Information on EC 1.13.11.18 - sulfur dioxygenase

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

EC NUMBER
COMMENTARY
1.13.11.18
-
RECOMMENDED NAME
GeneOntology No.
sulfur dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glutathione + sulfur = S-sulfanylglutathione
show the reaction diagram
(1a)
-
-
-
S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+
show the reaction diagram
(1b)
-
-
-
sulfur + O2 + H2O = sulfite + 2 H+
show the reaction diagram
overall reaction
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
Sulfur metabolism
-
SYSTEMATIC NAME
IUBMB Comments
S-sulfanylglutathione:oxygen oxidoreductase
An iron protein. Glutathione (GSH) plays a catalytic role in elemental sulfur activation, but is not consumed during the enzymic reaction. GSH and elemental sulfur react non-enzymically to yield S-sulfanylglutathione and it is only in this form that the sulfur can be oxidized to yield sulfite. The sulfite can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ETHE1
Q9C8L4
gene name
SDO
Acidithiobacillus ferrooxidans R1
-
-
-
SOR
Acidianus sp.
-
-
SOR
Acidianus sp. S5
-
-
-
sulfur dioxygenase
Q9C8L4
-
sulfur oxygenase
-
-
-
-
sulfur oxygenase/reductase
Acidianus sp.
-
-
sulfur oxygenase/reductase
Acidianus sp. S5
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37256-58-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acidianus sp.
strain S5
-
-
Manually annotated by BRENDA team
Acidianus sp. S5
strain S5
-
-
Manually annotated by BRENDA team
strain DSM 700
-
-
Manually annotated by BRENDA team
Acidithiobacillus ferrooxidans R1
strain R1
-
-
Manually annotated by BRENDA team
Acidithiobacillus thiooxidans NB1-3
strain NB1-3
-
-
Manually annotated by BRENDA team
gene ethe1
UniProt
Manually annotated by BRENDA team
strains N1 and SSO, in strain N1 increase of activity under microaerobic conditions, in strain SSO decrease of activity under micoaerobic conditions
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
ethylmalonic encephalopathy is caused by mutations in the mitochondrial matrix sulfur dioxygenase ETHE1 leading to failure to detoxify sulfide, a product of intestinal anaerobes and, in trace amounts, tissues
malfunction
Q9C8L4
seeds homozygous for a DNA insertion in ETHE1 exhibit alterations in endosperm development that are accompanied by a delay in embryo development followed by embryo arrest by early heart stage
physiological function
Q9C8L4
ETHE1 appears to play an essential role in regulating sulfide levels in seeds, it is essential for early seed development
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
show the reaction diagram
Acidianus sp.
-
-, incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
-
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
-
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
S2O32- may be formed through a secondary, non-enzymatic reaction
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
low amount of thiosulfate observed may result from a chemical reaction between sulfite and elemental sulfur
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
incorporation of elemental sulfur
-
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
Acidithiobacillus ferrooxidans R1
-
-, incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
Acidithiobacillus thiooxidans NB1-3
-
-
-
-
sulfur + O2 + H2O
thiosulfate
show the reaction diagram
-
-
in the presence of reduced glutathione and 2,2'-dipyridyl
-
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
show the reaction diagram
Acidianus sp. S5
-
-, incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
-
-
?
additional information
?
-
Q9C8L4
Arabidopsis ETHE1 catalyzes the glutathione persulfide-dependent consumption of oxygen
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
-
-
ir
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
incorporation of elemental sulfur
-
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
-
incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
-
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
show the reaction diagram
Acidianus sp., Acidianus sp. S5
-
incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
-
-
?
additional information
?
-
Q9C8L4
Arabidopsis ETHE1 catalyzes the glutathione persulfide-dependent consumption of oxygen
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Non-heme iron
-
0.000087 mmol of iron per mg of enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
diethyldithiocarbamate
-
-
H2O2
-
strong inhibition, reversible by subsequent addition of catalase and glutathione
Ni2+
-
3 mM, 91% inhibition, 10 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
similar stimulating effect as 2,2' dipyridyl
2,2'-dipyridyl
-
stimulation at low concentrations e.g. 0.1 mM, may protect glutathione from destruction
glutathione
-
reduced from
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.3
-
glutathione
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000352
-
-
activity in extracts of aerobic grown cells
0.000952
-
-
activity in extracts of anaerobic grown cells
7.95
-
Q9C8L4
recombinant enzyme, pH and temperature not specified in the publication
186.7
-
Acidianus sp.
-
purified enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
Acidianus sp.
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
6
Acidianus sp.
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65
-
-
no activity above
70
-
Acidianus sp.
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
80
Acidianus sp.
-
-
50
-
-
not active below
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q9C8L4
strong ETHE1 expression occurs in the peripheral and chalazal endosperm of wild-type seeds prior to cellularization
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acidithiobacillus ferrooxidans R1
-
-
-
-
Manually annotated by BRENDA team
additional information
Q9C8L4
no activity in the cytosol
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
-
Acidianus sp.
-
SDS-PAGE
560000
-
-
non denaturating PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 35000, SDS-PAGE
dimer
Acidithiobacillus ferrooxidans R1
-
-
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2,2'-dipyridyl stabilizes cofactor glutathione, activity is lost upon freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, DEAE-cellulose fraction, 7 d, almost complete loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein
Acidianus sp.
-
recombinant enzyme from Escherichia coli
Q9C8L4
30% ethanol, DEAE-cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli HB101
Acidianus sp.
-
gene ethe1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression in Escherichia coli
Q9C8L4
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L55P
-
the mutation is associated with ethylmalonic encephalopathy
additional information
Q9C8L4
generation of a ETHE1 loss-of-function mutation by DNA insertion, phenotpe overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
the combined oral treatment with metronidazole and N-acetylcysteine is an effective therapy for ethylmalonic encephalopathy which is caused by mutations in the mitochondrial matrix sulfur dioxygenase ETHE1