 mol per mol subunit for mutant enzyme C101A/C104A, 0.4 mol per mol subunit for mutant enzyme C101S/C104S
Fe2+
-
mononucler non-heme iron site
Fe2+
-
essential for activity, recombinant SOR had a molar ratio of 1.86:1 (iron to subunit of SOR), excesses of ferric and ferrous ions have inhibitory effect on SOR activity
Fe2+
non-heme iron. 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
Iron
-
contains iron atoms indispensable for the enzyme activity
Iron
-
the enzyme contains a low-potential mononuclear non-heme iron centre, which has a reduction potential of -268 mV at pH 6.5, one iron atom per subunit
Iron
-
low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitutes the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction
Zn2+
0.01 mM or 1-2 mM in crude extracts
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-dipyridyl
-
Fe2+-specific chelator, strong inhibition
2-iodoacetic acid
-
-
4,5-dihydroxy-meta-benzenedisulfonic acid
-
tiron, Fe3+-specific chelator, strong inhibition
4-chloromercuribenzoic acid
-
-
8-hydroxyquinoline
-
Fe3+-specific chelator, strong inhibition
Co2+
-
1 mM,89.2% inhibition
CoCl2
-
1 mM, 70C, 10.8% activity
Cu2+
-
1 mM, 99.3% inhibition
CuCl2
-
1 mM, 70C, 0.7% activity
Hg2+
blocks cysteines in the active site pocket
iodoacetic acid
blocks cysteines in the active site pocket
Mg2+
-
1 mM, 22.8% inhibition
MgCl2
-
1 mM, 70C, 77.2% activity
Mn2+
-
1 mM, 65.5% inhibition
N-ethylmaleimide
-
0.1-1 mM, 70C, 0.02-0.03% activity
N-ethylmaleimide
-
-
NEM
-
0.1 mM, complete
Ni2+
-
1 mM, 87.5% inhibition
NiCl2
-
1 mM, 70C, 12.5% activity
p-chloromercuribenzoic acid
-
Zn2+
-
1 mM, 70C, 27% activity; 1 mM, 73% inhibition
Zn2+
concentrations above 100 micromol
Zn2+
-
0.5 mM, 95% inhibition of oxygenase reaction (formation of hydrogen sulfide), 84% inhibition of reductase reaction (formation of sulfite plus thiosulfate)
Zn2+
zinc binds far from the actIve sIte , Zn2+ interferes over a distance with the subunit pores in the outer shell, possibly by restriction of protein flexibility or substrate access or product exit
MnCl2
-
1 mM, 70C, 34.5% activity
additional information
-
the enmzyme is not affected by CN-, N3-, or reduced glutathione
-
additional information
not inhibited by CN-, N2 and reduced glutathione
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
0.05 mM, 70C, 109.3% activity; 0.05 mM, 9.3% increase of activity
EDTA
-
0.05 mM, 8.8% increase of activity; 10 mM, 70C, 108.8% activity
EDTA
-
100 mM, slight stimulatory effect
glutathione
-
0.05 mM, 70C, 110% activity
glutathione
required for activity
GSH
-
0.05 mM, 10.8% increase of activity
additional information
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 3
sulfur
-
pH 7.2, 65C, oxygenase reaction (formation of hydrogen sulfide)
13
sulfur
-
pH 7.2, 65C, reductase reaction (formation of sulphite plus thiosulfate)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
sulfur
Acidianus ambivalens
-
pH 7.2, 65C, reductase reaction (formation of sulfite plus thiosulfate)
2.2
sulfur
Acidianus ambivalens
-
pH 7.2, 65C, oxygenase reaction (formation of hydrogen sulfide)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.046
Zn2+
pH 7.2, 80C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
-
mutant C101S, U/mg, reductase reaction
0.03
-
mutant E114D, U/mg, reductase reaction
0.04
-
mutant C104S, formation of sulfite plus thiosulfate, 70C
0.074
-
wild type in cellular lysate, formation of sulfite plus thiosulfate, 70C
0.08
-
mutant C101S, formation of sulfite plus thiosulfate, 70C
0.1078
-
wild type in supernatant, formation of sulfite plus thiosulfate, 70C
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, 80C
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, 70C
0.5
cytoplasm, pH 7.4, 85C, sulfur reduction
0.6
-
mutant C104S, U/mg, reductase reaction
0.64
-
mutant C101/104A, U/mg, reductase reaction
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, 80C
1.89
cytoplasm, pH 7.4, 85C, sulfur oxidation
2.28
-
mutant C104S, U/mg, oxygenase reaction
2.29
-
mutant C101/104S, U/mg, oxygenase reaction
3.28
mutant H90A, pH 8.0, 80C
3.47
mutant H86A, pH 8.0, 80C
4.19
-
wild type, U/mg, reductase reaction
4.85
-
wild type, formation of sulfite plus thiosulfate, 70C
5.46
mutant E114A, pH 8.0, 80C
8.09
mutant C104S, pH 8.0, 80C
10.6
-
pH 7.4, 85C
10.6
pH 7.4, 85C, formation of sulfite
11.52
-
wild type, U/mg, oxygenase reaction
17.17
wild-type enzyme in presence of GSH, pH 8.0, 80C
186.7
Acidianus sp.
-
formation of sulfite and thiosulfate
3100
Acidianus sp.
wild type, cell lysate, 65C, 20 mM Tris-HCl, pH 8.0, formation of H2S
3300
Acidianus sp.
wild type, cell lysate treated at 75C for 15 min, 65C, 20 mM Tris-HCl, pH 8.0, formation of H2S
6300
Acidianus sp.
Escherichia coli HB101, cell lysate, 65C, 20 mM Tris-HCl, pH 8.0, formation of H2S
28600
Acidianus sp.
wild type, cell lysate, 65C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
29700
Acidianus sp.
wild type, cell lysate treated at 75C for 15 min, 65C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
45200
Acidianus sp.
Escherichia coli HB101, cell lysate treated at 75C for 15 min, 65C, 20 mM Tris-HCl, pH 8.0, formation of H2S
75000
Acidianus sp.
Escherichia coli HB101, cell lysate, 65C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
753000
Acidianus sp.
Escherichia coli HB101, cell lysate treated at 75C for 15 min, 65C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
additional information
-
0.3% activity with 1 mM Fe3+ compared to activity without any treatment; 0% activity with 0.2 mM 2.2'-dipyridyl compared to activity without any treatment; 17.8% activity with 1.0 mM 8-hydroxyquinoline compared to activity without any treatment; 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; 21.1% activity with 0.04 mM 2.2'-dipyridyl compared to activity without any treatment; 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; 31.5% activity with 1 mM Fe2+ compared to activity without any treatment; 44% activity with 0.1 mM 8-hydroxyquinoline compared to activity without any treatment; 52.8% activity with 1.0 mM 4,5-dihydroxy-meta-benzenedisulfonic acid compared to activity without any treatment; 55% activity with 0.1 mM 4,5-dihydroxy-meta-benzenedisulfonic acid compared to activity without any treatment
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
Acidianus sp.
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 9
Acidianus sp.
-
-
5.4 - 11
activity range, recombinant enzyme, profile overview
5.5 - 8
-
the enzyme is active from pH 5.5 to 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
assay at room temperature
70
Acidianus sp.
-
-
70
Acidithiobacillus sp.
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 99
activity range, recombinant enzyme, profile overview
50 - 90
Acidianus sp.
-
-
75 - 100
-
75C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.64
-
recombinant protein
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
not detectable in anaerobically grown cells
Manually annotated by BRENDA team
Acidianus ambivalens DSM 3772
-
not detectable in anaerobically grown cells
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
; also associated with the cytoplasmic membrane
Manually annotated by BRENDA team
Acidianus ambivalens DSM 3772
-
-
-
Manually annotated by BRENDA team
Acidianus tengchongensis S5
-
; also associated with the cytoplasmic membrane
-
Manually annotated by BRENDA team
Acidithiobacillus caldus MTH-04
-
-
-
Manually annotated by BRENDA team
-
membrane-associated enzyme activity is colocalized with the activities of sulfite:acceptor oxidoreductase and thiosulfate:acceptor oxidoreductase to catalyze sulfur oxidation
-
Manually annotated by BRENDA team
Acidianus tengchongensis S5
-
membrane-associated enzyme activity is colocalized with the activities of sulfite:acceptor oxidoreductase and thiosulfate:acceptor oxidoreductase to catalyze sulfur oxidation
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
Acidianus sp.
SDS-PAGE
439600
35000
Acidianus sp.
-
SDS-PAGE
658665
35320
-
calculated from sequencing the sor gene
665355
35320
calculated from sor gene code
666952
550000
-
gel filtration
439594
560000
gel filtration
666952
602000
-
nondenaturing native gel electrophoresis
686624
732000
-
non-denaturing PAGE
724213
871000
-
-
664199
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE
?
-
x * 35000, SDS-PAGE; x * 35173, calculated from sequence
?
x * 35000, SDS-PAGE
?
Acidianus ambivalens DSM 3772
-
x * 40000, SDS-PAGE
-
?
-
x * 35000, SDS-PAGE
-
hexadecamer
16 * 35317, calculated from sor gene code
tetradecamer
14 * 40000, SDS-PAGE
tetraeicosamer
dodecamer of dimers, modeling of the SOR and its pores, overview
tetraicosamer
-
-
tetraicosamer
-
24 * 36000, SDS-PAGE
tetraicosamer
-
24 * 36000, ball-shaped assembly with a central hollow core probably consisting of 24 subunits in a 432 symmetry, the subunits form homodimers as the building blocks of the holoenzyme, SDS-PAGE
tetraicosamer
Acidianus ambivalens 5737
-
-
-
tetraicosamer
Acidianus ambivalens DSM 3772
-
24 * 36000, ball-shaped assembly with a central hollow core probably consisting of 24 subunits in a 432 symmetry, the subunits form homodimers as the building blocks of the holoenzyme, SDS-PAGE
-
hexadecamer
-
16 * 37674, calculated from nucleotide sequence; 16 * 38000, SDS-PAGE
additional information
-
24 identical SOR monomers form a hollow sphere. Within the icosatetramer sphere, the tetramer and trimer channels are proposed as the paths for the substrate and products, respectively
additional information
three-dimensional modeling of the enzyme, overview. Minimum building block is a dimer
additional information
Halothiobacillus neapolitanus DSM15147
-
three-dimensional modeling of the enzyme, overview. Minimum building block is a dimer
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion techniques
-
X-ray crystallography of SOR wild-type crystals soaked with inhibitors Hg2+ and iodoacetamide, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, crystal structure analysis
hanging drop vapor diffusion technique
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
Tm values are 45C and 70C
686624
70
-
Tm values are 45C and 70C
686624
70
Acidithiobacillus sp.
-
half-life: 37 min
724777
80
-
half-life: 100 min
724777
85
-
half-life: 58 min
724777
additional information
enzyme thermal unfolding analysis
725278
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses more than 80% of activity after three freezing and thawing steps
-
partially inactivated by freezing at -80C
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
-
reversible denaturation curve with midpoint at 3.4 M guanidine-HCl
guanidine-HCl
Acidianus ambivalens DSM 3772
-
reversible denaturation curve with midpoint at 3.4 M guanidine-HCl
-
urea
-
reversible denaturation curve with midpoints at 5.9 M urea
urea
Acidianus ambivalens DSM 3772
-
reversible denaturation curve with midpoints at 5.9 M urea
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
one-step procedure over Strep-Tactin columns
-
single-step purification of the proteins is obtained via fused His or Strep tags
-
sucrose density gradient centrifugation and preparative, non-denaturing PAGE
heat treatment, DEAE-52 anion exchange and Sephadex G-200 chromatography
Acidianus sp.
-
; Superdex 200 gel-filtration
-
purified by gel filtration
-
wild-type and recombinant enzyme
-
solubilized recombinant wild-type and mutant enzymes from Escherichia coli strain B21 inclusion bodies by nickel affinity chromatography, and refolded by a four-step dialysis
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
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
-
gene sor, sequence comparisons, expression in Escherichia coli strain BL21 Codon plus (DE3) RIL
overexpression in Escherichia coli
-
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 78C and subsequently shifted to 88C to induce the expression of the sor gene
-
expressed in Escherichia coli HB101
Acidianus sp.
-
overexpressed by Escherichia coli HB 101 opon a temperature shift from 30-42C
Acidianus sp.
expression in Escherichia coli
-
expression in Escherichia coli HB101; overexpression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild type and mutant enzyme in Escherichia coli
-
in Escherichia coli
-
gene sor, expression anaysis
-
expression in Escherichia coli
Acidithiobacillus sp.
-
recombinantly expressed in Escherichia coli
-
gene sor, sequence comparisons and phylogenetic analysis, expression in Escherichia coli
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
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C101/104A
-
enzyme with decreased specific activity
C101/104S
-
enzyme with decreased specific activity
C101A
-
enzyme with decreased specific activity; 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
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
-
enzyme with decreased specific activity and a proportional decrease in iron content; 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
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
-
enzyme with decreased specific activity; 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; 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; inactive mutant enzyme, iron content is similar to that of recombinant wild-type enzyme
C31S
-
inactive enzyme; inactive mutant enzyme, iron content is similar to that of recombinant wild-type enzyme
E114A
-
inactive enzyme with no iron incorporated; mutation results in inactive enzyme with no measurable iron found
E114D
-
enzyme with 1% of wild type activity; 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
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
-
inactive enzyme with no iron incorporated; mutation results in inactive enzyme with no measurable iron found
H90A
-
inactive enzyme with no iron incorporated; mutation results in inactive enzyme with no measurable iron found
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
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
-
98.4% loss of activity; mutant with reduced 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
-
99.2% loss of activity; mutant with reduced 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; mutant with reduced activity
C31S
-
complete loss of activity; 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
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
Acidianus tengchongensis S5
-
98.4% loss of activity; mutant with reduced activity
-
C104S
Acidianus tengchongensis S5
-
99.2% loss of activity; mutant with reduced 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
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
-
MM296/297VT
site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme
additional information
modeling of active site pore mutants based on the wild-type structure, overview
C31A
Acidianus tengchongensis S5
-
complete loss of activity
-
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
Acidithiobacillus caldus MTH-04
-
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
-
H90A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
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
H90A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
additional information
-
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
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reversible denaturation curves with midpoints at 3.4 M guanidine-HCl and 5.9 M urea
-
recombinant wild-type and mutant enzymes from Escherichia coli strain B21 inclusion bodies, purified by nickel affinity chromatography, are refolded by a four-step dialysis using 20 mM Tris/HCl, 150 mM NaCl, pH 8.14, containing 2 mM reduced glutathione, 0.02 mM oxidized glutathione, 5% glycerol, 0.005% Tween 20, and 0.1 mM ferric citrate with 6 M urea in the first step, 3 M urea in the second step, and 1 M urea in the third step
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
initial enzyme in the sulfur-oxidation pathway
pharmacology
-
sulfur metabolism
degradation
Acidianus sp.
-
enzyme in the sulfur-oxidation pathway
degradation
Acidianus sp. S5
-
enzyme in the sulfur-oxidation pathway
-
industry
-
Acidithiobacillus caldus is widely used in bio-leaching. It gains energy and electrons from oxidation of elemental sulfur and reduced inorganic sulfur compounds (RISCs) for carbon dioxide fixation and growth. Its sulfur oxidation system involves a truncated sulfur oxidation (Sox) system (omitting SoxCD), nonSox sulfur oxidation system similar to the sulfur oxidation in A. ferrooxidans, and sulfur oxygenase reductase (SOR)
industry
Acidithiobacillus caldus MTH-04
-
Acidithiobacillus caldus is widely used in bio-leaching. It gains energy and electrons from oxidation of elemental sulfur and reduced inorganic sulfur compounds (RISCs) for carbon dioxide fixation and growth. Its sulfur oxidation system involves a truncated sulfur oxidation (Sox) system (omitting SoxCD), nonSox sulfur oxidation system similar to the sulfur oxidation in A. ferrooxidans, and sulfur oxygenase reductase (SOR)
-