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Information on EC 1.13.11.55 - sulfur oxygenase/reductase and Organism(s) Acidianus ambivalens and UniProt Accession P29082

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IUBMB Comments
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. Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between sulfite and sulfur . This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfhydrogenase, in that both activities occur simultaneously.
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Acidianus ambivalens
UNIPROT: P29082
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Word Map
The taxonomic range for the selected organisms is: Acidianus ambivalens
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
sulfur oxygenase reductase, tpsor, sor protein, sulfur oxygenase/reductase, sor-at, aasor, sulphur oxygenase reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur oxygenase reductase
-
sulphur oxygenase reductase
-
sulfur oxygenase reductase
-
-
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. Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between 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
-
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 + OH- + O2
HSO3- + S2O32- + HS- + H+
show the reaction diagram
-
-
-
r
sulfur + H2O + O2
?
show the reaction diagram
initial enzyme in the sulfur oxidation pathway
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
sulfur + H2O + O2
?
show the reaction diagram
initial enzyme in the sulfur oxidation pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
0.01 mM or 1-2 mM in crude extracts
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-iodoacetic acid
-
4-chloromercuribenzoic acid
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Hg2+
blocks cysteines in the active site pocket
iodoacetic acid
blocks cysteines in the active site pocket
p-chloromercuribenzoic acid
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
100 mM, slight stimulatory effect
additional information
-
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
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
0.11
mutant E114D, U/mg, oxygenase reaction
0.12
mutant C101S, U/mg, oxygenase reaction
0.23
mutant C104A, U/mg, reductase reaction
0.43
mutant C101A, U/mg, reductase reaction
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
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
1.89
cytoplasm, pH 7.4, 85°C, sulfur oxidation
11.52
wild type, U/mg, oxygenase reaction
2.28
mutant C104S, U/mg, oxygenase reaction
2.29
mutant C101/104S, U/mg, oxygenase reaction
4.19
wild type, U/mg, reductase reaction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75 - 100
75°C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.64
-
recombinant protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
not detectable in anaerobically grown cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SOR_ACIAM
309
0
35318
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35317
16 * 35317, calculated from sor gene code
35320
calculated from sor gene code
36000
40000
550000
gel filtration
560000
gel filtration
732000
non-denaturing PAGE
35320
-
calculated from sequencing the sor gene
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, 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
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
PROTEIN VARIANTS
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
C101S
enzyme with decreased specific activity and a proportional decrease in iron content
C104A
enzyme with decreased specific activity
C104S
enzyme with decreased specific activity
C31A
inactive enzyme
C31S
inactive enzyme
E114A
inactive enzyme with no iron incorporated
E114D
enzyme with 1% of wild type activity
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
H90A
inactive enzyme with no iron incorporated
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
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
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
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
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
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses more than 80% of activity after three freezing and thawing steps
partially inactivated by freezing at -80°C
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
reversible denaturation curve with midpoint at 3.4 M guanidine-HCl
urea
reversible denaturation curve with midpoints at 5.9 M urea
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 78°C and subsequently shifted to 88°C to induce the expression of the sor gene
expression in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reversible denaturation curves with midpoints at 3.4 M guanidine-HCl and 5.9 M urea
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
initial enzyme in the sulfur-oxidation pathway
pharmacology
-
sulfur metabolism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kletzin, A.
Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens
J. Bacteriol.
171
1638-1643
1989
Acidianus ambivalens (P29082), Acidianus ambivalens, Acidianus ambivalens DSM 3772 (P29082)
Manually annotated by BRENDA team
Urich, T.; Coelho, R.; Kletzin, A.; Frazao, C.
The sulfur oxygenase reductase from Acidianus ambivalens is an icosatetramer as shown by crystallization and Patterson analysis
Biochim. Biophys. Acta
1747
267-270
2005
Acidianus ambivalens (P29082), Acidianus ambivalens, Acidianus ambivalens 5737 (P29082)
Manually annotated by BRENDA team
Urich, T.; Kroke, A.; Bauer, C.; Seyfarth, K.; Reuff, M.; Kletzin, A.
Identification of core active site residues of the sulfur oxygenase reductase from Acidianus ambivalens by site-directed mutagenesis
FEMS Microbiol. Lett.
248
171-176
2005
Acidianus ambivalens, Acidianus ambivalens (P29082)
Manually annotated by BRENDA team
Kletzin, A.
Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens
J. Bacteriol.
174
5854-5859
1992
Acidianus ambivalens
Manually annotated by BRENDA team
Kletzin, A.
Sulfur oxidation and reduction in Archaea: Sulfur oxygenase/-reductase and hydrogenases from the extremely thermophilic and facultatively anaerobic archaeon Desulfurolobus ambivalens
Syst. Appl. Microbiol.
16
534-543
1994
Acidianus ambivalens (P29082)
-
Manually annotated by BRENDA team
Albers, S.V.; Jonuscheit, M.; Dinkelaker, S.; Urich, T.; Kletzin, A.; Tamp, R.; Driessen, A.J.; Schleper, C.
Production of recombinant and tagged proteins in the hyperthermophilic archaeon Sulfolobus solfataricus
Appl. Environ. Microbiol.
72
102-111
2006
Acidianus ambivalens (P29082), Acidianus ambivalens
Manually annotated by BRENDA team
Urich, T.; Bandeiras, T.M.; Leal, S.S.; Rachel, R.; Albrecht, T.; Zimmermann, P.; Scholz, C.; Teixeira, M.; Gomes, C.M.; Kletzin, A.
The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre
Biochem. J.
381
137-146
2004
Acidianus ambivalens (P29082), Acidianus ambivalens, Acidianus ambivalens DSM 3772 (P29082)
Manually annotated by BRENDA team
Veith, A.; Urich, T.; Seyfarth, K.; Protze, J.; Frazao, C.; Kletzin, A.
Substrate pathways and mechanisms of inhibition in the sulfur oxygenase reductase of Acidianus ambivalens
Front. Microbiol.
2
37
2011
Acidianus ambivalens (P29082), Acidianus ambivalens
Manually annotated by BRENDA team
Urich, T.; Gomes, C.M.; Kletzin, A.; Frazao, C.
X-ray structure of a self-compartmentalizing sulfur cycle metalloenzyme
Science
311
996-1000
2006
Acidianus ambivalens (P29082), Acidianus ambivalens
Manually annotated by BRENDA team