Information on EC 1.13.11.55 - sulfur oxygenase/reductase

New: Word Map on EC 1.13.11.55
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.13.11.55
-
RECOMMENDED NAME
GeneOntology No.
sulfur oxygenase/reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 HSO3- + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
-
sulfate reduction
-
-
Sulfur metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
120598-92-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Acidianus sp.
Acidianus sp. S5
strain S5
-
-
Manually annotated by BRENDA team
gene sor
-
-
Manually annotated by BRENDA team
gene sor
-
-
Manually annotated by BRENDA team
Acidithiobacillus sp.
-
-
-
Manually annotated by BRENDA team
strain VF5
-
-
Manually annotated by BRENDA team
gene sor
UniProt
Manually annotated by BRENDA team
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 hide
LITERATURE
evolution
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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
S + O2
SO32- + S2O32- + H2S
show the reaction diagram
S + O2 + H2O
HSO3- + H2S + H+
show the reaction diagram
S + OH- + O2
HSO3- + S2O32- + HS- + H+
show the reaction diagram
-
-
-
r
sulfur + H2O + O2
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
sulfur + H2O + O2
?
show the reaction diagram
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 hide
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
Zn2+
0.01 mM or 1-2 mM in crude extracts
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
MnCl2
-
1 mM, 70C, 34.5% activity
N-ethylmaleimide
NEM
-
0.1 mM, complete
Ni2+
-
1 mM, 87.5% inhibition
NiCl2
-
1 mM, 70C, 12.5% activity
p-chloromercuribenzoic acid
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
0.05 mM, 70C, 109.3% activity; 0.05 mM, 9.3% increase of activity
glutathione
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 hide
LITERATURE
IMAGE
2 - 13
sulfur
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 2.2
sulfur
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046
Zn2+
pH 7.2, 80C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
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 hide
LITERATURE
5
Acidianus sp.
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
22
assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
10.64
-
recombinant protein
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
550000
-
gel filtration
560000
gel filtration
602000
-
nondenaturing native gel electrophoresis
732000
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexadecamer
tetradecamer
14 * 40000, SDS-PAGE
tetraeicosamer
dodecamer of dimers, modeling of the SOR and its pores, overview
tetraicosamer
additional information
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 hide
LITERATURE
45
-
Tm values are 45C and 70C
80
-
half-life: 100 min
85
-
half-life: 58 min
additional information
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 hide
LITERATURE
guanidine-HCl
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; Superdex 200 gel-filtration
-
heat treatment, DEAE-52 anion exchange and Sephadex G-200 chromatography
Acidianus sp.
-
one-step procedure over Strep-Tactin columns
-
purified by gel filtration
-
single-step purification of the proteins is obtained via fused His or Strep tags
-
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
sucrose density gradient centrifugation and preparative, non-denaturing PAGE
wild-type and recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli HB101
Acidianus sp.
-
expression in Escherichia coli
expression in Escherichia coli BL21
-
expression in Escherichia coli HB101; overexpression of wild-type and mutant enzymes in Escherichia coli
-
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 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
gene sor, expression anaysis
-
gene sor, sequence comparisons and phylogenetic analysis, expression in Escherichia coli
gene sor, sequence comparisons, expression in Escherichia coli strain BL21 Codon plus (DE3) RIL
in Escherichia coli
-
overexpressed by Escherichia coli HB 101 opon a temperature shift from 30-42C
Acidianus sp.
overexpression in Escherichia coli
-
recombinantly expressed 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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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
C31A
-
complete loss of activity; mutant with reduced 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
-
98.4% loss of activity; mutant with reduced activity
-
C104S
-
99.2% loss of activity; mutant with reduced activity
-
C31A
-
complete loss of 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
-
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
reversible denaturation curves with midpoints at 3.4 M guanidine-HCl and 5.9 M urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
industry
pharmacology
-
sulfur metabolism