Information on EC 1.13.11.18 - persulfide dioxygenase

for references in articles please use BRENDA:EC1.13.11.18
Word Map on EC 1.13.11.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

EC NUMBER
COMMENTARY hide
1.13.11.18
-
RECOMMENDED NAME
GeneOntology No.
persulfide dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+
show the reaction diagram
overall reaction
-
-
-
S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
show the reaction diagram
(1a)
-
-
-
S-sulfinatoglutathione + H2O = glutathione + sulfite + H+
show the reaction diagram
(1b), spontaneous
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction
-
-
Sulfur metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
S-sulfanylglutathione:oxygen oxidoreductase
An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
CAS REGISTRY NUMBER
COMMENTARY hide
37256-58-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain DSM 700
-
-
Manually annotated by BRENDA team
gene ethe1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
-
residue Cys314, located in the rhodanese-active site, is captured in its persulfidated Cys-SSH form. The PDO-active site is located at the bottom of a large pocket framed on one side by a positively charged ridge comprising residues Arg193-Lys216 and by Tyr176 on the other
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
bacillithiol persulfide + O2
bacillithiol + sulfite
show the reaction diagram
-
-
-
?
CoASSH + O2
CoA + sulfite
show the reaction diagram
-
-
-
?
S-sulfanyl-L-cysteine + O2
L-cysteine + sulfite
show the reaction diagram
-
-
-
?
S-sulfanylglutathione + O2
glutathione + sulfite
show the reaction diagram
-
-
-
?
S-sulfanylglutathione + O2
sulfite + glutathione + H+
show the reaction diagram
-
-
-
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
sulfur + O2 + H2O
thiosulfate
show the reaction diagram
-
-
in the presence of reduced glutathione and 2,2'-dipyridyl
-
?
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
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
show the reaction diagram
S-sulfanylglutathione + O2
sulfite + glutathione + H+
show the reaction diagram
-
-
-
-
?
sulfur + O2 + H2O
sulfite
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Non-heme iron
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyldithiocarbamate
-
-
DTT
23% inhibition at 1 mM
H2O2
-
strong inhibition, reversible by subsequent addition of catalase and glutathione
sulfite
-
sulfite build up can potentially inhibit PDO activity
additional information
-
no effect by thiosulfate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
ascorbate
-
addition of 2.5 mM ascorbate to the standard assay results in an 20% increase in the PDO-specific activity
DTT
9% activation at 1 mM
glutathione
GSH
-
GSH is slightly activating by about 1.3fold
additional information
-
no effect by thiosulfate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018
bacillithiol persulfide
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
0.0011
CoASSH
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
6.3
glutathione
-
-
0.13
O2
-
recombinant wild-type enzyme, pH 7.4, 22C
0.02
S-sulfanyl-L-cysteine
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
-
0.0078 - 0.07
S-sulfanylglutathione
50
sulfur
-
-
additional information
additional information
-
kinetics of sulfur-transfer reaction
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.7
bacillithiol persulfide
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
19.3
CoASSH
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
143
O2
-
recombinant wild-type enzyme, pH 7.4, 22C
2 - 8
S-sulfanyl-L-cysteine
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
-
5 - 143
S-sulfanylglutathione
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10944
bacillithiol persulfide
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
17545
CoASSH
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
1100
O2
-
recombinant wild-type enzyme, pH 7.4, 22C
1400
S-sulfanyl-L-cysteine
recombinant wild-type enzyme CstB, pH 6.0, 25C, coupled persulfide dioxygenase-persulfide transferase activity
-
14 - 2043
S-sulfanylglutathione
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000352
-
activity in extracts of aerobic grown cells
0.000952
-
activity in extracts of anaerobic grown cells
7.95
recombinant enzyme, pH and temperature not specified in the publication
186.7
-
purified enzyme
1484
purified recombinant enzyme, pH 6.5, 35C
2336
purified recombinant enzyme, pH 8.0, 45C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
coupled persulfide dioxygenase-persulfide transferase activity assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
-
6.5 - 9.6
activity range, recombinant enzyme
7.6 - 8.6
activity range, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
no activity above
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
optimal activity at 35C, more than 88%of its maximum activity between 20C and 37C. Very limited SDO activity is detected at 50C or above
50
-
not active below
50 - 80
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.43
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest enzyme activity
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
strong ETHE1 expression occurs in the peripheral and chalazal endosperm of wild-type seeds prior to cellularization
Manually annotated by BRENDA team
additional information
-
immunohistochemic analysis, the SDO protein is mainly located in epithelial tissue while there are few positive signals in the connective tissue and muscle in all four organs
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
B2TEQ2
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
B2TEQ2
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
B2TEQ2
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
gel filtration, recombinant wild-type enzyme
226000
recombinant full-length Fe(II)-loaded wild-type CstB, gel filtration
298000
recombinant full-length Fe(II)-loaded CstB mutant C408S, gel filtration
560000
-
non denaturating PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 41500, about, sequence calculation
tetramer
4 * 49276, wild-type enzyme, mass spectrometry, 4 * 49277, sequence calculation
additional information
enzyme CstB is predicted to be a three-domain enzyme containing an N-terminal metallo-beta-lactamase-like (MBL), non-heme Fe(II)-containing PDO domain, followed by a pseudo-rhodanese homology (RHD) domain, and a conventional C-terminal rhodanese (Rhod) domain
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type PRF and sulfurtransferase-inactivated C314S mutant with and without glutathione, X-ray diffraction structure determination and analysis at 1.8 A, 2.4 A, and 2.7 A resolution,respectively
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
the Tm value for the isolated rhodanese domain (55C) is slightly higher than for wild-type (50C) and the enzyme mutant C314S (51.6C)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2,2'-dipyridyl stabilizes cofactor glutathione, activity is lost upon freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, DEAE-cellulose fraction, 7 d, almost complete loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
30% ethanol, DEAE-cellulose
-
recombinant enzyme from Escherichia coli
recombinant protein
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli HB101
-
gene cst, CstB is encoded by the cst operon and is under the transcriptional control of the persulfide sensor CstR and H2S, recombinant expression of full-length wild-type and mutant enzymes and of the N-terminal PDO-RHD domain in Escherichia coli strain Rosetta (DE3)
gene ethe1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression in Escherichia coli
gene sdo, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis, recombinant overexpression in Escherichia coli strain BL21(DE3)
quantitative real-time RT-PCR enzyme expression analysis
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene cstB is encoded in the cst operon and is under the transcriptional control of the persulfide sensor CstR and H2S
the enzyme is induced by sulfide in the hindgut, about 2fold after 72 h, but not in the midgut
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L55P
-
the mutation is associated with ethylmalonic encephalopathy
C314S
-
site-directed mutagenesis, structure comparison with wild-type enzyme. C314S BpPRF exhibits a 29fold lower kcat and an 5fold higher Km for GSSH than the wild-type
C201S
site-directed mutagenesis, the mutant protein structure is similar to the wild-type, but it shows reduced activity
C201S/C408S
site-directed mutagenesis
C2S
site-directed mutagenesis, the mutant is larger than the wild-type and is a hexamer
C408S
site-directed mutagenesis, the mutant is larger than the wild-type and is a hexamer. Substitution of the presumed Rhod active-site C408 also appears to destabilize the native protein fold. Catalytically inactive mutant
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and cleavage of the His-tag by TEV protease, followed by another step of nickel affinity chromatography, and gel filtration to over 95% purity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine